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Lysozyme Human/ 重组人溶菌酶
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Lysozyme Human/ 重组人溶菌酶
产品编号：ENZ-362
产品规格：10mg/1g/10g
Synonyms Lysozyme C, EC 3.2.1.17, LYZ, LZM, 1,4-beta-N-acetylmuramidase C, Lysozyme. Introduction Lysozyme is an enzyme found in egg white, tears, ａnd other secretions. Lysozyme is responsible for attacking & breaking down the polysaccharide walls of many kinds of bacteria ａnd thus it provides some protection against infection. Bacteria build a tough skin of carbohydrate chains, interlocked by short peptide strands, that braces their delicate membrane against the cell＇s high osmotic pressure. Lysozyme breaks these carbohydrate chains, destroying the structural integrity of the cell wall. The bacteria burst under their own internal pressure. Lysozyme （muramidase） hydrolyzes preferentially the ?-1,4 glucosidic linkages between N-acetylmuramic acid ａnd N-acetylglucosamine which occur in the mucopeptide cell wall. Lysozyme is a mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. Cartilage lysozyme has a role in cartilage calcification. Presence of the Lysozyme in cerebrospinal fluid is indicative of tumor of the central nervous system, normally lysozyme activity is practically absent from urine, bile ａnd spinal fluid. Description Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5 mg/ml （7,000⁻⁷0,000 U/ml）.
Recombinant Human Lysozyme produced in Plant is a single, non-glycosilated polypeptide chain containing 130 amino acids ａnd a molecular mass of 14 kDa. Source Rice Grain. Physical Appearance Sterile Filtered white lyophilized powder. Formulation The Recombinant Lysozyme was lyophilized with no additives. Stability Recombinant Lysozyme although stable at room temperature for 3 weeks, should be stored at 2-8°C. Purity Greater than 90% as determined by both: （a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. Activity 136,227 Units/mg protein. 1 unit will produce a change of A450 0.001 per minute at pH-6.24 ａnd 25°C, using a suspension of micrococcus lysodeikticus as substrate in a 2.6ml reaction volume. Instructions for Use Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5mg/ml （7,000⁻⁷0,000 U/ml）. The common extraction buffer for E. coli cells contains 0.2mg/ml of recombinant Lysozyme in 100mM Tris-HCl, 2mM EDTA, 0.05% Triton X-100, pH 8. The cell paste is suspended in extraction buffer ａnd incubated for at least 15 min at room temperature. alternatively, Triton X-100 at 1% ａnd PMSF at 1mM can be added separately ａnd the lysis solution is further incubated for at least 15 min at 37 °C. The lysed cell suspension is clarified by centrifugation at 20,000g for at least 15 min. The extraction conditions ａnd concentration of the Recombinant Human Lysozyme needed for optimal cell lysis ａnd protein recovery depends on various factors ａnd has to be determined empirically. Usage Prospec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Lysozyme Human/ 重组人溶菌酶
产品编号：ENZ-362
产品规格：10mg/1g/10g
Synonyms Lysozyme C, EC 3.2.1.17, LYZ, LZM, 1,4-beta-N-acetylmuramidase C, Lysozyme. Introduction Lysozyme is an enzyme found in egg white, tears, ａnd other secretions. Lysozyme is responsible for attacking & breaking down the polysaccharide walls of many kinds of bacteria ａnd thus it provides some protection against infection. Bacteria build a tough skin of carbohydrate chains, interlocked by short peptide strands, that braces their delicate membrane against the cell＇s high osmotic pressure. Lysozyme breaks these carbohydrate chains, destroying the structural integrity of the cell wall. The bacteria burst under their own internal pressure. Lysozyme （muramidase） hydrolyzes preferentially the ?-1,4 glucosidic linkages between N-acetylmuramic acid ａnd N-acetylglucosamine which occur in the mucopeptide cell wall. Lysozyme is a mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. Cartilage lysozyme has a role in cartilage calcification. Presence of the Lysozyme in cerebrospinal fluid is indicative of tumor of the central nervous system, normally lysozyme activity is practically absent from urine, bile ａnd spinal fluid. Description Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5 mg/ml （7,000⁻⁷0,000 U/ml）.
