Recombinant Human ENPP2/ATX protein (Tag Free)
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- SDS-PAGE
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SDS-PAGE - Recombinant Human ENPP2/ATX protein (Tag Free) (AB126918)
SDS-PAGE showing ab126918
Reactivity data
Product details
Sequence info
Properties and storage information
Form
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
ATX protein influences cell proliferation migration and survival. It does not operate as part of a complex but directly impacts the biological processes previously mentioned due to its enzymatic function. It acts significantly during embryonic development and wound healing. The products of its catalysis LPA engage in various signaling pathways essential for these processes.
Pathways
ENPP2 integrates into the lysophospholipid and phospholipase pathways. It plays an important role in the LPA receptor signaling pathway contributing to various physiological and pathological processes. Proteins related to ENPP2 through these pathways include LPA receptors such as LPAR1 and LPAR2 with which it interacts closely to mediate cell signaling roles and phospholipase A2 which provides substrate for its enzymatic activity.
General info
Function
Secreted lysophospholipase D that hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids (PubMed : 12354767, PubMed : 14500380, PubMed : 15769751, PubMed : 26371182, PubMed : 27754931). Its major substrate is lysophosphatidylcholine (PubMed : 12176993, PubMed : 14500380, PubMed : 27754931). Can also act on sphingosylphosphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility (PubMed : 14500380). Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP (PubMed : 12176993, PubMed : 15769751). Involved in several motility-related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation (PubMed : 11559573). Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein (PubMed : 1733949). May have a role in induction of parturition (PubMed : 12176993). Possible involvement in cell proliferation and adipose tissue development (Probable). Required for LPA production in activated platelets, cleaves the sn-1 lysophospholipids to generate sn-1 lysophosphatidic acids containing predominantly 18 : 2 and 20 : 4 fatty acids (PubMed : 21393252). Shows a preference for the sn-1 to the sn-2 isomer of 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF) (PubMed : 21393252).
Sequence similarities
Belongs to the nucleotide pyrophosphatase/phosphodiesterase family.
Post-translational modifications
N-glycosylation, but not furin-cleavage, plays a critical role on secretion and on lysoPLD activity.. The interdomain disulfide bond between Cys-414 and Cys-806 is essential for catalytic activity.
Target data
Alternative Names
Product promise
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