LYG2 Human

Lysozyme G-Like 2 Human Recombinant
Cat. No.
BT21909
Source
E.coli.
Synonyms
Lysozyme G-Like 2, Lysozyme G-Like Protein 2, LYGH, EC 3.2.1.-.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% as determined by SDS-PAGE.
Usage
THE BioTek'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.
Shipped with Ice Packs
In Stock

Description

LYG2 Human Recombinant produced in E. coli is a single polypeptide chain containing 216 amino acids (20-212) and having a molecular mass of 23.9 kDa. LYG2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Lysozyme G-like 2, also known as LYGH or LYG2, belongs to the glycosyl hydrolase 23 family. It plays a crucial role in the human innate immune system by breaking down bacterial cell walls, leading to their destruction. LYG2 possesses an SLT domain, a protein structure found in both bacterial lytic transglycosylase (SLT) and eukaryotic lysozymes (GEWL). The SLT domain is responsible for catalyzing the breakdown of the β-1,4-glycosidic bond present between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc).
Description
Recombinant human LYG2, produced in E. coli, is a single polypeptide chain comprising 216 amino acids (residues 20-212). With a molecular weight of 23.9 kDa, it includes a 23 amino acid His-tag attached to the N-terminus. Purification is achieved through proprietary chromatographic methods.
Physical Appearance
A clear, sterile solution.
Formulation
The LYG2 solution is provided at a concentration of 0.5 mg/mL and is formulated in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.2 M NaCl, 1 mM DTT, and 20% glycerol.
Stability
For optimal storage, refrigerate the solution at 4°C if the entire volume will be used within 2-4 weeks. For extended storage, freeze the solution at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freezing and thawing of the solution.
Purity
The purity of LYG2 is greater than 90% as determined by SDS-PAGE analysis.
Synonyms
Lysozyme G-Like 2, Lysozyme G-Like Protein 2, LYGH, EC 3.2.1.-.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSSYPFSHS MKPHLHPRLY HGCYGDIMTM KTSGATCDAN SVMNCGIRGS EMFAEMDLRA IKPYQTLIKE VGQRHCVDPA VIAAIISRES HGGSVLQDGW DHRGLKFGLM QLDKQTYHPV GAWDSKEHLS QATGILTERI KAIQKKFPTW SVAQHLKGGL SAFKSGIEAI ATPSDIDNDF VNDIIARAKF YKRQSF.

Product Science Overview

Gene and Protein Structure

The LYG2 gene is located on chromosome 2q11.2 . The recombinant human LYG2 protein is a heat-resistant 20-kD protein obtained from yeast . It contains a SLT domain, which is present in bacterial lytic transglycosylase and eukaryotic lysozymes . This domain catalyzes the cleavage of the beta-1,4-glycosidic bond, contributing to its bacteriolytic function .

Expression Patterns and Tissue Distribution

LYG2 is predominantly expressed in the human eye, particularly in the lacrimal gland, and to a lesser extent in the testis . Using RT-PCR, high expression levels of LYG2 were detected in the eye, while weak expression was observed in the testis . SDS-PAGE and mass spectrometric analysis have identified LYG2 in human tears .

Biological Functions and Mode of Action

Recombinant human LYG2 has been shown to inhibit the growth of gram-positive bacteria but does not affect gram-negative bacteria or Candida albicans . Interestingly, the addition of lysozyme C (LYZ) does not enhance LYG2 activity . This specificity suggests that LYG2 plays a unique role in the immune defense mechanism against certain bacterial infections.

Regulatory Mechanisms

The regulatory mechanisms governing LYG2 expression and activity are not fully understood. However, its tissue-specific expression and bacteriolytic activity indicate that it may be tightly regulated to function effectively in innate immunity.

Applications and Research

Recombinant human LYG2, fused to a His-tag at the N-terminus, is expressed in E. coli and purified using conventional chromatography techniques . This recombinant protein is used in research to study its structure, function, and potential therapeutic applications in combating bacterial infections.

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