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Pepsin from porcine gastric mucosa

powder, ≥250 units/mg solid

Pepsin A, Pepsin from hog stomach
CAS Number:
Enzyme Commission number:
Número de EC:
Número MDL:

origen biológico

Porcine gastric mucosa

Nivel de calidad




specific activity

≥250 units/mg solid

mol peso

35 kDa

Nº de acceso UniProt


diagnostic assay manufacturing

enviado en

wet ice

temp. de almacenamiento


Gene Information

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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[1].
The enzyme from Sigma has been used to simulate in vitro gastric digestion of cooked cod.[2] It has been used to simulate in vitro gastric digestion of cocoa mass and supplemented dietary fiber.[3] 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.[4]
Pepsin cleavage can be used to produce F(ab′)2 fragments of antibodies. pepsin at


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

Acciones bioquímicas o fisiológicas

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.[5].
The enzyme does not cleave at valine, alanine, or glycine linkages.[6] Z-L-tyrosyl-L-phenylalanine, Z-L-glutamyl-L-tyrosine, and Z-L-methionyl-L-tyrosine may be used as substrates for pepsin digestion.[7][6] Pepsin is inhibited by several phenylalanine-containing peptides.[8]
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

Definición de unidad

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.)

Nota de análisis

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.

Otras notas

View more information on pepsin at


Exclamation markHealth hazard

Palabra de señalización


Frases de peligro

Clasificaciones de peligro

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

Órganos de actuación

Respiratory system

Código de clase de almacenamiento

11 - Combustible Solids



Punto de inflamabilidad F

Not applicable

Punto de inflamabilidad C

Not applicable

Equipo de protección personal

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

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