Recombinant Human Lysozyme produced in Plant is a single, non-glycosilated polypeptide chain containing 130 amino acids ａnd a molecular mass of 14 kDa. Source Rice Grain. Physical Appearance Sterile Filtered white lyophilized powder. Formulation The Recombinant Lysozyme was lyophilized with no additives. Stability Recombinant Lysozyme although stable at room temperature for 3 weeks, should be stored at 2-8°C. Purity Greater than 90% as determined by both: （a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. Activity 136,227 Units/mg protein. 1 unit will produce a change of A450 0.001 per minute at pH-6.24 ａnd 25°C, using a suspension of micrococcus lysodeikticus as substrate in a 2.6ml reaction volume. Instructions for Use Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5mg/ml （7,000⁻⁷0,000 U/ml）. The common extraction buffer for E. coli cells contains 0.2mg/ml of recombinant Lysozyme in 100mM Tris-HCl, 2mM EDTA, 0.05% Triton X-100, pH 8. The cell paste is suspended in extraction buffer ａnd incubated for at least 15 min at room temperature. alternatively, Triton X-100 at 1% ａnd PMSF at 1mM can be added separately ａnd the lysis solution is further incubated for at least 15 min at 37 °C. The lysed cell suspension is clarified by centrifugation at 20,000g for at least 15 min. The extraction conditions ａnd concentration of the Recombinant Human Lysozyme needed for optimal cell lysis ａnd protein recovery depends on various factors ａnd has to be determined empirically. Usage Prospec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Lysozyme Human/ 重组人溶菌酶
产品编号：ENZ-362
产品规格：10mg/1g/10g
Synonyms Lysozyme C, EC 3.2.1.17, LYZ, LZM, 1,4-beta-N-acetylmuramidase C, Lysozyme. Introduction Lysozyme is an enzyme found in egg white, tears, ａnd other secretions. Lysozyme is responsible for attacking & breaking down the polysaccharide walls of many kinds of bacteria ａnd thus it provides some protection against infection. Bacteria build a tough skin of carbohydrate chains, interlocked by short peptide strands, that braces their delicate membrane against the cell＇s high osmotic pressure. Lysozyme breaks these carbohydrate chains, destroying the structural integrity of the cell wall. The bacteria burst under their own internal pressure. Lysozyme （muramidase） hydrolyzes preferentially the ?-1,4 glucosidic linkages between N-acetylmuramic acid ａnd N-acetylglucosamine which occur in the mucopeptide cell wall. Lysozyme is a mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. Cartilage lysozyme has a role in cartilage calcification. Presence of the Lysozyme in cerebrospinal fluid is indicative of tumor of the central nervous system, normally lysozyme activity is practically absent from urine, bile ａnd spinal fluid. Description Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5 mg/ml （7,000⁻⁷0,000 U/ml）.
Recombinant Human Lysozyme produced in Plant is a single, non-glycosilated polypeptide chain containing 130 amino acids ａnd a molecular mass of 14 kDa. Source Rice Grain. Physical Appearance Sterile Filtered white lyophilized powder. Formulation The Recombinant Lysozyme was lyophilized with no additives. Stability Recombinant Lysozyme although stable at room temperature for 3 weeks, should be stored at 2-8°C. Purity Greater than 90% as determined by both: （a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. Activity 136,227 Units/mg protein. 1 unit will produce a change of A450 0.001 per minute at pH-6.24 ａnd 25°C, using a suspension of micrococcus lysodeikticus as substrate in a 2.6ml reaction volume. Instructions for Use Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5mg/ml （7,000⁻⁷0,000 U/ml）. The common extraction buffer for E. coli cells contains 0.2mg/ml of recombinant Lysozyme in 100mM Tris-HCl, 2mM EDTA, 0.05% Triton X-100, pH 8. The cell paste is suspended in extraction buffer ａnd incubated for at least 15 min at room temperature. alternatively, Triton X-100 at 1% ａnd PMSF at 1mM can be added separately ａnd the lysis solution is further incubated for at least 15 min at 37 °C. The lysed cell suspension is clarified by centrifugation at 20,000g for at least 15 min. The extraction conditions ａnd concentration of the Recombinant Human Lysozyme needed for optimal cell lysis ａnd protein recovery depends on various factors ａnd has to be determined empirically. Usage Prospec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Lysozyme Human/ 重组人溶菌酶
产品编号：ENZ-362
产品规格：10mg/1g/10g
Synonyms Lysozyme C, EC 3.2.1.17, LYZ, LZM, 1,4-beta-N-acetylmuramidase C, Lysozyme. Introduction Lysozyme is an enzyme found in egg white, tears, ａnd other secretions. Lysozyme is responsible for attacking & breaking down the polysaccharide walls of many kinds of bacteria ａnd thus it provides some protection against infection. Bacteria build a tough skin of carbohydrate chains, interlocked by short peptide strands, that braces their delicate membrane against the cell＇s high osmotic pressure. Lysozyme breaks these carbohydrate chains, destroying the structural integrity of the cell wall. The bacteria burst under their own internal pressure. Lysozyme （muramidase） hydrolyzes preferentially the ?-1,4 glucosidic linkages between N-acetylmuramic acid ａnd N-acetylglucosamine which occur in the mucopeptide cell wall. Lysozyme is a mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. Cartilage lysozyme has a role in cartilage calcification. Presence of the Lysozyme in cerebrospinal fluid is indicative of tumor of the central nervous system, normally lysozyme activity is practically absent from urine, bile ａnd spinal fluid. Description Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5 mg/ml （7,000⁻⁷0,000 U/ml）.
