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Merck

T5398

Sigma-Aldrich

Transglutaminase from guinea pig liver

lyophilized powder, ≥1.5 units/mg protein

Szinonimák:

Protein-Glutamine-γ-Glutamyltransferase, Protein-glutamine:amine γ-glutamyltransferase

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

CAS-szám:
Enzyme Commission szám:
MDL-szám:
UNSPSC kód:
12352204
NACRES:
NA.54

form

lyophilized powder

Minőségi szint

specifikus aktivitás

≥1.5 units/mg protein

molekulatömeg

76.6 kDa

összetétel

Protein, ≥80% modified Warburg-Christian

oldhatóság

H2O: soluble 1.0 mg/mL, clear

alkalmazás(ok)

diagnostic assay manufacturing

kiszállítva

dry ice

tárolási hőmérséklet

−20°C

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Alkalmazás

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. It has also been used to assess immune responses to A-gliadin peptides. Furthermore, it has been used to demonstrate that tTG selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease.
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.

Biokémiai/fiziológiai hatások

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. It is calcium dependent and has several calcium binding sites. The enzyme is inhibited by iodoacetamide and N-ethylmaleimide in the presence of calcium. 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.

Egység definíció

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.)

Fizikai forma

Lyophilized powder containing Tris and dithioerythritol

Piktogramok

Health hazard

Figyelmeztetés

Danger

Figyelmeztető mondatok

Óvintézkedésre vonatkozó mondatok

Veszélyességi osztályok

Resp. Sens. 1

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Egyéni védőeszköz

Eyeshields, Gloves, type N95 (US)


Analitikai tanúsítványok (COA)

Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.

Már rendelkezik ezzel a termékkel?

Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.

Dokumentumtár megtekintése

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
Syeda Warisul Fatima et al.
RSC advances, 11(55), 34613-34630 (2022-05-03)
Breast cancer is the most common malignancy among women. With the aim of decreasing the toxicity of conventional breast cancer treatments, an alternative that could provide appropriate and effective drug utilization was envisioned. Thus, we contemplated and compared the in
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)
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
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

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