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Mouse Anti-ENPP2 Recombinant Antibody (CAP698) (CBMAB-AP2068LY)


See all ENPP2 antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
CAP698
Antibody Isotype
IgG
Application
ICC, IHC, IP, WB

Basic Information

Immunogen
Arg637~Lys905
Specificity
Human
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Ectonucleotide Pyrophosphatase/Phosphodiesterase 2
Introduction
The protein encoded by this gene functions as both a phosphodiesterase, which cleaves phosphodiester bonds at the 5' end of oligonucleotides, and a phospholipase, which catalyzes production of lysophosphatidic acid (LPA) in extracellular fluids. LPA evokes growth factor-like responses including stimulation of cell proliferation and chemotaxis. This gene product stimulates the motility of tumor cells and has angiogenic properties, and its expression is upregulated in several kinds of carcinomas. The gene product is secreted and further processed to make the biologically active form. Several alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Aug 2008]
Entrez Gene ID
5168
UniProt ID
Q13822
Alternative Names
Ectonucleotide Pyrophosphatase/Phosphodiesterase 2; Autotaxin; Extracellular Lysophospholipase D; EC 3.1.4.39; E-NPP 2; LysoPLD; PDNP2; ATX;
Research Area
Hydrolyzes lysophospholipids to produce the signaling molecule lysophosphatidic acid (LPA) in extracellular fluids (PubMed:15769751, PubMed:26371182, PubMed:27754931, PubMed:14500380, PubMed:12354767,).

Major substrate is lysophosphatidylcholine (PubMed:12176993, PubMed:27754931, PubMed:14500380).

Also can 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:15769751, PubMed:12176993).

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). Tumor cell motility-stimulating factor (PubMed:1733949, PubMed:11559573).

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).
Biological Process
Cell motility Source: UniProtKB
Chemotaxis Source: UniProtKB
Immune response Source: InterPro
Phosphatidylcholine catabolic process Source: UniProtKB
Phospholipid catabolic process Source: UniProtKB
Positive regulation of epithelial cell migration Source: UniProtKB
Positive regulation of lamellipodium morphogenesis Source: UniProtKB
Positive regulation of peptidyl-tyrosine phosphorylation Source: UniProtKB
Regulation of angiogenesis Source: InterPro
Regulation of cell migration Source: UniProtKB
Sphingolipid catabolic process Source: UniProtKB
Cellular Location
Secreted
PTM
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.

Karshovska, E., Mohibullah, R., Zhu, M., Zahedi, F., Thomas, D., Magkrioti, C., ... & Schober, A. (2022). Endothelial ENPP2 (Ectonucleotide Pyrophosphatase/Phosphodiesterase 2) Increases Atherosclerosis in Female and Male Mice. Arteriosclerosis, Thrombosis, and Vascular Biology, 42(8), 1023-1036.

Borza, R., Salgado-Polo, F., Moolenaar, W. H., & Perrakis, A. (2022). Structure and function of the ecto-nucleotide pyrophosphatase/phosphodiesterase (ENPP) family: Tidying up diversity. Journal of Biological Chemistry, 298(2).

Li, Y., Zhang, L., Xu, T., Zhao, X., Jiang, X., Xiao, F., ... & Wang, L. (2022). Aberrant ENPP2 expression promotes tumor progression in multiple myeloma. Leukemia & Lymphoma, 63(4), 963-974.

Mamoor, S. (2021). Differential expression of ectonucleotide pyrophosphatase/phosphodiesterase 2 in cancers of the breast.

He, L., Yang, Y., Chen, J., Zou, P., & Li, J. (2021). Transcriptional activation of ENPP2 by FoxO4 protects cardiomyocytes from doxorubicin‑induced toxicity. Molecular Medicine Reports, 24(3), 1-11.

Deng, W., Chen, F., Zhou, Z., Huang, Y., Lin, J., Zhang, F., ... & Xu, L. (2021). Hepatitis B virus promotes hepatocellular carcinoma progression synergistically with hepatic stellate cells via facilitating the expression and secretion of ENPP2. Frontiers in molecular biosciences, 8.

Sah, J. P., Hao, N. T. T., Han, X., Tran, T. T. T., McCarthy, S., Oh, Y., & Yoon, J. K. (2020). Ectonucleotide pyrophosphatase 2 (ENPP2) plays a crucial role in myogenic differentiation through the regulation by WNT/β-catenin signaling. The international journal of biochemistry & cell biology, 118, 105661.

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For research use only. Not intended for any clinical use.

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