Tyrosine-protein kinase JAK2 Recombinant Protein | JAK2 recombinant protein
Recombinant Human Tyrosine-protein kinase JAK2
Gene Names
JAK2; JTK10; THCYT3
Purity
Greater or equal to 85% purity as determined by SDS-PAGE.
Synonyms
Tyrosine-protein kinase JAK2; N/A; 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
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
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
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 #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
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
UniProt Gene Name
JAK2
UniProt Synonym Gene Names
JAK-2
UniProt Entry Name
JAK2_HUMAN
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Product Notes
The JAK2 jak2 (Catalog #AAA114786) is a Recombinant Protein produced from E Coli or Yeast or Baculovirus or Mammalian Cell and is intended for research purposes only. The product is available for immediate purchase. The immunogen sequence is 752-1132aa; Partial. The amino acid sequence is listed below: KPLSALDSQR KLQFYEDRHQ LPAPKWAELA NLINNCMDYE PDFRPSFRAI IRDLNSLFTP DYELLTENDM LPNMRIGALG FSGAFEDRDP TQFEERHLKF LQQLGKGNFG SVEMCRYDPL QDNTGEVVAV KKLQHSTEEH LRDFEREIEI LKSLQHDNIV KYKGVCYSAG RRNLKLIMEY LPYGSLRDYL QKHKERIDHI KLLQYTSQIC KGMEYLGTKR YIHRDLATRN ILVENENRVK IGDFGLTKVL PQDKEYYKVK EPGESPIFWY APESLTESKF SVASDVWSFG VVLYELFTYI EKSKSPPAEF MRMIGNDKQG QMIVFHLIEL LKNNGRLPRP DGCPDEIYMI MTECWNNNVN QRPSFRDLAL RVDQIRDNMA G. It is sometimes possible for the material contained within the vial of "Tyrosine-protein kinase JAK2, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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