Recombinant Human Lysozyme produced in Plant is a single, non-glycosilated polypeptide chain containing 130 amino acids ａnd a molecular mass of 14 kDa. Source Rice Grain. Physical Appearance Sterile Filtered white lyophilized powder. Formulation The Recombinant Lysozyme was lyophilized with no additives. Stability Recombinant Lysozyme although stable at room temperature for 3 weeks, should be stored at 2-8°C. Purity Greater than 90% as determined by both: （a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. Activity 136,227 Units/mg protein. 1 unit will produce a change of A450 0.001 per minute at pH-6.24 ａnd 25°C, using a suspension of micrococcus lysodeikticus as substrate in a 2.6ml reaction volume. Instructions for Use Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5mg/ml （7,000⁻⁷0,000 U/ml）. The common extraction buffer for E. coli cells contains 0.2mg/ml of recombinant Lysozyme in 100mM Tris-HCl, 2mM EDTA, 0.05% Triton X-100, pH 8. The cell paste is suspended in extraction buffer ａnd incubated for at least 15 min at room temperature. alternatively, Triton X-100 at 1% ａnd PMSF at 1mM can be added separately ａnd the lysis solution is further incubated for at least 15 min at 37 °C. The lysed cell suspension is clarified by centrifugation at 20,000g for at least 15 min. The extraction conditions ａnd concentration of the Recombinant Human Lysozyme needed for optimal cell lysis ａnd protein recovery depends on various factors ａnd has to be determined empirically. Usage Prospec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Lysozyme Human/ 重组人溶菌酶
产品编号：ENZ-362
产品规格：10mg/1g/10g
Synonyms Lysozyme C, EC 3.2.1.17, LYZ, LZM, 1,4-beta-N-acetylmuramidase C, Lysozyme. Introduction Lysozyme is an enzyme found in egg white, tears, ａnd other secretions. Lysozyme is responsible for attacking & breaking down the polysaccharide walls of many kinds of bacteria ａnd thus it provides some protection against infection. Bacteria build a tough skin of carbohydrate chains, interlocked by short peptide strands, that braces their delicate membrane against the cell＇s high osmotic pressure. Lysozyme breaks these carbohydrate chains, destroying the structural integrity of the cell wall. The bacteria burst under their own internal pressure. Lysozyme （muramidase） hydrolyzes preferentially the ?-1,4 glucosidic linkages between N-acetylmuramic acid ａnd N-acetylglucosamine which occur in the mucopeptide cell wall. Lysozyme is a mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. Cartilage lysozyme has a role in cartilage calcification. Presence of the Lysozyme in cerebrospinal fluid is indicative of tumor of the central nervous system, normally lysozyme activity is practically absent from urine, bile ａnd spinal fluid. Description Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5 mg/ml （7,000⁻⁷0,000 U/ml）.
Recombinant Human Lysozyme produced in Plant is a single, non-glycosilated polypeptide chain containing 130 amino acids ａnd a molecular mass of 14 kDa. Source Rice Grain. Physical Appearance Sterile Filtered white lyophilized powder. Formulation The Recombinant Lysozyme was lyophilized with no additives. Stability Recombinant Lysozyme although stable at room temperature for 3 weeks, should be stored at 2-8°C. Purity Greater than 90% as determined by both: （a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. Activity 136,227 Units/mg protein. 1 unit will produce a change of A450 0.001 per minute at pH-6.24 ａnd 25°C, using a suspension of micrococcus lysodeikticus as substrate in a 2.6ml reaction volume. Instructions for Use Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5mg/ml （7,000⁻⁷0,000 U/ml）. The common extraction buffer for E. coli cells contains 0.2mg/ml of recombinant Lysozyme in 100mM Tris-HCl, 2mM EDTA, 0.05% Triton X-100, pH 8. The cell paste is suspended in extraction buffer ａnd incubated for at least 15 min at room temperature. alternatively, Triton X-100 at 1% ａnd PMSF at 1mM can be added separately ａnd the lysis solution is further incubated for at least 15 min at 37 °C. The lysed cell suspension is clarified by centrifugation at 20,000g for at least 15 min. The extraction conditions ａnd concentration of the Recombinant Human Lysozyme needed for optimal cell lysis ａnd protein recovery depends on various factors ａnd has to be determined empirically. Usage Prospec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Lysozyme Human/ 重组人溶菌酶
产品编号：ENZ-362
产品规格：10mg/1g/10g
Synonyms Lysozyme C, EC 3.2.1.17, LYZ, LZM, 1,4-beta-N-acetylmuramidase C, Lysozyme. Introduction Lysozyme is an enzyme found in egg white, tears, ａnd other secretions. Lysozyme is responsible for attacking & breaking down the polysaccharide walls of many kinds of bacteria ａnd thus it provides some protection against infection. Bacteria build a tough skin of carbohydrate chains, interlocked by short peptide strands, that braces their delicate membrane against the cell＇s high osmotic pressure. Lysozyme breaks these carbohydrate chains, destroying the structural integrity of the cell wall. The bacteria burst under their own internal pressure. Lysozyme （muramidase） hydrolyzes preferentially the ?-1,4 glucosidic linkages between N-acetylmuramic acid ａnd N-acetylglucosamine which occur in the mucopeptide cell wall. Lysozyme is a mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. Cartilage lysozyme has a role in cartilage calcification. Presence of the Lysozyme in cerebrospinal fluid is indicative of tumor of the central nervous system, normally lysozyme activity is practically absent from urine, bile ａnd spinal fluid. Description Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5 mg/ml （7,000⁻⁷0,000 U/ml）.
