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P0609

Sigma-Aldrich

Pepsin−Agarose from porcine gastric mucosa

lyophilized powder, ≥30 units/mg dry solid

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Synonym(s):
Pepsin A
Enzyme Commission number:
MDL number:
NACRES:
NA.54

biological source

Porcine gastric mucosa

Quality Level

form

lyophilized powder

specific activity

≥30 units/mg dry solid

mol wt

35 kDa

matrix

4% cross-linked beaded agarose

UniProt accession no.

storage temp.

−20°C

Gene Information

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

Signal Word

Danger

Hazard Statements

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

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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
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
Widya A Wahab et al.
International journal of experimental pathology, 97(4), 303-309 (2016-09-24)
Coeliac disease (CD) is an inflammatory disorder of the small intestine. It includes aberrant adaptive immunity with presentation of CD toxic gluten peptides by HLA-DQ2 or DQ8 molecules to gluten-sensitive T cells. A ω-gliadin/C-hordein peptide (QPFPQPEQPFPW) and a rye-derived secalin
Hana Dvořáková et al.
Frontiers in cellular and infection microbiology, 10, 66-66 (2020-03-17)
Schistosomula (the post-infective stages) of the neurotropic schistosome Trichobilharzia regenti possess multiple isoforms of cathepsin B1 peptidase (TrCB1.1-TrCB1.6) with involvement in nutrient digestion. The comparison of substrate preferences of TrCB1.1 and TrCB1.4 showed that TrCB1.4 had a very narrow substrate

Articles

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

Protocols

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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