P7012
Pepsin from porcine gastric mucosa
lyophilized powder, ≥2,500 units/mg protein (E1%/280)
Synonym(s):
Pepsin A, Pepsin from hog stomach
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About This Item
Recommended Products
form
lyophilized powder
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
pig ... LOC396892(396892)
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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.
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
Signal Word
Danger
Hazard Statements
Precautionary 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
Certificates of Analysis (COA)
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A digestion technique for the reduction of background staining in the immunoperoxidase method.
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Journal of clinical pathology, 30(1), 88-90 (1977-01-01)
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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
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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.
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
Enzymes of Molecular Biology
Sweeney, P.J., and Walker, J.M.
Methods in Molecular Biology, 290-291 (1993)
Protocols
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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