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SRE0001

Sigma-Aldrich

Pepsin from porcine gastric mucosa

Suitable for manufacturing of diagnostic kits and reagents, lyophilized powder, ≥3200 units/mg protein

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Synonym(s):
Pepsin A, Pepsin from hog stomach
CAS Number:
9001-75-6
Enzyme Commission number:
3.4.23.1 (BRENDA, IUBMB)
EC Number:
232-629-3
MDL number:
MFCD00081840
NACRES:
NA.54

Quality Level

400

form

lyophilized powder

specific activity

≥3200 units/mg protein

mol wt

35 kDa

impurities

salt, essentially free

color

white to off-white

UniProt accession no.

P00791

application(s)

diagnostic assay manufacturing

shipped in

wet ice

storage temp.

−20°C

Gene Information

pig ... LOC396892(396892)

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Application

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

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

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.)

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
GHS07,GHS08

Signal Word

Danger

Hazard Statements

H315 - H319 - H334 - H335

Precautionary Statements

P302 + P352 - P305 + P351 + P338

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

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Adrian Allen et al.
American journal of physiology. Cell physiology, 288(1), C1-19 (2004-12-14)
Secretion of bicarbonate into the adherent layer of mucus gel creates a pH gradient with a near-neutral pH at the epithelial surfaces in stomach and duodenum, providing the first line of mucosal protection against luminal acid. The continuous adherent mucus
Tina L Samuels et al.
The Annals of otology, rhinology, and laryngology, 119(3), 203-208 (2010-04-16)
Diagnosis of extraesophageal reflux (EER) currently relies on tools designed for diagnosis of gastroesophageal reflux. Such tools lack the sensitivity and reproducibility to detect the less frequent and mildly acidic reflux associated with upper airway disease. Pepsin has been posited
Yi Sun et al.
Journal of natural products, 77(7), 1749-1752 (2014-06-25)
Two linear peptides, ahpatinin Ac (1) and ahpatinin Pr (2), were isolated together with the known ahpatinin (i)Bu, pepstatin Ac, pepstatin Pr, and pepsinostreptin from a Streptomyces sp. derived from a deep-sea sediment. The structure of ahpatinin Pr (2) was
B I Hirschowitz
The Yale journal of biology and medicine, 72(2-3), 133-143 (2000-04-26)
Esophagitis results from excessive exposure of the esophagus to gastric juice through an ineffective or dysfunctional lower esophageal sphincter mechanism. A possible role of pepsin in damaging the esophageal mucosa with consequent esophagitis may be examined directly by testing pepsin
Michal Ciolkowski et al.
Biochimica et biophysica acta, 1834(10), 1982-1987 (2013-07-16)
In this study the ability of three polyamidoamine (PAMAM) dendrimers with different surface charge (positive, neutral and negative) to interact with a negatively charged protein (porcine pepsin) was examined. It was shown that the dendrimer with a positively charged surface
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