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P0609

Sigma-Aldrich

Pepsin−Agarose from porcine gastric mucosa

lyophilized powder, ≥30 units/mg dry solid

Synonym(s):

Pepsin A

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About This Item

Enzyme Commission number:
3.4.23.1 (BRENDA, IUBMB)
MDL number:
MFCD00081840
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Porcine gastric mucosa

form

lyophilized powder

specific activity

≥30 units/mg dry solid

mol wt

35 kDa

matrix

4% cross-linked beaded agarose

UniProt accession no.

P00791

storage temp.

−20°C

Gene Information

pig ... LOC396892(396892)

Related Categories

General description

Pepsin is an enzyme found in gastric secretion.

Application

Pepsin immobilized onto agarose beads can be used to digest and then separate out the active peptides of the glycoprotein gliadin.
Pepsin-agarose has been used as an immobilization tool to investigate the refolding ability of the pepsin enzyme. It has also been used for the preparation of F(ab′)2 fragments from rabbit IgG.
Used to produce F(ab′)2 fragments of antibodies.1

Biochem/physiol Actions

Preferentially cleaves C-terminal to Phe, Leu and Glu. It does not cleave at Val, Ala or Gly. pH optimum 2-4. Active in 4 M urea and 3 M guanidine HCl. Stable at 60 °C. Pepsin is irreversibly inactivated at pH > 6.

Unit Definition

One unit will produce a ΔA280 of 0.001 per min at pH 2.0 at 37 °C, measured as TCA-soluble products using hemoglobin as substrate. (Final volume = 16 mL. Light path = 1 cm.)

Quantity

One gram solid swells to 5-10ml packed gel.

Physical form

Lyophilized powder stabilized with lactose

inhibitor

Product No.
Description
Pricing

Pictograms

Health hazard
GHS08

Signal Word

Danger

Hazard Statements

H334

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

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M Feldman et al.
Gastroenterology, 110(4), 1043-1052 (1996-04-01)
Recent studies suggesting that gastric secretion does not decrease with aging included few elderly individuals and measured only acid secretion. The aims of this study were to measure gastric acid and pepsin output in 206 health Americans (age range, 18-98
Ludmila Tucková et al.
Journal of leukocyte biology, 71(4), 625-631 (2002-04-03)
Celiac disease, induced by dietary gluten, is characterized by mucosal atrophy and local inflammation associated with cell infiltration and activation. Unlike other food proteins, gluten and its proteolytic fragments, besides inducing a specific immune response, were shown to activate components
Thomas A Kraus et al.
The Journal of clinical investigation, 115(8), 2234-2243 (2005-07-26)
To explore the requirement for M cells and the Peyer's patch (PP) in induction of oral tolerance and address the potential in vivo role of intestinal epithelial cells as nonprofessional APCs, we have attempted to induce tolerance in mice with
Katrine Lindholm Bøgh et al.
International archives of allergy and immunology, 161(1), 21-36 (2012-12-22)
It is generally believed that protein hydrolysis in the gastrointestinal tract decreases the allergenicity of food allergens. However, it remains unknown if specific properties of digestion products determine whether a sensitisation or tolerogenic immune response will develop. We sought to
K L Bøgh et al.
Clinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology, 39(10), 1611-1621 (2009-08-20)
Food allergies are a public health issue of growing concern, with peanuts in particular being associated with severe reactions. The peanut allergen, Ara h 1, belongs to the cupin plant food allergen family, which, unlike other structural families, appears to
View All Related Papers

Articles

Antibody Fragmentation with Pepsin Digestion

Antibody fragmentation with our pepsin digestion protocol for IgG antibody fragmentation and preparation of F(ab’).

Protocols

Enzymatic Assay of Pepsin (3.4.23.1)

This procedure may be used for determination of Pepsin activity using hemoglobin as the substrate. It is a spectrophotometric stop rate determination.

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