Recombinant Human PLA2G6 protein

Specification
Description Recombinant protein from the full-length sequence of homo sapiens phospholipase A2 group VI (PLA2G6), transcript variant 1 (NM_003560).
Organism Homo sapiens (Human)
Expression Host Human Cells
Tag Info His or DYKDDDDK. Please contact us if you need further information or require specific designed tag.
Purity Greater than 90% by SDS-PAGE gel
Uniprot ID O60733
Entry Name PLPL9_HUMAN
Gene Names PLA2G6 PLPLA9
Alternative Gene Names PLPLA9
Alternative Protein Names 85/88 kDa calcium-independent phospholipase A2 (CaI-PLA2) (EC 3.1.1.4) (2-lysophosphatidylcholine acylhydrolase) (EC 3.1.1.5) (Group VI phospholipase A2) (GVI PLA2) (Intracellular membrane-associated calcium-independent phospholipase A2 beta) (iPLA2-beta) (Palmitoyl-CoA hydrolase) (EC 3.1.2.2) (Patatin-like phospholipase domain-containing protein 9) (PNPLA9)
Application Antigens, Western, ELISA and other in vitro binding or in vivo functional assays, and protein-protein interaction studies; For research & development use only!
Buffer Purified protein formulated in a sterile solution of PBS buffer, pH7.2, without any preservatives
Endotoxin Endotoxin level is < 0.1 ng/µg of protein (<1EU /µg)
Length 806
Molecular Weight(Da) 89903
Protein Sequence (The sequence of expressed protein may have some variation from the sequence shown below. Please contact us for the exact sequence.)
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLVNPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSWSVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMDVTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLRTVGAEYCFPPIHGVPAEQGSAAPHHPFSLERAQPPPISLNNLELQDLMHISRARKPAFILGSMRDEKRTHDHLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAKTVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHREEFQKLIQLLLSP
Background
Function FUNCTION: Calcium-independent phospholipase involved in phospholipid remodeling with implications in cellular membrane homeostasis, mitochondrial integrity and signal transduction. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 and A2 activity respectively), producing lysophospholipids that are used in deacylation-reacylation cycles (PubMed:9417066, PubMed:10092647, PubMed:10336645, PubMed:20886109). Hydrolyzes both saturated and unsaturated long fatty acyl chains in various glycerophospholipid classes such as phosphatidylcholines, phosphatidylethanolamines and phosphatidates, with a preference for hydrolysis at sn-2 position (PubMed:10092647, PubMed:10336645, PubMed:20886109). Can further hydrolyze lysophospholipids carrying saturated fatty acyl chains (lysophospholipase activity) (PubMed:20886109). Upon oxidative stress, contributes to remodeling of mitochondrial phospholipids in pancreatic beta cells, in a repair mechanism to reduce oxidized lipid content (PubMed:23533611). Preferentially hydrolyzes oxidized polyunsaturated fatty acyl chains from cardiolipins, yielding monolysocardiolipins that can be reacylated with unoxidized fatty acyls to regenerate native cardiolipin species (By similarity). Hydrolyzes oxidized glycerophosphoethanolamines present in pancreatic islets, releasing oxidized polyunsaturated fatty acids such as hydroxyeicosatetraenoates (HETEs) (By similarity). Has thioesterase activity toward fatty-acyl CoA releasing CoA-SH known to facilitate fatty acid transport and beta-oxidation in mitochondria particularly in skeletal muscle (PubMed:20886109). Plays a role in regulation of membrane dynamics and homeostasis. Selectively hydrolyzes sn-2 arachidonoyl group in plasmalogen phospholipids, structural components of lipid rafts and myelin (By similarity). Regulates F-actin polymerization at the pseudopods, which is required for both speed and directionality of MCP1/CCL2-induced monocyte chemotaxis (PubMed:18208975). Targets membrane phospholipids to produce potent lipid signaling messengers. Generates lysophosphatidate (LPA, 1-acyl-glycerol-3-phosphate), which acts via G-protein receptors in various cell types (By similarity). Has phospholipase A2 activity toward platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), likely playing a role in inactivation of this potent proinflammatory signaling lipid (By similarity). In response to glucose, amplifies calcium influx in pancreatic beta cells to promote INS secretion (By similarity). {ECO:0000250|UniProtKB:A0A3L7I2I8, ECO:0000250|UniProtKB:P97570, ECO:0000250|UniProtKB:P97819, ECO:0000269|PubMed:10092647, ECO:0000269|PubMed:10336645, ECO:0000269|PubMed:18208975, ECO:0000269|PubMed:20886109, ECO:0000269|PubMed:23533611, ECO:0000269|PubMed:9417066}.; FUNCTION: [Isoform Ankyrin-iPLA2-1]: Lacks the catalytic domain and may act as a negative regulator of the catalytically active isoforms. {ECO:0000269|PubMed:9417066}.; FUNCTION: [Isoform Ankyrin-iPLA2-2]: Lacks the catalytic domain and may act as a negative regulator of the catalytically active isoforms. {ECO:0000269|PubMed:9417066}.
Pathway
Protein Families
Tissue Specificity Four different transcripts were found to be expressed in a distinct tissue distribution.
QC Data
Note Please contact us for QC Data
Product Image (Reference Only) Product via image
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SKU
EB-EPE8599186

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