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Merck

P6887

Pepsin from porcine gastric mucosa

lyophilized powder, ≥3,200 units/mg protein

동의어(들):

Pepsin A, Pepsin from hog stomach

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제품정보 (DICE 배송 시 비용 별도)

CAS 번호:
UNSPSC Code:
12352204
eCl@ss:
42010127
EC Number:
232-629-3
NACRES:
NA.54
MDL number:
EC 번호:
Specific activity:
≥3,200 units/mg protein
Biological source:
Porcine gastric mucosa
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biological source

Porcine gastric mucosa

grade

Proteomics Grade

form

lyophilized powder

specific activity

≥3,200 units/mg protein

mol wt

35 kDa

impurities

salt, essentially free

color

white to off-white

solubility

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

UniProt accession no.

application(s)

diagnostic assay manufacturing

shipped in

wet ice

storage temp.

−20°C

Quality Level

Gene Information

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Application

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.

Biochem/physiol Actions

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.

Analysis Note

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

Other Notes

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

pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

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

target_organs

Respiratory system

저장 등급

11 - Combustible Solids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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


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시험 성적서(COA)

Lot/Batch Number

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이 제품을 이미 가지고 계십니까?

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
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)
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
Enzymes of Molecular Biology
Sweeney, P.J., and Walker, J.M.
Methods in Molecular Biology, 290-291 (1993)

문서

사용 가능한 형광 동소 교잡법(FISH) 절차, 시약, 장비.

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

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

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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