Tyrosine-protein kinase JAK2 Recombinant Protein | JAK2 recombinant protein

Recombinant Human Tyrosine-protein kinase JAK2

Cat. Num. AAA1066084

• Gene Names: JAK2; JTK10; THCYT3
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Tyrosine-protein kinase JAK2; Recombinant Human Tyrosine-protein kinase JAK2; Janus kinase 2; JAK-2; JAK2 recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 752-1132aa; Partial
• Sequence: KPLSALDSQRKLQFYEDRHQLPAPKWAELANLINNCMDYEPDFRPSFRAIIRDLNSLFTPDYELLTENDMLPNMRIGALGFSGAFEDRDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMAG
• Sequence Length: 1132

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for JAK2 recombinant protein

Non-receptor tyrosine kinase involved in various processes such as cell growth, development, differentiation or histone modifications. Mediates essential signaling events in both innate and adaptive immunity. In the cytoplasm, plays a pivotal role in signal transduction via its association with type I receptors such as growth hormone (GHR), prolactin (PRLR), leptin (LEPR), erythropoietin (EPOR), thrombopoietin (THPO); or type II receptors including IFN-alpha, IFN-beta, IFN-gamma and multiple interleukins. Following ligand-binding to cell surface receptors, phosphorylates specific tyrosine residues on the cytoplasmic tails of the receptor, creating docking sites for STATs proteins. Subsequently, phosphorylates the STATs proteins once they are recruited to the receptor. Phosphorylated STATs then form homodimer or heterodimers and translocate to the nucleus to activate gene transcription. For example, cell stimulation with erythropoietin (EPO) during erythropoiesis leads to JAK2 autophosphorylation, activation, and its association with erythropoietin receptor (EPOR) that becomes phosphorylated in its cytoplasmic domain. Then, STAT5 (STAT5A or STAT5B) is recruited, phosphorylated and activated by JAK2. Once activated, dimerized STAT5 translocates into the nucleus and promotes the transcription of several essential genes involved in the modulation of erythropoiesis. In addition, JAK2 mediates angiotensin-2-induced ARHGEF1 phosphorylation. Plays a role in cell cycle by phosphorylating CDKN1B. Cooperates with TEC through reciprocal phosphorylation to mediate cytokine-driven activation of FOS transcription. In the nucleus, plays a key role in chromatin by specifically mediating phosphorylation of 'Tyr-41' of histone H3 (H3Y41ph), a specific tag that promotes exclusion of CBX5 (HP1 alpha) from chromatin.