Recombinant Human Lysozyme produced in Plant is a single, non-glycosilated polypeptide chain containing 130 amino acids ａnd a molecular mass of 14 kDa. Source Rice Grain. Physical Appearance Sterile Filtered white lyophilized powder. Formulation The Recombinant Lysozyme was lyophilized with no additives. Stability Recombinant Lysozyme although stable at room temperature for 3 weeks, should be stored at 2-8°C. Purity Greater than 90% as determined by both: （a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. Activity 136,227 Units/mg protein. 1 unit will produce a change of A450 0.001 per minute at pH-6.24 ａnd 25°C, using a suspension of micrococcus lysodeikticus as substrate in a 2.6ml reaction volume. Instructions for Use Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5mg/ml （7,000⁻⁷0,000 U/ml）. The common extraction buffer for E. coli cells contains 0.2mg/ml of recombinant Lysozyme in 100mM Tris-HCl, 2mM EDTA, 0.05% Triton X-100, pH 8. The cell paste is suspended in extraction buffer ａnd incubated for at least 15 min at room temperature. alternatively, Triton X-100 at 1% ａnd PMSF at 1mM can be added separately ａnd the lysis solution is further incubated for at least 15 min at 37 °C. The lysed cell suspension is clarified by centrifugation at 20,000g for at least 15 min. The extraction conditions ａnd concentration of the Recombinant Human Lysozyme needed for optimal cell lysis ａnd protein recovery depends on various factors ａnd has to be determined empirically. Usage Prospec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Lysozyme Human/ 重组人溶菌酶
产品编号：ENZ-362
产品规格：10mg/1g/10g
Synonyms Lysozyme C, EC 3.2.1.17, LYZ, LZM, 1,4-beta-N-acetylmuramidase C, Lysozyme. Introduction Lysozyme is an enzyme found in egg white, tears, ａnd other secretions. Lysozyme is responsible for attacking & breaking down the polysaccharide walls of many kinds of bacteria ａnd thus it provides some protection against infection. Bacteria build a tough skin of carbohydrate chains, interlocked by short peptide strands, that braces their delicate membrane against the cell＇s high osmotic pressure. Lysozyme breaks these carbohydrate chains, destroying the structural integrity of the cell wall. The bacteria burst under their own internal pressure. Lysozyme （muramidase） hydrolyzes preferentially the ?-1,4 glucosidic linkages between N-acetylmuramic acid ａnd N-acetylglucosamine which occur in the mucopeptide cell wall. Lysozyme is a mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. Cartilage lysozyme has a role in cartilage calcification. Presence of the Lysozyme in cerebrospinal fluid is indicative of tumor of the central nervous system, normally lysozyme activity is practically absent from urine, bile ａnd spinal fluid. Description Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5 mg/ml （7,000⁻⁷0,000 U/ml）.
Recombinant Human Lysozyme produced in Plant is a single, non-glycosilated polypeptide chain containing 130 amino acids ａnd a molecular mass of 14 kDa. Source Rice Grain. Physical Appearance Sterile Filtered white lyophilized powder. Formulation The Recombinant Lysozyme was lyophilized with no additives. Stability Recombinant Lysozyme although stable at room temperature for 3 weeks, should be stored at 2-8°C. Purity Greater than 90% as determined by both: （a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. Activity 136,227 Units/mg protein. 1 unit will produce a change of A450 0.001 per minute at pH-6.24 ａnd 25°C, using a suspension of micrococcus lysodeikticus as substrate in a 2.6ml reaction volume. Instructions for Use Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5mg/ml （7,000⁻⁷0,000 U/ml）. The common extraction buffer for E. coli cells contains 0.2mg/ml of recombinant Lysozyme in 100mM Tris-HCl, 2mM EDTA, 0.05% Triton X-100, pH 8. The cell paste is suspended in extraction buffer ａnd incubated for at least 15 min at room temperature. alternatively, Triton X-100 at 1% ａnd PMSF at 1mM can be added separately ａnd the lysis solution is further incubated for at least 15 min at 37 °C. The lysed cell suspension is clarified by centrifugation at 20,000g for at least 15 min. The extraction conditions ａnd concentration of the Recombinant Human Lysozyme needed for optimal cell lysis ａnd protein recovery depends on various factors ａnd has to be determined empirically. Usage Prospec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Lysozyme Human/ 重组人溶菌酶
产品编号：ENZ-362
产品规格：10mg/1g/10g
Synonyms Lysozyme C, EC 3.2.1.17, LYZ, LZM, 1,4-beta-N-acetylmuramidase C, Lysozyme. Introduction Lysozyme is an enzyme found in egg white, tears, ａnd other secretions. Lysozyme is responsible for attacking & breaking down the polysaccharide walls of many kinds of bacteria ａnd thus it provides some protection against infection. Bacteria build a tough skin of carbohydrate chains, interlocked by short peptide strands, that braces their delicate membrane against the cell＇s high osmotic pressure. Lysozyme breaks these carbohydrate chains, destroying the structural integrity of the cell wall. The bacteria burst under their own internal pressure. Lysozyme （muramidase） hydrolyzes preferentially the ?-1,4 glucosidic linkages between N-acetylmuramic acid ａnd N-acetylglucosamine which occur in the mucopeptide cell wall. Lysozyme is a mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. Cartilage lysozyme has a role in cartilage calcification. Presence of the Lysozyme in cerebrospinal fluid is indicative of tumor of the central nervous system, normally lysozyme activity is practically absent from urine, bile ａnd spinal fluid. Description Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5 mg/ml （7,000⁻⁷0,000 U/ml）.
