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P7000 Sigma

Pepsin from porcine gastric mucosa

powder, ≥250 units/mg solid

Synonym: Pepsin A, Pepsin from hog stomach

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Properties

Related Categories 3.4.x.x Peptidases, 3.x.x.x Hydrolases, Application Index, Biochemicals and Reagents, Clinical Chemistry,
material   light beige
  off-white to light yellow
form   powder
mol wt   mol wt 35 kDa
solubility   10 mM HCl: soluble1.0 mg/mL, clear to faintly turbid, colorless
Featured Industry   Diagnostic Assay Manufacturing
shipped in   wet ice
storage temp.   2-8°C
Gene Information   pig ... LOC396892(396892)

Description

Frequently Asked Questions

Frequently Asked Questions are available for this Product.

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.

Application

Pepsin cleavage can be used to produce F(ab′)2 fragments of antibodies. pepsin at www.sigma-aldrich.com/enzymeexplorer.

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.

The enzyme from Sigma has been used to simulate in vitro gastric digestion of cooked cod. It has been used to simulate in vitro gastric digestion of cocoa mass and supplemented dietary fiber. 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.

Biochem/physiol Actions

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

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, and Z-L-methionyl-L-tyrosine may be used as substrates for pepsin digestion. Pepsin is inhibited by several phenylalanine-containing peptides.

Other Notes

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

Packaging

1 kg in poly bottle

25, 100 g in poly bottle

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.)

Price and Availability

Suggested Laboratory Gloves


Laboratory GlovesThis substance has been tested against several types of hand protection for CE compliance. Click below to find the recommended gloves for handling this product.




Available in ELITE Grade
Safety & Documentation

Safety Information

Symbol 
Signal word 
Danger
Hazard statements 
Precautionary statements 
Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
1
RTECS 
SC6132000

Documents

Certificate of Analysis

Certificate of Origin

Protocols & Articles

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.

Related Content

Enzymes & Proteins

Application Index | Enzyme Index | Substrate Index | Inhibitor Index | Cofactor Index | Lectin Index
Keywords: Cell signaling, Diagnostic, Drug discovery, Molecular biology

Peer-Reviewed Papers
15

References

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