Ugrás a tartalomra
Merck

P7012

Sigma-Aldrich

Pepsin from porcine gastric mucosa

lyophilized powder, ≥2,500 units/mg protein (E1%/280)

Szinonimák:

Pepsin A, Pepsin from hog stomach

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

CAS-szám:
Enzyme Commission szám:
EC-szám:
MDL-szám:
UNSPSC kód:
12352204
eCl@ss:
42010127
NACRES:
NA.54

Forma

lyophilized powder

Minőségi szint

specifikus aktivitás

≥2,500 units/mg protein (E1%/280)

molekulatömeg

35 kDa

szín

off-white to yellow

oldhatóság

deionized water: soluble 10 mg/mL
10 mM HCl: soluble 4 mg/mL (Cold)

UniProt elérési szám

alkalmazás(ok)

diagnostic assay manufacturing

tárolási hőmérséklet

−20°C

Géninformáció

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Alkalmazás

Pepsin is a peptidase used to digest proteins and is commonly used in the preparation of Fab fragments from antibodies. Pepsin, from porcine gastric mucosa, has been used to hydrolyze dry cervical samples in mice.
The enzyme from Sigma has been used in the digestion of crude wheat gliadin. It has been used along with other enzymes to demonstrate the effects of fixation and enzymatic digestion in immunohistochemical assays, using paraffin embedded tissue. It has been used for digestion (before using immunoperoxidase techniques) to reduce non-specific background staining in sections of bronchial tissues. The enzyme has also been used in the preparation of F(ab)2 fragment from IgG.
Pepsin cleavage can be used to produce F(ab′)2 fragments of antibodies. pepsin at www.sigma-aldrich.com/enzymeexplorer.

Biokémiai/fiziológiai hatások

Pepsin hydrolyzes peptide bonds, not amide or ester linkages. Pepsin cleaves peptides with an aromatic acid on either side of the peptide bond. Sulfur-containing amino acids increase susceptibility to hydrolysis when they are close to the peptide bond. Pepsin preferentially cleaves at the carboxyl side of phenylalanine and leucine and at the carboxyl side of glutamic acid residues. Cleaves Phe-Val, Gln-His, Glu-Ala, Ala-Leu, Leu-Tyr, Tyr-Leu, Gly-Phe, Phe-Phe and Phe-Tyr bonds in the β chain of insulin
Pepsin is the major proteolytic enzyme produced in the stomach. It digests proteins through the cleavage of interior peptide linkages.
The enzyme does not cleave at valine, alanine, or glycine linkages. Z-L-tyrosyl-L-phenylalanine, Z-L-glutamyl-L-tyrosine, or Z-L-methionyl-L-tyrosine may be used as substrates for pepsin digestion. Pepsin is inhibited by several phenylalanine-containing peptides.
Preferential cleavage: hydrophobic and aromatic residues in P1 and P1′ postitions. Cleaves Phe-Val, Gln-His, Glu-Ala, Ala-Leu, Leu-Tyr, Tyr-Leu, Gly-Phe, Phe-Phe and Phe-Tyr bonds in the β chain of insulin

Egység definíció

One unit will produce a ΔA280 of 0.001 per min at pH 2.0 at 37°C, measured as TCA-soluble products using hemoglobin as substrate. (Final volume = 16mL. Light path = 1cm.)

Analízis megjegyzés

E1%/280=14.7
Optimum pH is 2-4. Active in 4 M urea and 3 M guanidine HCl. Stable at 60 °C. Pepsin is irreversibly inactivated at pH 8.0 - 8.5.
Protein determined by E1%/280

Egyéb megjegyzések

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

Gátló

Product No.
Leírás
Árazás

Piktogramok

Health hazardExclamation mark

Figyelmeztetés

Danger

Figyelmeztető mondatok

Veszélyességi osztályok

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

Célzott szervek

Respiratory system

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable

Egyéni védőeszköz

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


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Analitikai tanúsítványok (COA)

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Dokumentumtár megtekintése

P Kirkpatrick et al.
Journal of clinical pathology, 37(6), 639-644 (1984-06-01)
The effects of different fixatives and enzymatic digestion procedures on the immunohistochemical demonstration of fibronectin and laminin in paraffin embedded tissues have been compared. None of the fixatives tested enabled staining of these proteins without enzymatic digestion. No intracytoplasmic laminin
A digestion technique for the reduction of background staining in the immunoperoxidase method.
M Reading
Journal of clinical pathology, 30(1), 88-90 (1977-01-01)
S B Halstead et al.
The Journal of experimental medicine, 146(1), 201-217 (1977-07-01)
Cultured mononuclear peripheral blood leukocytes (PBL) from nonimmune human beings and monkeys are nonpermissive to dengue 2 virus (D2V) infection at multiplicities of infection of 0.001-0.1, but become permissive when non-neutralizing dengue antibody is added to medium. D2V infection occurred
Chiara Zanoni et al.
Journal of agricultural and food chemistry, 65(40), 8829-8838 (2017-09-22)
This study had the objective of preparing a hempseed protein hydrolysate and investigating its hypocholesterolemic properties. The hydrolysate was prepared treating a total protein extract with pepsin. Nano HPLC-ESI-MS/MS analysis permitted identifying in total 90 peptides belonging to 33 proteins.
Charles P Read et al.
Reproduction (Cambridge, England), 134(2), 327-340 (2007-07-31)
Cervical remodeling during pregnancy and parturition is a single progressive process that can be loosely divided into four overlapping phases termed softening, ripening, dilation/labor, and post partum repair. Elucidating the molecular mechanisms that facilitate all phases of cervical remodeling is

Protocols

This procedure may be used for determination of Pepsin activity using hemoglobin as the substrate. It is a spectrophotometric stop rate determination.

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