The amount of material in a given package size varies from lot to lot. The minimum activity of this product is 1.5 units per milligram of protein. The minimum protein concentration is 80%. As an example, a lot reporting an activity of 1.5 units per milligram with an 80% protein concentration will contain 400ug, 800ug, and 4.0 mg of powder in the 1 Unit, 2 Unit, and 10 Unit package sizes, respectively. Please see the link below to review a sample or lot specific Certificate of Analysis:
https://www.sigmaaldrich.com/product/sigma/t5398#product-documenation
T5398
Transglutaminase from guinea pig liver
lyophilized powder, ≥1.5 units/mg protein
Synonym(s):
Protein-Glutamine-γ-Glutamyltransferase, Protein-glutamine:amine γ-glutamyltransferase
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1 UNIT
$192.00
2 UNITS
$333.00
10 UNITS
$1,310.00
$192.00
Estimated to ship onDecember 25, 2025Details
About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
MDL number:
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Product Name
Transglutaminase from guinea pig liver, lyophilized powder, ≥1.5 units/mg protein
form
lyophilized powder
specific activity
≥1.5 units/mg protein
mol wt
76.6 kDa
composition
Protein, ≥80% modified Warburg-Christian
solubility
H2O: soluble 1.0 mg/mL, clear
application(s)
diagnostic assay manufacturing
shipped in
dry ice
storage temp.
−20°C
Quality Level
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This Item | G2262 | WH0007052M10 | SAB4200073 |
|---|---|---|---|
| specific activity ≥1.5 units/mg protein | specific activity 2.0-6.0 units/mg solid | specific activity - | specific activity - |
| application(s) diagnostic assay manufacturing | application(s) - | application(s) - | application(s) - |
| form lyophilized powder | form powder | form buffered aqueous solution | form buffered aqueous solution |
| shipped in dry ice | shipped in - | shipped in dry ice | shipped in dry ice |
| storage temp. −20°C | storage temp. −20°C | storage temp. −20°C | storage temp. −20°C |
| mol wt 76.6 kDa | mol wt - | mol wt - | mol wt antigen ~78 kDa |
Application
This product from Sigma has been used to demonstrate that tissue transglutaminase (tTG) selectively deamidates gluten peptides, which results in strongly enhanced T cell-stimulatory activity.[1] It has also been used to assess immune responses to A-gliadin peptides.[2] Furthermore, it has been used to demonstrate that tTG selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease.[3]
Transglutaminase has been used in a study to improve quantifiable assays to fully characterize the role of transglutaminase in diseases such as Huntington′s disease and Alzheimer′s disease.Transglutaminase has also been used in a study to develop a nonradioactive dot blot assay for transglutaminase activity.
Biochem/physiol Actions
Transglutaminase from guinea pig liver consists of a single polypeptide chain of 691 amino acid residues. It has six potential glycosylation sites (Asn-X-Ser or Asn-X-Thr), but it is not glycosylated. The molecular mass is approximately 76.6 kDa.[4] It is calcium dependent and has several calcium binding sites. The enzyme is inhibited by iodoacetamide and N-ethylmaleimide in the presence of calcium.[5] It catalyzes the incorporation of small molecular weight amines into γ-glutamine sites of proteins. In the absence of small molecular weight amines, it catalyzes the cross linking of proteins that results in the formation of γ-glutamyl-ε-lysine side chain peptides. Liver transglutaminase is a nonzymogenic enzyme.[6]
Other Notes
One unit will catalyze the formation of 1.0 μmole of hydroxamate per min from Nα-Z-Gln-Gly and hydroxylamine at pH 6.0 at 37 °C. (L-Glutamic acid γ-monohydroxamate is the standard.)
Physical form
Lyophilized powder containing Tris and dithioerythritol
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Y van de Wal et al.
Journal of immunology (Baltimore, Md. : 1950), 161(4), 1585-1588 (1998-08-26)
Celiac disease (CD) is caused by gluten ingestion in susceptible individuals. Tissue transglutaminase (tTG)-specific Abs are characteristic of CD, and increased tTG activity has been observed in the jejunal biopsies of patients. Here we demonstrate that tTG selectively deamidates gluten
M P M Adriaanse et al.
Alimentary pharmacology & therapeutics, 37(4), 482-490 (2013-01-08)
Enterocyte damage is the hallmark of coeliac disease (CD) resulting in malabsorption. Little is known about the recovery of enterocyte damage and its clinical consequences. Serum intestinal fatty acid binding protein (I-FABP) is a sensitive marker to study enterocyte damage.
R P Anderson et al.
Nature medicine, 6(3), 337-342 (2000-03-04)
Celiac disease (CD) is an increasingly diagnosed enteropathy (prevalence, 1:200-1:300) that is induced by dietary exposure to wheat gliadins (as well as related proteins in rye and barley) and is strongly associated with HLA-DQ2 (alpha1*0501, beta1*0201), which is present in
L Lorand et al.
Molecular and cellular biochemistry, 58(1-2), 9-35 (1984-01-01)
This paper is intended as a background to the topic of transglutaminases, while focusing on current ideas regarding the biological roles of these enzymes. Specifically, the following topics are discussed: geometry of forming gamma-glutamyl-epsilon-lysine cross-linked structures; energetic considerations; the gamma-glutamyl-epsilon-lysine
Mechanism of action of guinea pig liver transglutaminase. I. Purification and properties of the enzyme: identification of a functional cysteine essential for activity.
J E Folk et al.
The Journal of biological chemistry, 241(23), 5518-5525 (1966-12-10)
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Hello , how much grams are in one Unit Transglutaminase enzyme T5398 ? thanks very much kind regards Alex
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