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P7000

Sigma-Aldrich

Pepsin from porcine gastric mucosa

powder, ≥250 units/mg solid

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

biological source

Porcine gastric mucosa

Quality Level

form

powder

specific activity

≥250 units/mg solid

mol wt

35 kDa

UniProt accession no.

application(s)

diagnostic assay manufacturing

shipped in

wet ice

storage temp.

2-8°C

Gene Information

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Related Categories

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. Product P7000 is provided as a powder and has been used to treat epithelial cells from a single feline mammary carcinoma[48].
The enzyme from Sigma has been used to simulate in vitro gastric digestion of cooked cod.[42] It has been used to simulate in vitro gastric digestion of cocoa mass and supplemented dietary fiber.[43] It has also been used to increase the fraction of extractable soluble collagen and to lower the immunogenicity of the resulting collagen from bovine dermal tissue.[44]
Pepsin cleavage can be used to produce F(ab′)2 fragments of antibodies. pepsin at www.sigma-aldrich.com/enzymeexplorer.

Packaging

25, 100 g in poly bottle
1 kg in poly bottle

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.
[38].
The enzyme does not cleave at valine, alanine, or glycine linkages.[46] Z-L-tyrosyl-L-phenylalanine, Z-L-glutamyl-L-tyrosine, and Z-L-methionyl-L-tyrosine may be used as substrates for pepsin digestion.[45][46] Pepsin is inhibited by several phenylalanine-containing peptides.[02]
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 pH2.0 at 37 °C, measured as TCA-soluble products using hemoglobin as substrate. (Final volume = 16ml. Light path = 1cm.)

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.

Other Notes

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

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

Certificate of Analysis

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Certificate of Origin

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