Tyrosine-protein kinase JAK2 antibody

Principal name

Tyrosine-protein kinase JAK2 antibody

Alternative names for Tyrosine-protein kinase JAK2 antibody

Janus kinase 2, JAK-2

SwissProt ID

O19064 (Pig), O60674 (Human), Q62120 (Mouse), Q62689 (Rat), Q75R65 (Chick)

Gene ID

3717 (JAK2), 16452 (Jak2), 24514

Available reactivities

Hu (Human), Ms (Mouse), Rt (Rat), Chk (Chicken), Por (Porcine), Ze (Zebrafish), Can (Canine), Mky (Monkey), Rb (Rabbit)

Available hosts

Rabbit, Mouse

Available applications

Western blot / Immunoblot (WB), Paraffin Sections (P), Enzyme Immunoassay (E), Frozen Sections (C), Dot blot (Dot), Immunoprecipitation (IP), Immunocytochemistry/Immunofluorescence (ICC/IF)

Background of Tyrosine-protein kinase JAK2 antibody

JAK2 (Janus Kinase 2) belongs to the emerging family of non-receptor Janus tyrosine kinases, which regulate a spectrum of cellular functions downstream of activated cytokine receptors in the lympho-hematopoietic system. Immunological stimuli, such as interferons and cytokines, induce recruitment of Stat transcription factors to cytokine receptor-associated JAK2. JAK2 then phosphorylates proximal Stat factors, which subsequently dimerize, translocate to the nucleus and bind to CIS elements upstream of target gene promoters to regulate transcription. The canonical JAK/Stat pathway is integral to maintaining a normal immune system by stimulating proliferation, differentiation, survival and host resistance to pathogens. Altering JAK/Stat signaling to reduce cytokine induced pro-inflammatory responses represents an attractive target for anti-inflammatory therapies. Within the JAK2 kinase domain, there is a region that has considerable sequence homology to the regulatory region of the insulin receptor. Among a variety of sites, Tyrosines 1007 and 1008 are sites of trans- or autophosphorylation in vivo and in in vitro kinase reactions.

General readings

Frank, G.D., et al. (2003) Distinct mechanisms of receptor and nonreceptor tyrosine kinase activation by reactive oxygen species in vascular smooth muscle cells: role of metalloprotease and protein kinase C-delta. Mol. Cell. Biol. 23(5):1581-1589.
Kaszubska, W., et al. (2002) Protein tyrosine phosphatase 1B negatively regulates leptin signaling in a hypothalamic cell line. Mol. Cell. Endocrinol. 195(1-2):109-118.
Kirito, K., et al. (2002) Thrombopoietin regulates Bcl-xL gene expression through Stat5 and phosphatidylinositol 3-kinase activation pathways. J. Biol. Chem. 277(10):8329-8337.
Shaw, S., et al. (2002) Janus kinase 2, an early target of alpha 7 nicotinic acetylcholine receptor-mediated neuroprotection against Abeta-(1-42) amyloid. J. Biol. Chem. 277(47):44920-44924.
Sutherland, C.L., et al. (2002) UL16-binding proteins, novel MHC class I-related proteins, bind to NKG2D and activate multiple signaling pathways in primary NK cells. J. Immunol. 168(2):671-679.
Zeng, Z.Z., et al. (2002) 5(S)-hydroxyeicosatetraenoic acid stimulates DNA synthesis in human microvascular endothelial cells via activation of Jak/STAT and phosphatidylinositol 3-kinase/Akt signaling, leading to induction of expression of basic fibroblast growth factor 2. J. Biol. Chem. 277(43):41213-41219.
Eguchi, S., et al. (2001) Activation of MAPKs by angiotensin II in vascular smooth muscle cells. Metalloprotease-dependent EGF receptor activation is required for activation of ERK and p38 MAPK but not for JNK. J. Biol. Chem. 276(11):7957-7962.
Madamanchi, N.R., et al. (2001) Thrombin regulates vascular smooth muscle cell growth and heat shock proteins via the JAK-STAT pathway. J. Biol. Chem. 276(22):18915-18924.
Myers, M.P., et al. (2001) TYK2 and JAK2 are substrates of protein-tyrosine phosphatase 1B. J. Biol. Chem. 276(51):47771-47774.
Madamanchi, N.R., et al. (2000) Reactive oxygen species regulate heat shock protein 70 via the JAK/STAT Pathway. Arteriocher. Thromb. Vasc. Biol. 21(3):321-326.
Amiri, F., et al. (1999) Hyperglycemia enhances angiotensin II-induced janus-activated kinase/STAT signaling in vascular smooth muscle cells. J. Biol. Chem. 274(45):32382-32386.
Ihle, J.N. (1996) STATs: signal transducers and activators of transcription. Cell 84(3):331-334.

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