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Pepsin from porcine gastric mucosa

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

Pepsin from hog stomach, Pepsin A
Número de CAS:
Comisión internacional de enzimas:
Número de EC:
Número MDL:

Nivel de calidad



lyophilized powder

specific activity

≥2,500 units/mg protein (E1%/280)

mol peso

35 kDa


off-white to yellow


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

Nº de acceso UniProt


diagnostic assay manufacturing

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.
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


250 mg in poly bottle
1, 5, 10, 25, 100 g in poly bottle

Acciones bioquímicas o fisiológicas

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.
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.
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 pH 2.0 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.
Protein determined by E1%/280

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

Certificado de Análisis

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Más documentos

Quotes and Ordering

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
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)
Chiara Zanoni et al.
Journal of agricultural and food chemistry, 65(40), 8829-8838 (2017-09-22)
This study had the objective of preparing a hempseed protein hydrolysate and investigating its hypocholesterolemic properties. The hydrolysate was prepared treating a total protein extract with pepsin. Nano HPLC-ESI-MS/MS analysis permitted identifying in total 90 peptides belonging to 33 proteins.
Dixon, M., et al.
Enzymes, 262-262 (1979)
Sambavy Nadaraja et al.
Acta oncologica (Stockholm, Sweden), 59(1), 40-47 (2019-09-04)
Background: Little is known about the biological factors influencing ovarian cancer (OC) patient outcome, especially in older patients who are often underrepresented in clinical trials. We examined alterations in the transcriptomic profile of primary high-grade serous carcinoma (HGSC) samples from


Enzymatic Assay of Pepsin (

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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