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P7012

Sigma-Aldrich

Pepsin from porcine gastric mucosa

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

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Synonym(s):
Pepsin A, Pepsin from hog stomach
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
eCl@ss:
42010127
NACRES:
NA.54

form

lyophilized powder

Quality Level

specific activity

≥2,500 units/mg protein (E1%/280)

mol wt

35 kDa

color

off-white to yellow

solubility

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

UniProt accession no.

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

Gene Information

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This Item
SRE0001P7000P7125
specific activity

≥2,500 units/mg protein (E1%/280)

specific activity

≥3200 units/mg protein

specific activity

≥250 units/mg solid

specific activity

≥400 units/mg protein

mol wt

35 kDa

mol wt

35 kDa

mol wt

35 kDa

mol wt

35 kDa

color

off-white to yellow

color

white to off-white

color

-

color

-

solubility

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

solubility

-

solubility

-

solubility

10 mM HCl: soluble 1.0 mg/mL, clear to faintly turbid, colorless

UniProt accession no.

P00791

UniProt accession no.

P00791

UniProt accession no.

P00791

UniProt accession no.

P00791

Application

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.

Biochem/physiol Actions

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

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 = 16mL. Light path = 1cm.)

Analysis Note

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

Other Notes

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

inhibitor

Product No.
Description
Pricing

Pictograms

Exclamation markHealth hazard

Signal Word

Danger

Hazard Statements

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

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

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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