TGM2 Human

Tissue Transglutaminase Human Recombinant
Cat. No.
BT15723
Source
Escherichia Coli.
Synonyms

Protein gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.

Appearance
Sterile Filtered clear solution.
Purity
Greater than 95% as determined by SDS-PAGE.
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.
Shipped with Ice Packs
In Stock

Description

Tissue Transglutaminase Human Recombinant produced in E.coli is a non-glycosylated, polypeptide chain having a molecular mass of 78,018 Dalton. tTG is expressed with a -6xHis tag and purified by proprietary chromatographic techniques. By point mutation of the active center the catalytic transglutaminase activity has been eliminated, resulting in increased stability during storage and coating.

Product Specs

Introduction
Celiac disease is an intestinal disorder characterized by varying degrees of intestinal damage. Tissue-type transglutaminase (tTG) is considered the primary target for the immune system in celiac disease, and antibodies against tTG are more accurate in diagnosis than anti-gliadin antibodies. Highly purified recombinant human tTG is now available as an alternative to the traditionally used tTG fraction from guinea pigs. Tissue-type transglutaminase antigens have been specifically engineered for improved handling: modification of an active site amino acid eliminates the protein cross-linking activity of the enzyme while preserving its natural three-dimensional structure and secondary GTPase activity. This modification ensures consistent properties of the antigen preparations by preventing the formation of variable and poorly defined aggregates of tTG antigen and host cell proteins.
Description
Recombinant Human Tissue Transglutaminase, produced in E. coli, is an unglycosylated polypeptide chain with a molecular weight of 78,018 Daltons. It is expressed with a -6xHis tag and purified using proprietary chromatography methods. The catalytic transglutaminase activity has been eliminated by introducing a point mutation in the active site, resulting in enhanced stability during storage and coating.
Physical Appearance
A clear, sterile-filtered solution.
Formulation
TGM2 is provided in a solution containing 16mM HEPES buffer (pH 8.0), 400mM NaCl, and 20% glycerol.
Purity
Purity exceeds 95% as determined by SDS-PAGE analysis.
Stability
For short-term storage (2-4 weeks), keep at 4°C. For long-term storage, freeze at -20°C. Repeated freezing and thawing should be avoided.
Synonyms

Protein gamma-glutamyltransferase 2, EC 2.3.2.13, Tissue transglutaminase, TGase C, TGC, TG(C), Transglutaminase-2, TGase-H, TG2, TGM2.

Source
Escherichia Coli.

Product Science Overview

Introduction

Tissue transglutaminase (tTG), also known as transglutaminase 2 (TG2), is an enzyme that plays a crucial role in various biological processes, including cell adhesion, extracellular matrix assembly, and wound healing . It is widely expressed in human tissues such as the skin, liver, and jejunal mucosa . Recombinant human tissue transglutaminase (rh-tTG) is a form of this enzyme that is produced through recombinant DNA technology, allowing for its use in research and clinical applications.

Background and Significance

Tissue transglutaminase is best known for its role as the autoantigen in celiac disease, a chronic autoimmune disorder triggered by the ingestion of gluten . In individuals with celiac disease, the immune system mistakenly targets tTG, leading to inflammation and damage to the small intestine . Beyond celiac disease, tTG has been implicated in the pathophysiology of various other conditions, including different cancers and neurodegenerative diseases .

Preparation Methods

Recombinant human tissue transglutaminase is typically produced using mammalian cell lines, such as the human embryonic kidney cell line 293-EBNA . The enzyme is expressed as a C-terminal fusion protein with a tag (e.g., Strep-tag II) that facilitates its purification via affinity chromatography . This method ensures that the recombinant enzyme retains its activity and can be used for various biochemical assays and diagnostic tests.

Chemical Reactions and Applications

Tissue transglutaminase catalyzes the formation of covalent bonds between glutamine residues and primary amines, a process known as transamidation . This reaction is essential for the cross-linking of proteins, which contributes to the stability and integrity of the extracellular matrix . In the context of celiac disease, tTG modifies gluten peptides, making them more immunogenic and triggering an autoimmune response .

Recombinant human tissue transglutaminase is used in various research and clinical applications. For instance, it is employed in enzyme-linked immunosorbent assays (ELISAs) to diagnose gluten-sensitive enteropathy (GSE), including celiac disease and dermatitis herpetiformis . These assays detect antibodies against tTG in patient sera, providing a non-invasive and reliable diagnostic tool .

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