Sie suchten nach: \u03B3-L-Glutamyl-p-nitroanilide+hydrochloride

Lieferant: Molekula

Beschreibung: L(-)-Glutathion (reduzierte Form)

Artikel-Nr: (PRSI33-944)

Lieferant: ProSci Inc.

Beschreibung: Involucrin is a highly reactive, soluble, transglutaminase substrate protein present in keratinocytes of epidermis and other stratified squamous epithelia. It first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase thus helping in the formation of an insoluble envelope beneath the plasma membrane functioning as a glutamyl donor during assembly of the cornified envelope. [Wiki].

VE: 1 * 100 µG

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Artikel-Nr: (786-15)

Lieferant: G-Biosciences

Beschreibung: SG-Glutamic-C™ is a serine endopeptidase, from<i> S. aureus V8</i>, that is highly specific for the cleavage of peptide bonds at the carboxy side of either aspartic or glutamic acid, depending on the buffer used. In Tris-HCl buffer, in particular in the absence of phosphate ions, the enzyme is specific for the glutamyl site. Recommended buffers for fragmentation of proteins using this enzyme are 50 mM Tris-HCI, pH 8,0 or bicarbonate buffer. Highly purified preparations of SG-Glutamic-C™ are chemically modified making the enzyme both resistant to autolysis and stabilises its enzymatic activity.

VE: 1 * 2 ST

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Artikel-Nr: (ENZOBMLZW93450005)

Lieferant: ENZO LIFE SCIENCES

Beschreibung: Fluorogenes Substrat für die Peptidyl-glutamyl-peptid-hydrolysierende (Caspase-ähnliche) Aktivität des Proteasoms, die in Gegenwart von Mg²⁺ stimuliert und schnell durch N-Acetylimidazol deaktiviert werden kann.

VE: 1 * 5 mg

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Lieferant: Merck

Beschreibung: Glutathion (reduziert) 98,0-101,0% (durch Iodometrie), EMPROVE® EXPERT Ph. Eur. für die biopharmazeutische Produktion, SAFC®

Lieferant: Merck

Beschreibung: L(-)-Glutathion (reduzierte Form), Sigma-Aldrich®

Lieferant: Merck

Beschreibung: L(-)-Glutathion (reduzierte Form), Sigma-Aldrich®

Artikel-Nr: (PRSI6537)

Lieferant: ProSci Inc.

Beschreibung: TGM5 Antibody: Transglutaminases (TGM) are a family of structurally and functionally related Ca2+-dependent enzymes (TGases) that stabilize protein assemblies through the formation of gamma-glutamyl-epsilon lysine crosslinks. TGases influence numerous biological processes, including blood coagulation, cell differentiation, fertilization and apoptosis. TGM5 belongs to the transglutaminase superfamily and catalyzes the cross-linking of proteins between glutamine and lysine residues, often resulting in stabilization of protein assemblies. TGM5 is also expressed in the human hair follicle. Defects in TGM5 are associated with acral peeling skin syndrome.

VE: 1 * 100 µG

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Lieferant: Merck

Beschreibung: L(-)-Glutathion (reduzierte Form), Sigma-Aldrich®

Artikel-Nr: (PRSI6541)

Lieferant: ProSci Inc.

Beschreibung: TGM7 Antibody: Transglutaminases (TGM) are a family of structurally and functionally related Ca2+-dependent enzymes (TGases) that stabilize protein assemblies through the formation of gamma-glutamyl-epsilon lysine crosslinks. TGases influence numerous biological processes, including blood coagulation, cell differentiation, fertilization and apoptosis. TGM7 belongs to the transglutaminase superfamily and is also thought to catalyze the cross-linking of proteins, often resulting in stabilization of protein assemblies. Little is known of the role of TGM7, but defects in the highly related protein TGM5 are associated with acral peeling skin syndrome.

VE: 1 * 100 µG

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Lieferant: Serva

Beschreibung: L(-)-Glutathion (reduzierte Form)

Artikel-Nr: (ICNA0215900905)

Lieferant: MP Biomedicals

Beschreibung: Alamethicin is a monovalent cation ionophore that can mimic nerve action potential across artificial membranes. It increases the incorporation of 32P into phosphatidylinositol 4-phosphate and sarcoplasmic reticulum vesicles permeability and causes fusion of lipid vesicles.