Recombinant Human Lysozyme produced in Plant is a single, non-glycosilated polypeptide chain containing 130 amino acids ａnd a molecular mass of 14 kDa. Source Rice Grain. Physical Appearance Sterile Filtered white lyophilized powder. Formulation The Recombinant Lysozyme was lyophilized with no additives. Stability Recombinant Lysozyme although stable at room temperature for 3 weeks, should be stored at 2-8°C. Purity Greater than 90% as determined by both: （a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. Activity 136,227 Units/mg protein. 1 unit will produce a change of A450 0.001 per minute at pH-6.24 ａnd 25°C, using a suspension of micrococcus lysodeikticus as substrate in a 2.6ml reaction volume. Instructions for Use Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5mg/ml （7,000⁻⁷0,000 U/ml）. The common extraction buffer for E. coli cells contains 0.2mg/ml of recombinant Lysozyme in 100mM Tris-HCl, 2mM EDTA, 0.05% Triton X-100, pH 8. The cell paste is suspended in extraction buffer ａnd incubated for at least 15 min at room temperature. alternatively, Triton X-100 at 1% ａnd PMSF at 1mM can be added separately ａnd the lysis solution is further incubated for at least 15 min at 37 °C. The lysed cell suspension is clarified by centrifugation at 20,000g for at least 15 min. The extraction conditions ａnd concentration of the Recombinant Human Lysozyme needed for optimal cell lysis ａnd protein recovery depends on various factors ａnd has to be determined empirically. Usage Prospec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Lysozyme Human/ 重组人溶菌酶
产品编号：ENZ-362
产品规格：10mg/1g/10g
Synonyms Lysozyme C, EC 3.2.1.17, LYZ, LZM, 1,4-beta-N-acetylmuramidase C, Lysozyme. Introduction Lysozyme is an enzyme found in egg white, tears, ａnd other secretions. Lysozyme is responsible for attacking & breaking down the polysaccharide walls of many kinds of bacteria ａnd thus it provides some protection against infection. Bacteria build a tough skin of carbohydrate chains, interlocked by short peptide strands, that braces their delicate membrane against the cell＇s high osmotic pressure. Lysozyme breaks these carbohydrate chains, destroying the structural integrity of the cell wall. The bacteria burst under their own internal pressure. Lysozyme （muramidase） hydrolyzes preferentially the ?-1,4 glucosidic linkages between N-acetylmuramic acid ａnd N-acetylglucosamine which occur in the mucopeptide cell wall. Lysozyme is a mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. Cartilage lysozyme has a role in cartilage calcification. Presence of the Lysozyme in cerebrospinal fluid is indicative of tumor of the central nervous system, normally lysozyme activity is practically absent from urine, bile ａnd spinal fluid. Description Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5 mg/ml （7,000⁻⁷0,000 U/ml）.
Recombinant Human Lysozyme produced in Plant is a single, non-glycosilated polypeptide chain containing 130 amino acids ａnd a molecular mass of 14 kDa. Source Rice Grain. Physical Appearance Sterile Filtered white lyophilized powder. Formulation The Recombinant Lysozyme was lyophilized with no additives. Stability Recombinant Lysozyme although stable at room temperature for 3 weeks, should be stored at 2-8°C. Purity Greater than 90% as determined by both: （a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. Activity 136,227 Units/mg protein. 1 unit will produce a change of A450 0.001 per minute at pH-6.24 ａnd 25°C, using a suspension of micrococcus lysodeikticus as substrate in a 2.6ml reaction volume. Instructions for Use Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5mg/ml （7,000⁻⁷0,000 U/ml）. The common extraction buffer for E. coli cells contains 0.2mg/ml of recombinant Lysozyme in 100mM Tris-HCl, 2mM EDTA, 0.05% Triton X-100, pH 8. The cell paste is suspended in extraction buffer ａnd incubated for at least 15 min at room temperature. alternatively, Triton X-100 at 1% ａnd PMSF at 1mM can be added separately ａnd the lysis solution is further incubated for at least 15 min at 37 °C. The lysed cell suspension is clarified by centrifugation at 20,000g for at least 15 min. The extraction conditions ａnd concentration of the Recombinant Human Lysozyme needed for optimal cell lysis ａnd protein recovery depends on various factors ａnd has to be determined empirically. Usage Prospec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Lysozyme Human/ 重组人溶菌酶
产品编号：ENZ-362
产品规格：10mg/1g/10g
Synonyms Lysozyme C, EC 3.2.1.17, LYZ, LZM, 1,4-beta-N-acetylmuramidase C, Lysozyme. Introduction Lysozyme is an enzyme found in egg white, tears, ａnd other secretions. Lysozyme is responsible for attacking & breaking down the polysaccharide walls of many kinds of bacteria ａnd thus it provides some protection against infection. Bacteria build a tough skin of carbohydrate chains, interlocked by short peptide strands, that braces their delicate membrane against the cell＇s high osmotic pressure. Lysozyme breaks these carbohydrate chains, destroying the structural integrity of the cell wall. The bacteria burst under their own internal pressure. Lysozyme （muramidase） hydrolyzes preferentially the ?-1,4 glucosidic linkages between N-acetylmuramic acid ａnd N-acetylglucosamine which occur in the mucopeptide cell wall. Lysozyme is a mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. Cartilage lysozyme has a role in cartilage calcification. Presence of the Lysozyme in cerebrospinal fluid is indicative of tumor of the central nervous system, normally lysozyme activity is practically absent from urine, bile ａnd spinal fluid. Description Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5 mg/ml （7,000⁻⁷0,000 U/ml）.
