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P7125

Sigma-Aldrich

Pepsin from porcine gastric mucosa

powder, ≥400 units/mg protein

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Synonym(s):
Pepsin A, Pepsin from hog stomach
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
eCl@ss:
42010127
NACRES:
NA.54

biological source

Porcine gastric mucosa

Quality Level

form

powder

specific activity

≥400 units/mg protein

mol wt

35 kDa

solubility

10 mM HCl: soluble 1.0 mg/mL, clear to faintly turbid, colorless

UniProt accession no.

storage temp.

2-8°C

Gene Information

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This Item
P6887SRE0001516360
form

powder

form

lyophilized powder

form

lyophilized powder

form

lyophilized

specific activity

≥400 units/mg protein

specific activity

≥3,200 units/mg protein

specific activity

≥3200 units/mg protein

specific activity

≥2000 units/mg protein

mol wt

35 kDa

mol wt

35 kDa

mol wt

35 kDa

mol wt

-

solubility

10 mM HCl: soluble 1.0 mg/mL, clear to faintly turbid, colorless

solubility

deionized water: soluble 10 mg/mL, 10 mM HCl: soluble 4.0 mg/mL (Cold)

solubility

-

solubility

10 mM HCl: 0.5 mg/mL

UniProt accession no.

P00791

UniProt accession no.

P00791

UniProt accession no.

P00791

UniProt accession no.

-

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 P7125 is provided in powder form. Product P7125 has been used to denature DNA from kidney cells and to digest pathology samples from anal canal carcinomas (ACC) biopsies prior to EGFR staining.
The enzyme from Sigma has been used to obtain total vitamin B12 content in food products prior using immunoaffinity columns It has also been used to digest minced soft tissue of snails prior to the isolation of the third stage larvae (L3).
Pepsin cleavage can be used to produce F(ab′)2 fragments of antibodies. pepsin at www.sigma-aldrich.com/enzymeexplorer.

Biochem/physiol Actions

It 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

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 = 16 mL. Light path = 1 cm.)

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.
Protein determined by E1%/280

Other Notes

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

inhibitor

Product No.
Description
Pricing

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

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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.

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