P0609
Pepsin−Agarose from porcine gastric mucosa
lyophilized powder, ≥30 units/mg dry solid
Sinónimos:
Pepsin A
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About This Item
Nombre del producto
Pepsin−Agarose from porcine gastric mucosa, lyophilized powder, ≥30 units/mg dry solid
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.
storage temp.
−20°C
Quality Level
Gene Information
pig ... LOC396892(396892)
Categorías relacionadas
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.
General description
Pepsin is an enzyme found in gastric secretion.
Other Notes
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.)
Physical form
Lyophilized powder stabilized with lactose
Preparation Note
One gram solid swells to 5-10ml packed gel.
signalword
Danger
hcodes
Hazard Classifications
Resp. Sens. 1
Clase de almacenamiento
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
dust mask type N95 (US), Eyeshields, Faceshields, 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
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