Product Categories/Family for JAK2 recombinant protein

Immunology

References

Cloning and characterization of human Jak-2 kinase high mRNA expression in immune cells and muscle tissue.Saltzman A., Stone M., Franks C., Searfoss G., Munro R., Jaye M., Ivashchenko Y.Biochem. Biophys. Res. Commun. 246:627-633(1998) Cloning and characterization of the human homolog of mouse Jak2.Dalal I., Arpaia E., Dadi H., Kulkarni S., Squire J., Roifman C.M.Blood 91:844-851(1998) Fusion of TEL, the ETS-variant gene 6 (ETV6) , to the receptor-associated kinase JAK2 as a result of t(9;12) in a lymphoid and t(9;15;12) in a myeloid leukemia.Peeters P., Raynaud S.D., Cools J., Wlodarska I., Grosgeorge J., Philip P., Monpoux F., Van Rompaey L., Baens M., Van Den Berghe H., Marynen P.Blood 90:2535-2540(1997) DNA sequence and analysis of human chromosome 9.Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.Nature 429:369-374(2004) The human homologue of the yeast proteins Skb1 and Hsl7p interacts with Jak kinases and contains protein methyltransferase activity.Pollack B.P., Kotenko S.V., He W., Izotova L.S., Barnoski B.L., Pestka S.J. Biol. Chem. 274:31531-31542(1999) STAM2, a new member of the STAM family, binding to the Janus kinases.Endo K., Takeshita T., Kasai H., Sasaki Y., Tanaka N., Asao H., Kikuchi K., Yamada M., Chenb M., O'Shea J.J., Sugamura K.FEBS Lett. 477:55-61(2000) A receptor for the heterodimeric cytokine IL-23 is composed of IL-12Rbeta1 and a novel cytokine receptor subunit, IL-23R.Parham C., Chirica M., Timans J., Vaisberg E., Travis M., Cheung J., Pflanz S., Zhang R., Singh K.P., Vega F., To W., Wagner J., O'Farrell A.-M., McClanahan T.K., Zurawski S., Hannum C., Gorman D., Rennick D.M., Kastelein R.A., de Waal Malefyt R., Moore K.W.J. Immunol. 168:5699-5708(2002) The t(8;9) (p22;p24) is a recurrent abnormality in chronic and acute leukemia that fuses PCM1 to JAK2.Reiter A., Walz C., Watmore A., Schoch C., Blau I., Schlegelberger B., Berger U., Telford N., Aruliah S., Yin J.A., Vanstraelen D., Barker H.F., Taylor P.C., O'Driscoll A., Benedetti F., Rudolph C., Kolb H.-J., Hochhaus A., Hehlmann R., Chase A., Cross N.C.P.Cancer Res. 65:2662-2667(2005) PCM1-JAK2 fusion in myeloproliferative disorders and acute erythroid leukemia with t(8;9) translocation.Murati A., Gelsi-Boyer V., Adelaide J., Perot C., Talmant P., Giraudier S., Lode L., Letessier A., Delaval B., Brunel V., Imbert M., Garand R., Xerri L., Birnbaum D., Mozziconacci M.-J., Chaffanet M.Leukemia 19:1692-1696(2005) The t(8;9) (p22;p24) translocation in atypical chronic myeloid leukaemia yields a new PCM1-JAK2 fusion gene.Bousquet M., Quelen C., De Mas V., Duchayne E., Roquefeuil B., Delsol G., Laurent G., Dastugue N., Brousset P.Oncogene 24:7248-7252(2005) A combination of cytomorphology, cytogenetic analysis, fluorescence in situ hybridization and reverse transcriptase polymerase chain reaction for establishing clonality in cases of persisting hypereosinophilia.Bacher U., Reiter A., Haferlach T., Mueller L., Schnittger S., Kern W., Schoch C.Haematologica 91:817-820(2006) A t(8;9) translocation with PCM1-JAK2 fusion in a patient with T-cell lymphoma.Adelaide J., Perot C., Gelsi-Boyer V., Pautas C., Murati A., Copie-Bergman C., Imbert M., Chaffanet M., Birnbaum D., Mozziconacci M.-J.Leukemia 20:536-537(2006) JAK2 phosphorylates histone H3Y41 and excludes HP1alpha from chromatin.Dawson M.A., Bannister A.J., Gottgens B., Foster S.D., Bartke T., Green A.R., Kouzarides T.Nature 461:819-822(2009) Heme controls the regulation of protein tyrosine kinases Jak2 and Src.Yao X., Balamurugan P., Arvey A., Leslie C., Zhang L.Biochem. Biophys. Res. Commun. 403:30-35(2010) The Rho exchange factor Arhgef1 mediates the effects of angiotensin II on vascular tone and blood pressure.Guilluy C., Bregeon J., Toumaniantz G., Rolli-Derkinderen M., Retailleau K., Loufrani L., Henrion D., Scalbert E., Bril A., Torres R.M., Offermanns S., Pacaud P., Loirand G.Nat. Med. 16:183-190(2010) Phosphorylation of p27Kip1 by JAK2 directly links cytokine receptor signaling to cell cycle control.Jakel H., Weinl C., Hengst L.Oncogene 30:3502-3512(2011) Jak2 tyrosine kinase a mediator of both housekeeping and ligand-dependent gene expression?Wallace T.A., Sayeski P.P.Cell Biochem. Biophys. 