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P6887

Sigma-Aldrich

Pepsin from porcine gastric mucosa

lyophilized powder, ≥3,200 units/mg protein

Synonym(s):

Pepsin A, Pepsin from hog stomach

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100 G
CN¥980.32
500 G
CN¥881.77
1 KG
CN¥1,593.12

CN¥980.32

Available to ship onApril 10, 2025Details

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100 G
CN¥980.32
500 G
CN¥881.77
1 KG
CN¥1,593.12

About This Item

CAS Number:
9001-75-6
EC Number:
3.4.23.1 (BRENDA, IUBMB)
EC Number:
232-629-3
MDL number:
MFCD00081840
UNSPSC Code:
12352204
eCl@ss:
42010127
NACRES:
NA.54

CN¥980.32

Available to ship onApril 10, 2025Details

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.

P00791

application(s)

diagnostic assay manufacturing

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Show Differences

1 of 4

This Item
E5134ED2SS27285
乙二胺四乙酸 二钠盐 二水合物 Sigma Grade, suitable for plant cell culture, 98.5-101.5%

E6635

乙二胺四乙酸 二钠盐 二水合物

乙二胺四乙酸 二钠盐 二水合物 suitable for electrophoresis, for molecular biology, 99.0-101.0% (titration)

E5134

乙二胺四乙酸 二钠盐 二水合物

乙二胺四乙酸 二钠盐 二水合物 reagent grade, 98.5-101.5% (titration)

ED2SS

乙二胺四乙酸 二钠盐 二水合物

乙二胺四乙酸 二钠盐 二水合物 meets analytical specification of Ph. Eur., BP, USP, FCC, 99.0-101.0%

27285

乙二胺四乙酸 二钠盐 二水合物

grade

Sigma Grade

grade

for molecular biology

grade

reagent grade

grade

-

assay

98.5-101.5%

assay

99.0-101.0% (titration)

assay

98.5-101.5% (titration)

assay

99.0-101.0%

Quality Level

200

Quality Level

300

Quality Level

200

Quality Level

200

mp

248 °C (dec.) (lit.)

mp

248 °C (dec.) (lit.)

mp

248 °C (dec.) (lit.)

mp

248 °C (dec.) (lit.)

solubility

H2O: soluble, clear, colorless

solubility

3  M NaOH: 1.6 g/10 mL

solubility

H2O: soluble, clear, colorless

solubility

water: soluble 100 g/L at 20 °C

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.[1] It has also been used to simulate in vitro gastrointestinal digestion of pea or whey protein isolates.[2]
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[3].

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.[4] Z-L-tyrosyl-L-phenylalanine, Z-L-glutamyl-L-tyrosine, or Z-L-methionyl-L-tyrosine may be used as substrates for pepsin digestion.[4][5] Pepsin is inhibited by several phenylalanine-containing peptides.[6]

Unit Definition

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.)

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

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

inhibitor

Product No.
Description
Pricing

Pictograms

Health hazardExclamation mark
GHS08,GHS07

Signal Word

Danger

Hazard Statements

H315,H319,H334,H335

Hazard Classifications

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

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

动植物源性产品
  • Specification Sheet

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    Certificates of Analysis (COA)

    Lot/Batch Number
    0000437291
    0000437289
    0000437287
    0000437286
    0000437287

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    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)
    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
    Enzymes of Molecular Biology
    Sweeney, P.J., and Walker, J.M.
    Methods in Molecular Biology, 290-291 (1993)
    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
    Arno G B Wouters et al.
    Journal of agricultural and food chemistry, 65(6), 1263-1271 (2017-01-27)
    The relationship between structural and foaming properties of two tryptic and two peptic wheat gluten hydrolysates was studied at different pH conditions. The impact of pH on foam stability (FS) of the samples heavily depended on the peptidase used and
    View All Related Papers

    Articles

    Antibody Fragmentation with Pepsin Digestion

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

    Fluorescent in situ Hybridization (FISH)

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

    Protocols

    Enzymatic Assay of Pepsin (3.4.23.1)

    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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