Receptor-interacting serine/threonine-protein kinase 2 (RIPK2) Recombinant Protein | RIPK2 recombinant protein

Recombinant Human Receptor-interacting serine/threonine-protein kinase 2 (RIPK2)

Cat. Num. AAA1174923

• Gene Names: RIPK2; CCK; RICK; RIP2; CARD3; GIG30; CARDIAK
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Receptor-interacting serine/threonine-protein kinase 2 (RIPK2); Recombinant Human Receptor-interacting serine/threonine-protein kinase 2 (RIPK2); CARD-containing interleukin-1 beta-converting enzyme-associated kinase; CARD-containing IL-1 beta ICE-kinase; RIP-like-interacting CLARP kinase; Receptor-interacting protein 2; RIP-2; Tyrosine-protein kinase RIPK2 (EC:2.7.10.2); RIPK2 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: 1-540. Full Length
• Sequence: MNGEAICSALPTIPYHKLADLRYLSRGASGTVSSARHADWRVQVAVKHLHIHTPLLDSERKDVLREAEILHKARFSYILPILGICNEPEFLGIVTEYMPNGSLNELLHRKTEYPDVAWPLRFRILHEIALGVNYLHNMTPPLLHHDLKTQNILLDNEFHVKIADFGLSKWRMMSLSQSRSSKSAPEGGTIIYMPPENYEPGQKSRASIKHDIYSYAVITWEVLSRKQPFEDVTNPLQIMYSVSQGHRPVINEESLPYDIPHRARMISLIESGWAQNPDERPSFLKCLIELEPVLRTFEEITFLEAVIQLKKTKLQSVSSAIHLCDKKKMELSLNIPVNHGPQEESCGSSQLHENSGSPETSRSLPAPQDNDFLSRKAQDCYFMKLHHCPGNHSWDSTISGSQRAAFCDHKTTPCSSAIINPLSTAGNSERLQPGIAQQWIQSKREDIVNQMTEACLNQSLDALLSRDLIMKEDYELVSTKPTRTSKVRQLLDTTDIQGEEFAKVIVQKLKDNKQMGLQPYPEILVVSRSPSLNLLQNKSM

• Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to [email protected] for more details.
• 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 RIPK2 recombinant protein

Serine/threonine/tyrosine kinase that plays an essential role in modulation of innate and adaptive immune responses. Upon stimulation by bacterial peptidoglycans, NOD1 and NOD2 are activated, oligomerize and recruit RIPK2 through CARD-CARD domains. Contributes to the tyrosine phosphorylation of the guanine exchange factor ARHGEF2 through Src tyrosine kinase leading to NF-kappaB activation by NOD2. Once recruited, RIPK2 autophosphorylates and undergoes 'Lys-63'-linked polyubiquitination by E3 ubiquitin ligases XIAP, BIRC2 and BIRC3. The polyubiquitinated protein mediates the recruitment of MAP3K7/TAK1 to IKBKG/NO and induces 'Lys-63'-linked polyubiquitination of IKBKG/NO and subsequent activation of IKBKB/IKKB. In turn, NF-kappa-B is released from NF-kappa-B inhibitors and translocates into the nucleus where it activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. Plays also a role during engagent of the T-cell receptor (TCR) in promoting BCL10 phosphorylation and subsequent NF-kappa-B activation.

