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Merck
모든 사진(6)

주요 문서

P6887

Sigma-Aldrich

Pepsin from porcine gastric mucosa

lyophilized powder, ≥3,200 units/mg protein

동의어(들):

Pepsin A, Pepsin from hog stomach

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About This Item

CAS Number:
효소 위원회 번호:
EC Number:
MDL number:
UNSPSC 코드:
12352204
eCl@ss:
42010127
NACRES:
NA.54

생물학적 소스

Porcine gastric mucosa

Quality Level

Grade

Proteomics Grade

양식

lyophilized powder

특이 활성도

≥3,200 units/mg protein

분자량

35 kDa

불순물

salt, essentially free

색상

white to off-white

solubility

deionized water: soluble 10 mg/mL
10 mM HCl: soluble 4.0 mg/mL (Cold)

UniProt 수납 번호

응용 분야

diagnostic assay manufacturing

배송 상태

wet ice

저장 온도

−20°C

유전자 정보

유사한 제품을 찾으십니까? 방문 제품 비교 안내

애플리케이션

Pepsin cleavage can be used to produce F(ab′)2 fragments of antibodies. pepsin at www.sigma-aldrich.com/enzymeexplorer.
Pepsin from Sigma has been used along with other enzymes for the determination of enzyme-resistant starch (RS) in bread. It has also been used to simulate in vitro gastrointestinal digestion of pea or whey protein isolates.
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. Product P6887 is provided as a lyophilized powder and has been used to digest protein during dietary fiber analysis.

생화학적/생리학적 작용

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
Unlike many other peptidases, pepsin hydrolyzes only peptide bonds, not amide or ester linkages. The cleavage specificity includes peptides with an aromatic acid on either side of the peptide bond, especially if the other residue is also an aromatic or a dicarboxylic amino acid. Increased susceptibility to hydrolysis occurs if there is a sulfur-containing amino acid close to the peptide bond, which has an aromatic amino acid. Pepsin will also preferentially cleave at the carboxyl side of phenylalanine and leucine, and to a lesser extent at the carboxyl side of glutamic acid residues. It 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.

단위 정의

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 = 16 ml. Light path = 1 cm.)

분석 메모

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

기타 정보

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

저해제

제품 번호
설명
가격

픽토그램

Health hazardExclamation mark

신호어

Danger

유해 및 위험 성명서

Hazard Classifications

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

표적 기관

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point (°F)

Not applicable

Flash Point (°C)

Not applicable

개인 보호 장비

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


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시험 성적서(COA)

Lot/Batch Number

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문서 라이브러리에서 최근에 구매한 제품에 대한 문서를 찾아보세요.

문서 라이브러리 방문

J A Marlett et al.
The American journal of clinical nutrition, 50(3), 479-485 (1989-09-01)
The effects of different methods on the distribution of total neutral sugars (TNS), uronic acids (UA), and beta-glucans (beta G) between the soluble (S) and insoluble (I) fractions of dietary fiber (DF) were determined for peas, kidney beans, oat bran
V Vermeirssen et al.
Journal of dairy science, 86(2), 429-438 (2003-03-22)
Pea and whey protein were fermented by Lactobacillus helveticus and Saccharomyces cerevisiae in monoculture and in combination at 28 and 37 degrees C in order to release angiotensin-I-converting enzyme (ACE) inhibitory peptides. The fermentation products were subjected to in vitro
Enzyme-resistant starch. III. The quality of straight-dough bread containing varying levels of enzyme-resistant starch.
Eerlingen, R. C., et al.
Cereal Chem., 71(2), 165-169 (1994)
Dixon, M., et al.
Enzymes, 262-262 (1979)
Oksana Lockridge et al.
The Journal of biological chemistry, 283(33), 22582-22590 (2008-06-26)
Human albumin is thought to hydrolyze esters because multiple equivalents of product are formed for each equivalent of albumin. Esterase activity with p-nitrophenyl acetate has been attributed to turnover at tyrosine 411. However, p-nitrophenyl acetate creates multiple, stable, acetylated adducts

문서

Antibody fragmentation with our pepsin digestion protocol for IgG antibody fragmentation and preparation of F(ab’).

사용 가능한 형광 동소 교잡법(FISH) 절차, 시약, 장비.

Available Fluorescent in situ hybridization (FISH) procedures, reagents and equipment.

프로토콜

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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