Pular para o conteúdo
Merck
Todas as fotos(1)

Key Documents

T1143

Sigma-Aldrich

Trypsinogen from bovine pancreas

essentially salt-free, lyophilized powder, ≥10,000 BAEE units/mg protein (E1%/280, after activation to trypsin)

Faça loginpara ver os preços organizacionais e de contrato


About This Item

Número CAS:
Número CE:
Código UNSPSC:
12352202
NACRES:
NA.56

fonte biológica

bovine pancreas

Ensaio

85-100% (UV)

forma

essentially salt-free, lyophilized powder

atividade específica

≥10,000 BAEE units/mg protein (E1%/280, after activation to trypsin)

peso molecular

23,981 Da by calculation

técnica(s)

mass spectrometry (MS): suitable

solubilidade

H2O: soluble 10 mg/mL

nº de adesão UniProt

temperatura de armazenamento

−20°C

Informações sobre genes

bovine ... TRYP8(282603)

Procurando produtos similares? Visita Guia de comparação de produtos

Descrição geral

Trypsinogen is a proenzyme (zymogen) that is activated to form trypsin. It is synthesized in the pancreas and activated by enterokinase once it reaches the lumen of the small intestine. Bovine trypsinogen is a single polypeptide chain of 229 amino acids that is cross linked by six disulfide bridges. Enterokinase cleaves a hexapeptide to from the NH2 terminus of trypsinogen at the Lys6 - Ile7 peptide bond and activates it. Trypsin, thus formed, autocatalytically activates more trypsinogen to trypsin. This native form of trypsin is called β-trypsin, which undergoes autolysis at Lys131 - Ser132 resulting in α-trypsin that is held together by disulfide bridges. Trypsin is a serine protease with His46 and Ser183 at the active site. The pH optimum of trypsin is 7 - 9.

Aplicação

Trypsinogen from bovine pancreas is suitable for use in:
  • the secondary structure analysis of proteins in H2O solution using single-pass attenuated total reflection Fourier transform infrared (ATR-FT-IR) microscopy
  • tuning and calibration of electrospray ionization quadrupole time-of-flight (ESI-Q-TOF) mass spectrometer
  • the secondary structure analysis of proteins by infrared (IR) spectroscopy
  • SDS-PAGE as a molecular weight standard (24kDa)

Ações bioquímicas/fisiológicas

Phytic acid complexed with calcium has been shown to increase the secretion of trypsinogen unable to be cleaved for activation. It also reduced the stabilization effect of calcium on activated trypsin. The active form of trypsinogen, referred to as trypsin, cleaves peptides on the C-terminal side of lysine and arginine amino acid residues. It also hydrolyzes ester and amide linkages of synthetic derivatives of amino acids such as, benzoyl L-arginine ethyl ester (BAEE), p-toluenesulfonyl-L-arginine methyl ester (TAME), etc.

Definição da unidade

One BAEE unit is equal to a ΔA253 of 0.001 per min with BAEE as substrate at pH 7.6 at 25 °C and a reaction volume of 3.2 mL (1 cm light path).

Pictogramas

Health hazard

Palavra indicadora

Danger

Frases de perigo

Classificações de perigo

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Faceshields, Gloves, type N95 (US)


Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

Já possui este produto?

Encontre a documentação dos produtos que você adquiriu recentemente na biblioteca de documentos.

Visite a Biblioteca de Documentos

Os clientes também visualizaram

Slide 1 of 5

1 of 5

Keil B, et al.
The Enzymes, 3, 250-275 null
Evidence for an active center histidine in trypsin through use of a specific reagent, 1-chloro-3-tosylamido-7-amino-2-heptanone, the chloromethyl ketone derived from Nα-tosyl-L-lysine.
Shae E, et al.
Biochemistry, 4, 2219-2224 (1965)
Trypsinogens and trypsins of various species.
Walsh K A, et al.
Methods in Enzymology, 19, 41-63 (1970)
An effect of calcium ions on the activity, heat stability, and structure of trypsin.
T Sipos et al.
Biochemistry, 9(14), 2766-2775 (1970-07-07)
TRYPSINOGEN AND CHYMOTRYPSINOGEN AS HOMOLOGOUS PROTEINS.
K A WALSH et al.
Proceedings of the National Academy of Sciences of the United States of America, 52, 884-889 (1964-10-01)

Protocolos

Enzymatic Assay of Urease from Jack Beans

Nossa equipe de cientistas tem experiência em todas as áreas de pesquisa, incluindo Life Sciences, ciência de materiais, síntese química, cromatografia, química analítica e muitas outras.

Entre em contato com a assistência técnica