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T6424

Sigma-Aldrich

Trypsin from human pancreas

salt-free, lyophilized powder, vial of ≥1,000 BAEE units

Sinônimo(s):

Serine Protease 1

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About This Item

Número CAS:
9002-07-7
Número da licença da enzima:
3.4.21.4 (BRENDA, IUBMB)
Número CE:
232-650-8
Número MDL:
MFCD01323069
Código UNSPSC:
12352204
NACRES:
NA.54

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fonte biológica

human pancreas

Nível de qualidade

200

Formulário

salt-free, lyophilized powder

embalagem

vial of ≥1,000 BAEE units

nº de adesão UniProt

P07477
P07478
P35030

temperatura de armazenamento

−20°C

Informações sobre genes

human ... PRSS1(5644) , PRSS2(5645) , PRSS3(5646)

Categorias relacionadas

Descrição geral

The trypsin molecule has two domains: one is related to the enzyme active site and the tryptophan residues; the other is related to the 8-anilinonaphthalene-1-sulfonate binding.
Trypsin is a serine protease. The pancreas produce the precursor trypsinogen and secretes it to the intestine. Trypsinogen is converted to trypsin by enterokinase in the intestinal mucous membrane.[1]

Aplicação

Trypsin has been used in a study to assess the similarities between the hepatitis E virus and human astrovirus. [2] Trypsin has also been used in a study to characterize a unique technique for culturing primary adult human epithelial progenitor, or stem, cells. [3]

Definição da unidade

One BAEE unit will produce a ΔA253 of 0.001 per min at pH 7.6 at 25 °C using BAEE as substrate. Reaction volume = 3.2 mL (1 cm light path).

Quantidade

Minimum 1,000 BAEE units/vial

Nota de análise

Protein determined by E1%/280.

Outras notas

View more information on trypsin at www.sigma-aldrich.com/enzymeexplorer

Inibidor

Nº do produto
Descrição
Preços

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Trypsin inhibitor from Glycine max (soybean), lyophilized powder

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D7910

3,4-Dichloroisocoumarin, serine protease inhibitor

D0879

Diisopropylfluorophosphate

L2023

Leupeptin trifluoroacetate salt, ≥90% (HPLC), microbial

A6191

Antipain dihydrochloride from microbial source, protease inhibitor

T9777

Trypsin-chymotrypsin inhibitor from Glycine max (soybean), lyophilized powder

A1153

Aprotinina, lyophilized powder, 3-8 TIU/mg solid

P7626

Fluoreto de fenilmetanosulfonil, ≥98.5% (GC)

A9024

α1-Antitrypsin from human plasma, salt-free, lyophilized powder

A6150

α1-Antitrypsin from human plasma, salt-free, lyophilized powder

T2011

Trypsin inhibitor from chicken egg white, Type III-O (free of ovoinhibitor)

substrato

Nº do produto
Descrição
Preços

Pictogramas

Health hazardExclamation mark
GHS08,GHS07

Palavra indicadora

Danger

Frases de perigo

H315,H319,H334,H335

Classificações de perigo

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

Órgãos-alvo

Respiratory system

Código de classe de armazenamento

11 - Combustible Solids

Classe de risco de água (WGK)

WGK 1

Equipamento de proteção individual

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

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Certificados de análise (COA)

Lot/Batch Number
0000426761
0000426761
0000376372
0000330530
0000376372

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Jia Liu et al.
Nature protocols, 16(7), 3522-3546 (2021-06-06)
Cellular heterogeneity is pervasive and of paramount importance in biology. Single-cell analysis techniques are indispensable for understanding the heterogeneity and functions of cells. Low-copy-number proteins (fewer than 1,000 molecules per cell) perform multiple crucial functions such as gene expression, cellular
Kelly A Dryden et al.
Journal of molecular biology, 422(5), 650-658 (2012-06-30)
Human astroviruses (HAstVs) are a major cause of gastroenteritis. HAstV assembles from the structural protein VP90 and undergoes a cascade of proteolytic cleavages. Cleavage to VP70 is required for release of immature particles from cells, and subsequent cleavage by trypsin
Cynthia Luz Marcelo et al.
BMC dermatology, 12, 8-8 (2012-06-26)
Primary keratinocytes derived from epidermis, oral mucosa, and urothelium are used in construction of cell based wound healing devices and in regenerative medicine. This study presents in vitro technology that rapidly expands keratinocytes in culture by growing monolayers under large
Industrial Enzymes and Their Applications (1998)
R J Read et al.
Biochemistry, 23(26), 6570-6575 (1984-12-18)
The X-ray crystal structure of Streptomyces griseus trypsin has been solved and refined at 1.7-A resolution. The structure of this protein had been predicted in two models on the basis of its expected homology to structures of bovine trypsin and
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Protocolos

Trypsin Assay Procedure (EC 3.4.21.4)

Continuous spectrophotometric rate determination method using BAEE substrate measures trypsin activity, essential for enzyme characterization.

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