P0861
Phospholipase A2 from porcine pancreas
≥10,000 unit/mL
Synonym(s):
Lecithinase A, PLA2, Phosphatidylcholine 2-acylhydrolase
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About This Item
CAS Number:
UNSPSC Code:
41106300
EC Number:
232-637-7
MDL number:
concentration
≥10,000 unit/mL
UniProt accession no.
storage temp.
2-8°C
Gene Information
pig ... PLA2G1B(445525)
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General description
A product of Novozyme Corp.
Biochem/physiol Actions
Hydrolyzes the β-ester bond of zwitterionic glycerophospholipids. Preferred substrates are phosphatidylcholine, phosphatidylethanolamine, and their plasmalogen analogues. Phosphatidylinositol and phosphatidylserine are also hydrolyzed. Aggressively attacks phospholipids in membranes of intact cells.
Other Notes
One unit is equivalent to the amount of enzyme producing 1 μmole of free fatty acid per minute at pH 8 and 40 °C.
Storage Class
13 - Non Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Willem van de Veen et al.
The Journal of allergy and clinical immunology, 131(4), 1204-1212 (2013-03-05)
IL-10-producing regulatory B cells suppress immune responses, and lack of these cells leads to exacerbated symptoms in mouse models of chronic inflammation, transplantation, and chronic infection. IgG4 is a blocking antibody isotype with anti-inflammatory potential that is induced in human
P K Larsson Forsell et al.
European journal of biochemistry, 262(2), 575-585 (1999-05-21)
Recently, we reported the human 88-kDa calcium-independent phospholipase A2 (iPLA2) cDNA sequence, as well as extensive alternative splicing of the iPLA2 mRNA. In this report we identified the gene coding for iPLA2, which was localized on chromosome 22q13.1. The gene
R Grataroli et al.
European journal of biochemistry, 122(1), 111-117 (1982-02-01)
Upon tryptic activation of pure human prophospholipase A2, a heptapeptide is released from the N-terminal part of the protein yielding active phospholipase A2 (EC 3.1.1.4). Both the kinetics of the activation process and the amino acid sequence of the activation
Cedric H De Smet et al.
Biochimica et biophysica acta, 1831(6), 1167-1176 (2013-03-19)
In the yeast Saccharomyces cerevisiae, the molecular species profile of the major membrane glycerophospholipid phosphatidylcholine (PC) is determined by the molecular species-selectivity of the biosynthesis routes and by acyl chain remodeling. Overexpression of the glycerol-3-phosphate acyltransferase Sct1p was recently shown
Petra Massoner et al.
PloS one, 8(2), e55207-e55207 (2013-02-08)
ERG gene rearrangements are found in about one half of all prostate cancers. Functional analyses do not fully explain the selective pressure causing ERG rearrangement during the development of prostate cancer. To identify transcriptional changes in prostate cancer, including tumors
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