Mouse Recombinant ENPP2 protein, His Tag (V2LY-0526-LY7831)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Mouse
Tag
His Tag
Protein Construction
This product is Mouse Recombinant ENPP2 protein, His Tag consist of Amino Acid: 49-862 and predicts a molecular mass of 96 kDa.
Molecule Mass
96 kDa
Sequence
Amino Acid: 49-862
Species
Mouse

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

Purity
>93% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Ectonucleotide Pyrophosphatase/Phosphodiesterase 2
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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