Recombinant Human Lysozyme produced in Plant is a single, non-glycosilated polypeptide chain containing 130 amino acids ａnd a molecular mass of 14 kDa. Source Rice Grain. Physical Appearance Sterile Filtered white lyophilized powder. Formulation The Recombinant Lysozyme was lyophilized with no additives. Stability Recombinant Lysozyme although stable at room temperature for 3 weeks, should be stored at 2-8°C. Purity Greater than 90% as determined by both: （a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. Activity 136,227 Units/mg protein. 1 unit will produce a change of A450 0.001 per minute at pH-6.24 ａnd 25°C, using a suspension of micrococcus lysodeikticus as substrate in a 2.6ml reaction volume. Instructions for Use Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5mg/ml （7,000⁻⁷0,000 U/ml）. The common extraction buffer for E. coli cells contains 0.2mg/ml of recombinant Lysozyme in 100mM Tris-HCl, 2mM EDTA, 0.05% Triton X-100, pH 8. The cell paste is suspended in extraction buffer ａnd incubated for at least 15 min at room temperature. alternatively, Triton X-100 at 1% ａnd PMSF at 1mM can be added separately ａnd the lysis solution is further incubated for at least 15 min at 37 °C. The lysed cell suspension is clarified by centrifugation at 20,000g for at least 15 min. The extraction conditions ａnd concentration of the Recombinant Human Lysozyme needed for optimal cell lysis ａnd protein recovery depends on various factors ａnd has to be determined empirically. Usage Prospec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Lysozyme Human/ 重组人溶菌酶
产品编号：ENZ-362
产品规格：10mg/1g/10g
Synonyms Lysozyme C, EC 3.2.1.17, LYZ, LZM, 1,4-beta-N-acetylmuramidase C, Lysozyme. Introduction Lysozyme is an enzyme found in egg white, tears, ａnd other secretions. Lysozyme is responsible for attacking & breaking down the polysaccharide walls of many kinds of bacteria ａnd thus it provides some protection against infection. Bacteria build a tough skin of carbohydrate chains, interlocked by short peptide strands, that braces their delicate membrane against the cell＇s high osmotic pressure. Lysozyme breaks these carbohydrate chains, destroying the structural integrity of the cell wall. The bacteria burst under their own internal pressure. Lysozyme （muramidase） hydrolyzes preferentially the ?-1,4 glucosidic linkages between N-acetylmuramic acid ａnd N-acetylglucosamine which occur in the mucopeptide cell wall. Lysozyme is a mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. Cartilage lysozyme has a role in cartilage calcification. Presence of the Lysozyme in cerebrospinal fluid is indicative of tumor of the central nervous system, normally lysozyme activity is practically absent from urine, bile ａnd spinal fluid. Description Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5 mg/ml （7,000⁻⁷0,000 U/ml）.
Recombinant Human Lysozyme produced in Plant is a single, non-glycosilated polypeptide chain containing 130 amino acids ａnd a molecular mass of 14 kDa. Source Rice Grain. Physical Appearance Sterile Filtered white lyophilized powder. Formulation The Recombinant Lysozyme was lyophilized with no additives. Stability Recombinant Lysozyme although stable at room temperature for 3 weeks, should be stored at 2-8°C. Purity Greater than 90% as determined by both: （a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. Activity 136,227 Units/mg protein. 1 unit will produce a change of A450 0.001 per minute at pH-6.24 ａnd 25°C, using a suspension of micrococcus lysodeikticus as substrate in a 2.6ml reaction volume. Instructions for Use Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5mg/ml （7,000⁻⁷0,000 U/ml）. The common extraction buffer for E. coli cells contains 0.2mg/ml of recombinant Lysozyme in 100mM Tris-HCl, 2mM EDTA, 0.05% Triton X-100, pH 8. The cell paste is suspended in extraction buffer ａnd incubated for at least 15 min at room temperature. alternatively, Triton X-100 at 1% ａnd PMSF at 1mM can be added separately ａnd the lysis solution is further incubated for at least 15 min at 37 °C. The lysed cell suspension is clarified by centrifugation at 20,000g for at least 15 min. The extraction conditions ａnd concentration of the Recombinant Human Lysozyme needed for optimal cell lysis ａnd protein recovery depends on various factors ａnd has to be determined empirically. Usage Prospec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Lysozyme Human/ 重组人溶菌酶
产品编号：ENZ-362
产品规格：10mg/1g/10g
Synonyms Lysozyme C, EC 3.2.1.17, LYZ, LZM, 1,4-beta-N-acetylmuramidase C, Lysozyme. Introduction Lysozyme is an enzyme found in egg white, tears, ａnd other secretions. Lysozyme is responsible for attacking & breaking down the polysaccharide walls of many kinds of bacteria ａnd thus it provides some protection against infection. Bacteria build a tough skin of carbohydrate chains, interlocked by short peptide strands, that braces their delicate membrane against the cell＇s high osmotic pressure. Lysozyme breaks these carbohydrate chains, destroying the structural integrity of the cell wall. The bacteria burst under their own internal pressure. Lysozyme （muramidase） hydrolyzes preferentially the ?-1,4 glucosidic linkages between N-acetylmuramic acid ａnd N-acetylglucosamine which occur in the mucopeptide cell wall. Lysozyme is a mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. Cartilage lysozyme has a role in cartilage calcification. Presence of the Lysozyme in cerebrospinal fluid is indicative of tumor of the central nervous system, normally lysozyme activity is practically absent from urine, bile ａnd spinal fluid. Description Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5 mg/ml （7,000⁻⁷0,000 U/ml）.
