SRE0001
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:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-629-3
MDL number:
Specific activity:
≥3200 units/mg protein
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
Quality Level
Gene Information
pig ... LOC396892(396892)
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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
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
Other Notes
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.)
View more information on pepsin at www.sigma-aldrich.com/enzymeexplorer.
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
低风险生物材料
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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
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
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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