44:213-222(2006) Janus kinases in immune cell signaling.Ghoreschi K., Laurence A., O'Shea J.J.Immunol. Rev. 228:273-287(2009) The structural basis of Janus kinase 2 inhibition by a potent and specific pan-Janus kinase inhibitor.Lucet I.S., Fantino E., Styles M., Bamert R., Patel O., Broughton S.E., Walter M., Burns C.J., Treutlein H., Wilks A.F., Rossjohn J.Blood 107:176-183(2006) Acquired mutation of the tyrosine kinase JAK2 in human myeloproliferative disorders.The cancer genome projectBaxter E.J., Scott L.M., Campbell P.J., East C., Fourouclas N., Swanton S., Vassiliou G.S., Bench A.J., Boyd E.M., Curtin N., Scott M.A., Erber W.N., Green A.R.Lancet 365:1054-1061(2005) ErratumThe cancer genome projectBaxter E.J., Scott L.M., Campbell P.J., East C., Fourouclas N., Swanton S., Vassiliou G.S., Bench A.J., Boyd E.M., Curtin N., Scott M.A., Erber W.N., Green A.R.Lancet 366:122-122(2005) Definition of subtypes of essential thrombocythaemia and relation to polycythaemia vera based on JAK2 V617F mutation status a prospective study.The United Kingdom myeloproliferative disorders study group, The medical research council adult leukaemia working party, The Australasian leukaemia and lymphoma groupCampbell P.J., Scott L.M., Buck G., Wheatley K., East C.L., Marsden J.T., Duffy A., Boyd E.M., Bench A.J., Scott M.A., Vassiliou G.S., Milligan D.W., Smith S.R., Erber W.N., Bareford D., Wilkins B.S., Reilly J.T., Harrison C.N., Green A.R.Lancet 366:1945-1953(2005) A unique clonal JAK2 mutation leading to constitutive signalling causes polycythaemia vera.James C., Ugo V., Le Couedic J.-P., Staerk J., Delhommeau F., Lacout C., Garcon L., Raslova H., Berger R., Bennaceur-Griscelli A., Villeval J.L., Constantinescu S.N., Casadevall N., Vainchenker W.Nature 434:1144-1148(2005) A gain-of-function mutation of JAK2 in myeloproliferative disorders.Kralovics R., Passamonti F., Buser A.S., Teo S.-S., Tiedt R., Passweg J.R., Tichelli A., Cazzola M., Skoda R.C.N. Engl. J. Med. 352:1779-1790(2005) Case records of the Massachusetts General Hospital. Case 15-2006 a 46-year-old woman with sudden onset of abdominal distention.Chung R.T., Iafrate A.J., Amrein P.C., Sahani D.V., Misdraji J.N. Engl. J. Med. 354:2166-2175(2006) The JAK2 V617F mutation in de novo acute myelogenous leukemias.Lee J.W., Kim Y.G., Soung Y.H., Han K.J., Kim S.Y., Rhim H.S., Min W.S., Nam S.W., Park W.S., Lee J.Y., Yoo N.J., Lee S.H.Oncogene 25:1434-1436(2006) The JAK2 V617F mutation occurs in hematopoietic stem cells in polycythemia vera and predisposes toward erythroid differentiation.Jamieson C.H.M., Gotlib J., Durocher J.A., Chao M.P., Mariappan M.R., Lay M., Jones C., Zehnder J.L., Lilleberg S.L., Weissman I.L.Proc. Natl. Acad. Sci. U.S.A. 103:6224-6229(2006) JAK2 exon 12 mutations in polycythemia vera and idiopathic erythrocytosis.Scott L.M., Tong W., Levine R.L., Scott M.A., Beer P.A., Stratton M.R., Futreal P.A., Erber W.N., McMullin M.F., Harrison C.N., Warren A.J., Gilliland D.G., Lodish H.F., Green A.R.N. Engl. J. Med. 356:459-468(2007) Patterns of somatic mutation in human cancer genomes.Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.Nature 446:153-158(2007) Germline JAK2 mutation in a family with hereditary thrombocytosis.Mead A.J., Rugless M.J., Jacobsen S.E., Schuh A.N. Engl. J. Med. 366:967-969(2012) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 4826776
• NCBI GeneID: 3717
• NCBI Accession #: NP_004963.1
• NCBI GenBank Nucleotide #: NM_004972.3
• UniProt Accession #: O60674; O14636; O75297
• Molecular Weight: 48.6 kDa
• NCBI Official Full Name: tyrosine-protein kinase JAK2
• NCBI Official Synonym Full Names: Janus kinase 2
• NCBI Official Symbol: JAK2
• NCBI Official Synonym Symbols: JTK10; THCYT3
• NCBI Protein Information: tyrosine-protein kinase JAK2
• UniProt Protein Name: Tyrosine-protein kinase JAK2
• Protein Family: Tyrosine-protein kinase
• UniProt Gene Name: JAK2
• UniProt Synonym Gene Names: JAK-2
• UniProt Entry Name: JAK2_HUMAN