VE: 1 * 5 mg

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Lieferant: MP Biomedicals

Beschreibung: Preparation Method Produced from 3× crystallised chymotrypsinogen α-Chymotrypsin is used for treating pancreatic insufficiency and in traumatology. Chymotrypsin preferentially catalyses the hydrolysis of peptide bonds involving L-isomers of tyrosine, phenylalanine, and tryptophan. It also readily acts upon amides and esters of susceptible amino acids. In addition to bonds involving aromatic amino acids, chymotrypsin catalyses at a high rate the hydrolysis of bonds of leucyl, methionyl, asparaginyl, and glutamyl residues. a-Chymotrypsin is a protein consisting of 241 amino acid residues. The molecule has three peptide chains: an A chain of 13 residues, a B chain of 131 residues, and a C chain of 97 residues.

Zertifikate

Artikel-Nr: (SPCMGL146-25GM)

Lieferant: Spectrum Chemical

Beschreibung: L-Glutathione, Reduced can also be referred to as GSH and is an organic chemical that can be traced in plants and animals alike. It is an antioxidant that prevents damage from reactive oxygen species to cellular components that are important. It can be used to raise levels of plasma and liver GSH concentrations and is thought to have some positive effects on reducing cancer development.

VE: 1 * 25 mg

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Artikel-Nr: (PRSI25-736)

Lieferant: ProSci Inc.

Beschreibung: F13B contains 10 Sushi (CCP/SCR) domains. The B chain of factor XIII is not catalytically active, but is thought to stabilize the A subunits and regulate the rate of transglutaminase formation by thrombin. Defects in F13B can result in a lifelong bleeding tendency, defective wound healing, and habitual abortion.This gene encodes coagulation factor XIII B subunit. Coagulation factor XIII is the last zymogen to become activated in the blood coagulation cascade. Plasma factor XIII is a heterotetramer composed of 2 A subunits and 2 B subunits. The A subunits have catalytic function, and the B subunits do not have enzymatic activity and may serve as a plasma carrier molecules. Platelet factor XIII is comprised only of 2 A subunits, which are identical to those of plasma origin. Upon activation by the cleavage of the activation peptide by thrombin and in the presence of calcium ion, the plasma factor XIII dissociates its B subunits and yields the same active enzyme, factor XIIIa, as platelet factor XIII. This enzyme acts as a transglutaminase to catalyze the formation of gamma-glutamyl-epsilon-lysine crosslinking between fibrin molecules, thus stabilizing the fibrin clot. Factor XIII deficiency is classified into two categories: type I deficiency, characterized by the lack of both the A and B subunits; and type II deficiency, characterized by the lack of the A subunit alone. These defects can result in a lifelong bleeding tendency, defective wound healing, and habitual abortion. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

VE: 1 * 50 µG

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Lieferant: MP Biomedicals

Beschreibung: Storage: Store at +4 °C, store under nitrogen
Glutathione is the major low molecular weight thiol compound of the living plant or animal cell. It is a tripeptide with a gamma peptide linkage between the amine group of cysteine (which is attached by normal peptide linkage to a glycine) and the carboxyl group of the glutamate side-chain. It is an antioxidant, preventing damage to important cellular components caused by reactive oxygen species such as free radicals and peroxides. The sulfhydryl (thiol) group (SH) of cysteine serves as a proton donor and is responsible for the biological activity of glutathione.
Glutathione suppresses human immunodeficiency virus expression in chronically infected monocytic cells. It is a useful tripeptide involved in many aspects of metabolism, including transport of g-glutanyl amino acids and reductive cleavage of disulfide bonds.
Endogenous antioxidant that plays a major role in reducing reactive oxygen species formed during cellular metabolism and the respiratory burst. Glutathione-S-transferase catalyzes the formation of glutathione thioethers with xenobiotics, leukotrienes, and other molecules that have an electrophilic center. Glutathione also forms disulfide bonds with cysteine residues in proteins. Via these mechanisms, it can have the paradoxical effect of reducing the efficacy of anti-cancer agents.