Recombinant Human Lysozyme produced in Plant is a single, non-glycosilated polypeptide chain containing 130 amino acids ａnd a molecular mass of 14 kDa. Source Rice Grain. Physical Appearance Sterile Filtered white lyophilized powder. Formulation The Recombinant Lysozyme was lyophilized with no additives. Stability Recombinant Lysozyme although stable at room temperature for 3 weeks, should be stored at 2-8°C. Purity Greater than 90% as determined by both: （a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. Activity 136,227 Units/mg protein. 1 unit will produce a change of A450 0.001 per minute at pH-6.24 ａnd 25°C, using a suspension of micrococcus lysodeikticus as substrate in a 2.6ml reaction volume. Instructions for Use Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5mg/ml （7,000⁻⁷0,000 U/ml）. The common extraction buffer for E. coli cells contains 0.2mg/ml of recombinant Lysozyme in 100mM Tris-HCl, 2mM EDTA, 0.05% Triton X-100, pH 8. The cell paste is suspended in extraction buffer ａnd incubated for at least 15 min at room temperature. alternatively, Triton X-100 at 1% ａnd PMSF at 1mM can be added separately ａnd the lysis solution is further incubated for at least 15 min at 37 °C. The lysed cell suspension is clarified by centrifugation at 20,000g for at least 15 min. The extraction conditions ａnd concentration of the Recombinant Human Lysozyme needed for optimal cell lysis ａnd protein recovery depends on various factors ａnd has to be determined empirically. Usage Prospec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Lysozyme Human/ 重组人溶菌酶
产品编号：ENZ-362
产品规格：10mg/1g/10g
Synonyms Lysozyme C, EC 3.2.1.17, LYZ, LZM, 1,4-beta-N-acetylmuramidase C, Lysozyme. Introduction Lysozyme is an enzyme found in egg white, tears, ａnd other secretions. Lysozyme is responsible for attacking & breaking down the polysaccharide walls of many kinds of bacteria ａnd thus it provides some protection against infection. Bacteria build a tough skin of carbohydrate chains, interlocked by short peptide strands, that braces their delicate membrane against the cell＇s high osmotic pressure. Lysozyme breaks these carbohydrate chains, destroying the structural integrity of the cell wall. The bacteria burst under their own internal pressure. Lysozyme （muramidase） hydrolyzes preferentially the ?-1,4 glucosidic linkages between N-acetylmuramic acid ａnd N-acetylglucosamine which occur in the mucopeptide cell wall. Lysozyme is a mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. Cartilage lysozyme has a role in cartilage calcification. Presence of the Lysozyme in cerebrospinal fluid is indicative of tumor of the central nervous system, normally lysozyme activity is practically absent from urine, bile ａnd spinal fluid. Description Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5 mg/ml （7,000⁻⁷0,000 U/ml）.
Recombinant Human Lysozyme produced in Plant is a single, non-glycosilated polypeptide chain containing 130 amino acids ａnd a molecular mass of 14 kDa. Source Rice Grain. Physical Appearance Sterile Filtered white lyophilized powder. Formulation The Recombinant Lysozyme was lyophilized with no additives. Stability Recombinant Lysozyme although stable at room temperature for 3 weeks, should be stored at 2-8°C. Purity Greater than 90% as determined by both: （a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. Activity 136,227 Units/mg protein. 1 unit will produce a change of A450 0.001 per minute at pH-6.24 ａnd 25°C, using a suspension of micrococcus lysodeikticus as substrate in a 2.6ml reaction volume. Instructions for Use Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5mg/ml （7,000⁻⁷0,000 U/ml）. The common extraction buffer for E. coli cells contains 0.2mg/ml of recombinant Lysozyme in 100mM Tris-HCl, 2mM EDTA, 0.05% Triton X-100, pH 8. The cell paste is suspended in extraction buffer ａnd incubated for at least 15 min at room temperature. alternatively, Triton X-100 at 1% ａnd PMSF at 1mM can be added separately ａnd the lysis solution is further incubated for at least 15 min at 37 °C. The lysed cell suspension is clarified by centrifugation at 20,000g for at least 15 min. The extraction conditions ａnd concentration of the Recombinant Human Lysozyme needed for optimal cell lysis ａnd protein recovery depends on various factors ａnd has to be determined empirically. Usage Prospec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Lysozyme Human/ 重组人溶菌酶
产品编号：ENZ-362
产品规格：10mg/1g/10g
Synonyms Lysozyme C, EC 3.2.1.17, LYZ, LZM, 1,4-beta-N-acetylmuramidase C, Lysozyme. Introduction Lysozyme is an enzyme found in egg white, tears, ａnd other secretions. Lysozyme is responsible for attacking & breaking down the polysaccharide walls of many kinds of bacteria ａnd thus it provides some protection against infection. Bacteria build a tough skin of carbohydrate chains, interlocked by short peptide strands, that braces their delicate membrane against the cell＇s high osmotic pressure. Lysozyme breaks these carbohydrate chains, destroying the structural integrity of the cell wall. The bacteria burst under their own internal pressure. Lysozyme （muramidase） hydrolyzes preferentially the ?-1,4 glucosidic linkages between N-acetylmuramic acid ａnd N-acetylglucosamine which occur in the mucopeptide cell wall. Lysozyme is a mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. Cartilage lysozyme has a role in cartilage calcification. Presence of the Lysozyme in cerebrospinal fluid is indicative of tumor of the central nervous system, normally lysozyme activity is practically absent from urine, bile ａnd spinal fluid. Description Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5 mg/ml （7,000⁻⁷0,000 U/ml）.