NCBI Description

This gene product is a protein tyrosine kinase involved in a specific subset of cytokine receptor signaling pathways. It has been found to be constituitively associated with the prolactin receptor and is required for responses to gamma interferon. Mice that do not express an active protein for this gene exhibit embryonic lethality associated with the absence of definitive erythropoiesis. [provided by RefSeq, Jul 2008]

Uniprot Description

JAK2: a non-receptor tyrosine-kinase involved in a specific subset of cytokine receptor signaling pathways, including IL-3, -5 and GM-CSF. Interacts with IL23R, SKB1 and STAM2. It has been found to be constitutively associated with the prolactin receptor and is required for responses to gamma interferon. Mice that do not express an active protein for this gene exhibit embryonic lethality associated with the absence of definitive erythropoiesis. Fusion of Jak2 to TEL1 (ETV6) by t(9;12)(p24;p13) causes myeloproliferative disease in humans and mouse models. The Jak inhibitor AG490 inhibits constitutive Jak2 phosphorylation and causes apoptosis in cells from breast cancer and relapsing acute lymphoblastic leukemia. A single activating mutation is associated with several hematological malignancies. Inhibitor: AG490.

Protein type: Protein kinase, TK; Protein kinase, tyrosine (non-receptor); Kinase, protein; EC 2.7.10.2; Oncoprotein; TK group; JakA family

Chromosomal Location of Human Ortholog: 9p24

Cellular Component: caveola; cytoplasm; cytoskeleton; cytosol; extrinsic to internal side of plasma membrane; lipid raft; nuclear matrix; nucleoplasm; nucleus

Molecular Function: acetylcholine receptor binding; ATP binding; growth hormone receptor binding; heme binding; histone binding; insulin receptor substrate binding; interleukin-12 receptor binding; non-membrane spanning protein tyrosine kinase activity; peptide hormone receptor binding; phosphoinositide 3-kinase binding; protein binding; protein C-terminus binding; protein kinase activity; protein kinase binding; protein-tyrosine kinase activity; receptor binding; SH2 domain binding; type 1 angiotensin receptor binding

Biological Process: actin filament polymerization; activation of MAPKK activity; adaptive immune response; apoptosis; axon guidance; axon regeneration; blood coagulation; caspase activation; cell differentiation; cell migration; cell motility; cytokine and chemokine mediated signaling pathway; elevation of cytosolic calcium ion concentration; enzyme linked receptor protein signaling pathway; epidermal growth factor receptor signaling pathway; erythrocyte differentiation; establishment and/or maintenance of chromatin architecture; fibroblast growth factor receptor signaling pathway; G-protein coupled receptor protein signaling pathway; hormone-mediated signaling; host programmed cell death induced by symbiont; induction of apoptosis by oxidative stress; innate immune response; insulin receptor signaling pathway; JAK-STAT cascade; MAPKKK cascade; mesoderm development; mineralocorticoid receptor signaling pathway; negative regulation of cell proliferation; negative regulation of cell-cell adhesion; negative regulation of DNA binding; negative regulation of heart contraction; negative regulation of neuron apoptosis; nerve growth factor receptor signaling pathway; peptidyl-tyrosine phosphorylation; platelet-derived growth factor receptor signaling pathway; positive regulation of cell activation; positive regulation of cell differentiation; positive regulation of cell migration; positive regulation of cell proliferation; positive regulation of DNA binding; positive regulation of inflammatory response; positive regulation of insulin secretion; positive regulation of interleukin-1 beta production; positive regulation of nitric oxide biosynthetic process; positive regulation of nitric-oxide synthase biosynthetic process; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of phosphoinositide 3-kinase cascade; positive regulation of phosphoprotein phosphatase activity; positive regulation of protein import into nucleus, translocation; positive regulation of transcription factor activity; positive regulation of transcription from RNA polymerase II promoter; positive regulation of tumor necrosis factor production; positive regulation of tyrosine phosphorylation of Stat3 protein; positive regulation of tyrosine phosphorylation of Stat5 protein; protein amino acid autophosphorylation; protein amino acid phosphorylation; Ras protein signal transduction; regulation of apoptosis; regulation of cell proliferation; regulation of inflammatory response; response to antibiotic; response to hydroperoxide; response to lipopolysaccharide; signal transduction; small GTPase mediated signal transduction; STAT protein nuclear translocation; tumor necrosis factor-mediated signaling pathway; tyrosine phosphorylation of JAK2 protein; tyrosine phosphorylation of STAT protein; tyrosine phosphorylation of Stat1 protein; tyrosine phosphorylation of Stat3 protein; tyrosine phosphorylation of Stat5 protein; vascular endothelial growth factor receptor signaling pathway

Disease: Budd-chiari Syndrome; Erythrocytosis, Familial, 1; Myelofibrosis; Polycythemia Vera; Thrombocythemia 3