Lysozyme Human | ProSpec

Description

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Lysozyme Human Recombinant

	10mg($80)
	1gr($100)
	10gr($650)

Catalogue Number

ENZ-362

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.