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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:
9001-75-6
Enzyme Commission number:
3.4.23.1 (BRENDA, IUBMB)
EC Number:
232-629-3
MDL number:
MFCD00081840
UNSPSC Code:
12352204
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

Health hazardExclamation mark
GHS08,GHS07

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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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
Joseph S Fruton
The Quarterly review of biology, 77(2), 127-147 (2002-07-02)
Studies on gastric digestion during 1820-1840 led to the discovery of pepsin as the agent which, in the presence of stomach acid, causes the dissolution of nutrients such as meat or coagulated egg white. Soon afterward it was shown that
Shenlin Wang et al.
The Journal of biological chemistry, 289(2), 697-707 (2013-11-23)
Multidomain protein folding is often more complex than a two-state process, which leads to the spontaneous folding of the native state. Pepsin, a zymogen-derived enzyme, without its prosegment (PS), is irreversibly denatured and folds to a thermodynamically stable, non-native conformation
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
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