Product Categories/Family for RIPK2 recombinant protein

Immunology

References

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Biol. 8:885-888(1998) The secreted protein discovery initiative (SPDI) , a large-scale effort to identify novel human secreted and transmembrane proteins a bioinformatics assessment.Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.Genome Res. 13:2265-2270(2003) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) DNA sequence and analysis of human chromosome 8.Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.Nature 439:331-335(2006) Rip2 participates in Bcl10 signaling and T-cell receptor-mediated NF-kappaB activation.Ruefli-Brasse A.A., Lee W.P., Hurst S., Dixit V.M.J. Biol. Chem. 279:1570-1574(2004) Identification of a regulatory autophosphorylation site in the serine-threonine kinase RIP2.Dorsch M., Wang A., Cheng H., Lu C., Bielecki A., Charron K., Clauser K., Ren H., Polakiewicz R.D., Parsons T., Li P., Ocain T., Xu Y.Cell. Signal. 18:2223-2229(2006) Solution structure of NOD1 CARD and mutational analysis of its interaction with the CARD of downstream kinase RICK.Manon F., Favier A., Nunez G., Simorre J.P., Cusack S.J. Mol. Biol. 365:160-174(2007) MEKK4 sequesters RIP2 to dictate NOD2 signal specificity.Clark N.M., Marinis J.M., Cobb B.A., Abbott D.W.Curr. Biol. 18:1402-1408(2008) A critical role of RICK/RIP2 polyubiquitination in Nod-induced NF-kappaB activation.Hasegawa M., Fujimoto Y., Lucas P.C., Nakano H., Fukase K., Nunez G., Inohara N.EMBO J. 27:373-383(2008) Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.Mol. Cell 31:438-448(2008) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) ITCH K63-ubiquitinates the NOD2 binding protein, RIP2, to influence inflammatory signaling pathways.Tao M., Scacheri P.C., Marinis J.M., Harhaj E.W., Matesic L.E., Abbott D.W.Curr. Biol. 19:1255-1263(2009) Cellular inhibitors of apoptosis cIAP1 and cIAP2 are required for innate immunity signaling by the pattern recognition receptors NOD1 and NOD2.Bertrand M.J., Doiron K., Labbe K., Korneluk R.G., Barker P.A., Saleh M.Immunity 30:789-801(2009) Large-scale proteomics analysis of the human kinome.Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.Mol. Cell. Proteomics 8:1751-1764(2009) Inhibition of RIP2's tyrosine kinase activity limits NOD2-driven cytokine responses.Tigno-Aranjuez J.T., Asara J.M., Abbott D.W.Genes Dev. 24:2666-2677(2010) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) cIAP1/2 are direct E3 ligases conjugating diverse types of ubiquitin chains to receptor interacting proteins kinases 1 to 4 (RIP1-4) .Bertrand M.J., Lippens S., Staes A., Gilbert B., Roelandt R., De Medts J., Gevaert K., Declercq W., Vandenabeele P.PLoS ONE 6:E22356-E22356(2011) NLRP10 enhances Shigella-induced pro-inflammatory responses.Lautz K., Damm A., Menning M., Wenger J., Adam A.C., Zigrino P., Kremmer E., Kufer T.A.Cell. Microbiol. 14:1568-1583(2012) Control of NOD2 and Rip2-dependent innate immune activation by GEF-H1.Zhao Y., Alonso C., Ballester I., Song J.H., Chang S.Y., Guleng B., Arihiro S., Murray P.J., Xavier R., Kobayashi K.S., Reinecker H.C.Inflamm. Bowel Dis. 18:603-612(2012) OTULIN restricts Met1-linked ubiquitination to control innate immune signaling.Fiil B.K., Damgaard R.B., Wagner S.A., Keusekotten K., Fritsch M., Bekker-Jensen S., Mailand N., Choudhary C., Komander D., Gyrd-Hansen M.Mol. Cell 50:818-830(2013) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) 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) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 4506537
• NCBI GeneID: 8767
• NCBI Accession #: NP_003812.1
• NCBI GenBank Nucleotide #: NM_003821.5
• UniProt Accession #: O43353; Q6UWF0; B7Z748
• Molecular Weight: 65.2 kDa
• NCBI Official Full Name: receptor-interacting serine/threonine-protein kinase 2
• NCBI Official Synonym Full Names: receptor interacting serine/threonine kinase 2
• NCBI Official Symbol: RIPK2
• NCBI Official Synonym Symbols: CCK; RICK; RIP2; CARD3; GIG30; CARDIAK
• NCBI Protein Information: receptor-interacting serine/threonine-protein kinase 2
• UniProt Protein Name: Receptor-interacting serine/threonine-protein kinase 2
• Protein Family: Receptor-interacting serine/threonine-protein kinase
• UniProt Gene Name: RIPK2
• UniProt Synonym Gene Names: CARDIAK; RICK; RIP2; CARD-containing IL-1 beta ICE-kinase; RIP-2
• UniProt Entry Name: RIPK2_HUMAN

NCBI Description

This gene encodes a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases. The encoded protein contains a C-terminal caspase activation and recruitment domain (CARD), and is a component of signaling complexes in both the innate and adaptive immune pathways. It is a potent activator of NF-kappaB and inducer of apoptosis in response to various stimuli. [provided by RefSeq, Jul 2008]

Uniprot Description

RIPK2: a tyrosine kinase-like kinase of the RIPK family. Activates pro-caspase-1 and pro-caspase-8. Potentiates casp-8-mediated apoptosis. May activate NF-kappaB.

Protein type: Kinase, protein; Protein kinase, TKL; Protein kinase, Ser/Thr (non-receptor); EC 2.7.11.1; EC 2.7.10.2; TKL group; RIPK family

Chromosomal Location of Human Ortholog: 8q21

Cellular Component: cytoplasm; cytoskeleton; cytosol; protein complex; vesicle

Molecular Function: ATP binding; CARD domain binding; LIM domain binding; non-membrane spanning protein tyrosine kinase activity; protein binding; protein homodimerization activity; protein serine/threonine kinase activity; receptor binding; signal transducer activity

Biological Process: activation of MAPK activity; activation of NF-kappaB transcription factor; adaptive immune response; apoptosis; defense response to Gram-positive bacterium; I-kappaB kinase/NF-kappaB cascade; inflammatory response; innate immune response; JNK cascade; lipopolysaccharide-mediated signaling pathway; MyD88-dependent toll-like receptor signaling pathway; MyD88-independent toll-like receptor signaling pathway; negative regulation of apoptosis; nerve growth factor receptor signaling pathway; peptidyl-tyrosine phosphorylation; positive regulation of alpha-beta T cell proliferation; positive regulation of apoptosis; positive regulation of chemokine production; positive regulation of cytokine and chemokine mediated signaling pathway; positive regulation of I-kappaB kinase/NF-kappaB cascade; positive regulation of immature T cell proliferation; positive regulation of interferon-alpha production; positive regulation of interferon-beta production; positive regulation of interferon-gamma production; positive regulation of interleukin-12 production; positive regulation of interleukin-2 production; positive regulation of interleukin-6 production; positive regulation of JNK cascade; positive regulation of peptidyl-serine phosphorylation; positive regulation of peptidyl-tyrosine phosphorylation; positive regulation of protein ubiquitination; positive regulation of T-helper 1 cell differentiation; positive regulation of transcription from RNA polymerase II promoter; positive regulation of tumor necrosis factor production; response to exogenous dsRNA; signal transduction; stress-activated MAPK cascade; T cell proliferation; T cell receptor signaling pathway; toll-like receptor 10 signaling pathway; toll-like receptor 2 signaling pathway; toll-like receptor 3 signaling pathway; toll-like receptor 4 signaling pathway; toll-like receptor 5 signaling pathway; toll-like receptor 9 signaling pathway; toll-like receptor signaling pathway