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Biologics

Recombinant Tissue Transglutaminase from Human

 Product Information

Cat #
MBS-1145
CAS No.
80146-85-6
Enzyme Commission Number
EC 2.3.2.13
Product Overview
High-quality enzyme products. Well-defined strains can be also provided for our clients to manufacture fermented products in a cost-effective way.
Features
Ready-to-use product, accelerating research progress, enhancing application performance.
Method
Technology
Synonyms
transglutaminase; Factor XIIIa; fibrinoligase; fibrin stabilizing factor; glutaminylpeptide γ-glutamyltransferase; polyamine transglutaminase; tissue transglutaminase; R-glutaminyl-peptide:amine γ-glutamyl transferase
Type
Function
Requires Ca2+. The γ-carboxamide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino-groups of protein- and peptide-bound lysine residues act as acceptors, to give intra- and inter-molecular N6-(5-glutamyl)-lysine crosslinks. Formed by proteolytic cleavage from plasma Factor XIII
Applications
Research and Development
Storage
Storage Buffer
Shelf Life
Strains
Sf9 cells
Source
Sf9 insect cells
Appearance
Molecular Weight
78,018 Da
Color / Form
Instruction
Enzyme Class
Transferases
Production Methods
Fermentation
Activity
Specific Enzyme Activity
Purity
Greater than 95% as determined by SDS-PAGE.
Unit Definition
Amino Acids Sequence
WARNINGS
Shipping
Formula
Reaction
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
Recommendation
Species Reactivity
Contents
Compatibility
Melting Point
Final Titre
Fermentation Time
Recovery Yield
Starting Material
Specification
On customer requests
Substrates
Concentration
0.6-1.4 µg/ml
Usage And Dosage
Product Type
Enzymes

 Description

Celiac disease is an enteropathy that is characterized by intestinal lesions of variable severity. Tissue-type transglutaminase (tTG) is believed to be the predominant autoantigen for celiac disease and the corresponding autoantibodies show higher sensitivity and specificity than anti-gliadin antibodies. Highly pure recombinant human tTG is now available to replace the traditionally used tTG fraction from guinea pig. Tissue-type transglutaminase antigens have been specifically modified for improved handling: exchange of an active site amino acid eliminates the protein cross-linking activity of the enzyme, while maintaining the native three-dimensional structure and the enzyme's secondary GTPase activity. This engineering assures reproducible properties of the antigen preparations through the absence of variable and ill-defined covalent aggregates of tTG antigen and host cell proteins.

For Research Use Only.
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