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SAB4200129

Sigma-Aldrich

Anti-Phospholipase A2 (iPLA2) antibody produced in rabbit

~1.5 mg/mL, affinity isolated antibody

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Synonym(s):
Anti-CaI-PLA2, Anti-GVI, Anti-INAD1, Anti-IPLA2-VIA, Anti-PARK14, Anti-PLA2, Anti-PLA2G6, Anti-PNPLA9, Anti-Phospholipase A2, group VI (cytosolic, calcium-independent), Anti-iPLA2
MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

~85 kDa (and ~95 kDa human iPLA2 and ~95 kDa mouse and rat iPLA2.)

species reactivity

human, mouse, rat

concentration

~1.5 mg/mL

technique(s)

western blot: 1.5-3.0 μg/mL using using extracts of HEK-293T cells overexpressing human iPLA2, RAW264 cell lysates and rat pancreas extracts (S1 fraction).

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PLA2G6(8398)
mouse ... pla2g6(53357)
rat ... pla2g6(360426)

Related Categories

General description

Calcium-independent phospholipase A2 (iPLA2) belongs to the group six of phospholipase A2 (PLA2) enzymes. The protein is encoded by the gene mapped to human chromosome 22q13.1. iPLA2 is an intracellular enzyme. It is present both in the cytosol and in membrane fractions. The encoded protein contains 752 amino acids and has a mass of 85kDa. It is characterized with a eight ankyrin repeats and a catalytic domain.

Application

Anti-Phospholipase A2 (iPLA2) antibody produced in rabbit has been used in western blotting.

Biochem/physiol Actions

Calcium-independent phospholipase A2 (iPLA2) in the absence of Ca2+, catalyzes the hydrolysis of the Sn-2 ester bond in phospholipids to produce free fatty acids and lysophospholipids. iPLA2 might play an essential role in activating the receptor-mediated signaling pathway. Additionally, it also yields precursors for bioactive compounds such as eicosanoid and platelet-activating factor. The encoded protein performs housekeeping role in phospholipid remodeling.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

常规特殊物品

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Phospholipase A2 enzymes: physical structure, biological function, disease implication, chemical inhibition, and therapeutic intervention.
Dennis EA
Chemical Reviews, 111, 6130-6185 (2011)
Cellular Function of Calcium-Independent Phospholipase A2
AKIBA S and SATO T
Biological & Pharmaceutical Bulletin, 27, 1174?1178-1174?1178 (2004)
Human Pancreatic Islets Express mRNA Species Encoding Two Distinct Catalytically Active Isoforms of Group VI Phospholipase A2 (iPLA2) That Arise from an Exon-skipping Mechanism of Alternative Splicing of the Transcript from the iPLA2 Gene on Chromosome 22q13.1
Ma Z
The Journal of Biological Chemistry, 274, 9607-9616 (1999)
Chinese patent medicine Xin-Ke-Shu inhibits Ca2+ overload and dysfunction of fatty acid β-oxidation in rats with myocardial infarction induced by LAD ligation
Yang Y, et al.
Journal of Chromatography. B, Biomedical Sciences and Applications, 1079, 85-94 (2018)
Guang Lin et al.
eLife, 12 (2023-01-17)
Infantile neuroaxonal dystrophy (INAD) is caused by recessive variants in PLA2G6 and is a lethal pediatric neurodegenerative disorder. Loss of the Drosophila homolog of PLA2G6, leads to ceramide accumulation, lysosome expansion, and mitochondrial defects. Here, we report that retromer function

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