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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)

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
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
F Halter et al.
The Yale journal of biology and medicine, 69(1), 99-104 (1997-01-01)
Chronic Helicobacter pylori infection causes a slight postprandial hypergastinemia, generally referred to as exaggerated or inappropriate gastrin release. This can be ablated by eradication of this infective agent. The expectations that this would further unravel the mysteries of the pathogenesis
Autonomic control of secretion of gastric acid and pepsin.
K Bech
Journal of autonomic pharmacology, 9(6), 419-428 (1989-12-01)
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

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