TGM2 Mouse

Tissue Transglutaminase Mouse Recombinant
Cat. No.
BT15892
Source
E.coli.
Synonyms
Protein-glutamine gamma-glutamyltransferase 2, G[a]h, TG2, TGase2, tTG, tTGas, Protein-glutamine gamma-glutamyltransferase 2, Tissue transglutaminase, Transglutaminase C.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 85% 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

TGM2 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 709 amino acids (1-686 a.a) and having a molecular mass of 79.4kDa.
TGM2 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
Celiac disease is an intestinal disorder characterized by varying degrees of intestinal damage. The enzyme tissue-type transglutaminase (tTG) is considered the primary target of the immune system in celiac disease, and antibodies against tTG are more accurate in diagnosing celiac disease compared to antibodies against gliadin. Recombinant human tTG, produced in a highly purified form, is now available as an alternative to the traditionally used tTG extracted from guinea pigs. To improve handling, modifications have been made to tissue-type transglutaminase antigens. These modifications involve replacing an amino acid at the enzyme's active site, which eliminates its protein-linking activity while preserving its original three-dimensional structure and secondary GTPase activity. This engineering ensures consistent properties of the antigen preparations by preventing the formation of unpredictable and poorly defined aggregates between the tTG antigen and proteins from the host cells.
Description
Recombinant Mouse TGM2, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 709 amino acids (1-686 a.a) with a molecular weight of 79.4 kDa. It includes a 23-amino acid His-tag fused to the N-terminus and is purified using proprietary chromatographic methods.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The TGM2 protein is supplied as a solution at a concentration of 0.5 mg/ml in a buffer containing phosphate-buffered saline (pH 7.4), 10% glycerol, and 1 mM DTT.
Stability
For short-term storage (2-4 weeks), keep refrigerated at 4°C. For longer periods, store frozen at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. It's important to avoid repeated freezing and thawing cycles.
Purity
The purity is determined to be greater than 85% by SDS-PAGE analysis.
Synonyms
Protein-glutamine gamma-glutamyltransferase 2, G[a]h, TG2, TGase2, tTG, tTGas, Protein-glutamine gamma-glutamyltransferase 2, Tissue transglutaminase, Transglutaminase C.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMAEELLL ERCDLEIQAN GRDHHTADLC QEKLVLRRGQ RFRLTLYFEG RGYEASVDSL TFGAVTGPDPSEEAGTKARF SLSDNVEEGS WSASVLDQQD NVLSLQLCTP ANAPIGLYRL SLEASTGYQG SSFVLGHFIL LYNAWCPADD VYLDSEEERR EYVLTQQGFI YQGSVKFIKS VPWNFGQFED GILDTCLMLL DMNPKFLKNR SRDCSRRSSP IYVGRVVSAM VNCNDDQGVL LGRWDNNYGD GISPMAWIGS VDILRRWKEH GCQQVKYGQC WVFAAVACTV LRCLGIPTRV VTNYNSAHDQ NSNLLIEYFR NEFGELESNK SEMIWNFHCW VESWMTRPDL QPGYEGWQAI DPTPQEKSEG TYCCGPVSVR AIKEGDLSTK YDAPFVFAEV NADVVDWIRQ EDGSVLKSIN RSLVVGQKIS TKSVGRDDRE DITHTYKYPE GSPEEREVFT KANHLNKLAE KEETGVAMRI RVGDSMSMGN DFDVFAHIGN DTSETRECRL LLCARTVSYN GVLGPECGTE DINLTLDPYS ENSIPLRILY EKYSGCLTES NLIKVRGLLI EPAANSYLLA ERDLYLENPE IKIRVLGEPK QNRKLVAEVS LKNPLSDPLY DCIFTVEGAG LTKEQKSVEV SDPVPAGDLV KARVDLFPTD IGLHKLVVNF QCDKLKSVKG YRNVIIGPA.

Product Science Overview

Introduction

Tissue transglutaminase, also known as transglutaminase 2 (TG2), is a multifunctional enzyme that belongs to the family of protein-glutamine γ-glutamyltransferases . This enzyme is involved in various physiological processes, including protein cross-linking, cell signaling, and apoptosis . The recombinant form of tissue transglutaminase from mice is widely used in research to study its functions and regulatory mechanisms.

Structure and Function

Tissue transglutaminase is a 78-kDa, calcium-dependent enzyme that catalyzes the formation of covalent bonds between an ε-amino group of a lysine residue and a γ-carboxamide group of a glutamine residue . This cross-linking activity is crucial for stabilizing protein structures and is highly resistant to proteolysis . Additionally, tissue transglutaminase exhibits guanosine 5′-triphosphate (GTP) hydrolysis activity, protein disulfide isomerase activity, and protein kinase activity .

Physiological Roles

Tissue transglutaminase is involved in several physiological processes, including:

  • Apoptosis: It plays a role in the clearance of apoptotic cells .
  • Angiogenesis: It is involved in the formation of new blood vessels .
  • Wound Healing: It contributes to tissue repair and regeneration .
  • Cellular Differentiation: It aids in the differentiation of various cell types .
  • Neuronal Regeneration: It supports the regeneration of nerve cells .
  • Bone Development: It is essential for the development and maintenance of bone tissue .
Recombinant Production

The recombinant form of tissue transglutaminase from mice is produced using genetic engineering techniques. The gene encoding tissue transglutaminase is cloned into an expression vector, which is then introduced into a suitable host cell, such as Escherichia coli or mammalian cells . The host cells are cultured under optimal conditions to express the recombinant protein, which is subsequently purified using chromatographic techniques .

Applications in Research

Recombinant tissue transglutaminase is used in various research applications, including:

  • Studying Enzyme Mechanisms: Researchers use recombinant tissue transglutaminase to investigate its enzymatic activities and regulatory mechanisms .
  • Disease Models: It is used to study the role of tissue transglutaminase in diseases such as celiac disease, neurodegenerative diseases, and cancer .
  • Drug Development: Recombinant tissue transglutaminase is employed in the development of therapeutic agents targeting its enzymatic activities .

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