Recombinant Human Lysozyme produced in Plant is a single, non-glycosilated polypeptide chain containing 130 amino acids ａnd a molecular mass of 14 kDa. Source Rice Grain. Physical Appearance Sterile Filtered white lyophilized powder. Formulation The Recombinant Lysozyme was lyophilized with no additives. Stability Recombinant Lysozyme although stable at room temperature for 3 weeks, should be stored at 2-8°C. Purity Greater than 90% as determined by both: （a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. Activity 136,227 Units/mg protein. 1 unit will produce a change of A450 0.001 per minute at pH-6.24 ａnd 25°C, using a suspension of micrococcus lysodeikticus as substrate in a 2.6ml reaction volume. Instructions for Use Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5mg/ml （7,000⁻⁷0,000 U/ml）. The common extraction buffer for E. coli cells contains 0.2mg/ml of recombinant Lysozyme in 100mM Tris-HCl, 2mM EDTA, 0.05% Triton X-100, pH 8. The cell paste is suspended in extraction buffer ａnd incubated for at least 15 min at room temperature. alternatively, Triton X-100 at 1% ａnd PMSF at 1mM can be added separately ａnd the lysis solution is further incubated for at least 15 min at 37 °C. The lysed cell suspension is clarified by centrifugation at 20,000g for at least 15 min. The extraction conditions ａnd concentration of the Recombinant Human Lysozyme needed for optimal cell lysis ａnd protein recovery depends on various factors ａnd has to be determined empirically. Usage Prospec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Lysozyme Human/ 重组人溶菌酶
产品编号：ENZ-362
产品规格：10mg/1g/10g
产品规格：10mg/1g/10g
| Synonyms | Lysozyme C, EC 3.2.1.17, LYZ, LZM, 1,4-beta-N-acetylmuramidase C, Lysozyme. |
| Introduction | Lysozyme is an enzyme found in egg white, tears, ａnd other secretions. Lysozyme is responsible for attacking & breaking down the polysaccharide walls of many kinds of bacteria ａnd thus it provides some protection against infection. Bacteria build a tough skin of carbohydrate chains, interlocked by short peptide strands, that braces their delicate membrane against the cell＇s high osmotic pressure. Lysozyme breaks these carbohydrate chains, destroying the structural integrity of the cell wall. The bacteria burst under their own internal pressure. Lysozyme （muramidase） hydrolyzes preferentially the ?-1,4 glucosidic linkages between N-acetylmuramic acid ａnd N-acetylglucosamine which occur in the mucopeptide cell wall. Lysozyme is a mediator in the anti-tumor function of macrophages which, it has been shown, secrete the enzyme. Cartilage lysozyme has a role in cartilage calcification. Presence of the Lysozyme in cerebrospinal fluid is indicative of tumor of the central nervous system, normally lysozyme activity is practically absent from urine, bile ａnd spinal fluid. |
| Description | Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5 mg/ml （7,000⁻⁷0,000 U/ml）. Recombinant Human Lysozyme produced in Plant is a single, non-glycosilated polypeptide chain containing 130 amino acids ａnd a molecular mass of 14 kDa. |
| Source | Rice Grain. |
| Physical Appearance | Sterile Filtered white lyophilized powder. |
| Formulation | The Recombinant Lysozyme was lyophilized with no additives. |
| Stability | Recombinant Lysozyme although stable at room temperature for 3 weeks, should be stored at 2-8°C. |
| Purity | Greater than 90% as determined by both: （a） Analysis by RP-HPLC. （b） Analysis by SDS-PAGE. |
| Activity | 136,227 Units/mg protein. 1 unit will produce a change of A450 0.001 per minute at pH-6.24 ａnd 25°C, using a suspension of micrococcus lysodeikticus as substrate in a 2.6ml reaction volume. |
| Instructions for Use | Recombinant Human Lysozyme is added in lysing bacterial cells to the cell extraction buffer at a range of 0.05-0.5mg/ml （7,000⁻⁷0,000 U/ml）. The common extraction buffer for E. coli cells contains 0.2mg/ml of recombinant Lysozyme in 100mM Tris-HCl, 2mM EDTA, 0.05% Triton X-100, pH 8. The cell paste is suspended in extraction buffer ａnd incubated for at least 15 min at room temperature. alternatively, Triton X-100 at 1% ａnd PMSF at 1mM can be added separately ａnd the lysis solution is further incubated for at least 15 min at 37 °C. The lysed cell suspension is clarified by centrifugation at 20,000g for at least 15 min. The extraction conditions ａnd concentration of the Recombinant Human Lysozyme needed for optimal cell lysis ａnd protein recovery depends on various factors ａnd has to be determined empirically. |
| Usage | Prospec＇s products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals. |
Lysozyme,Human,重组人溶菌酶
