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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

Synonym(s):

Pepsin A, Pepsin from hog stomach

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

Quality Level

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.

application(s)

diagnostic assay manufacturing

shipped in

wet ice

storage temp.

−20°C

Gene Information

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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

Health hazardExclamation mark

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


Certificates of Analysis (COA)

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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
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
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
J Tack
Alimentary pharmacology & therapeutics, 22 Suppl 1, 48-54 (2005-07-27)
Gastro-oesophageal reflux disease is defined as the presence of symptoms or lesions that can be attributed to the reflux of gastric contents into the oesophagus. Aspiration and prolonged monitoring studies in humans have shown that reflux of gastric contents is

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