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Receptor-Interacting Serine/Threonine-Protein Kinase 2 (RIPK2) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS1174923

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.… More details

$455 / 0.02 mg (E-Coli) +1 FREE 8GB USB
Product Documentation
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Sample Manual Insert View PDF
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Testing Data View PDF
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Certificate of Analysis (COA) View PDF
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QC Report View PDF
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Material Safety Data Sheet View PDF
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Technical Datasheet View PDF
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Product Overview

Online Datasheet in PDF
Product Name
Receptor-interacting serine/threonine-protein kinase 2 (RIPK2), Recombinant Protein
Full Product Name
Recombinant Human Receptor-interacting serine/threonine-protein kinase 2 (RIPK2)
Product Gene Name
Product Synonym Names
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)
Sequence
MNGEAICSAL PTIPYHKLAD LRYLSRGASG TVSSARHADW RVQVAVKHLH IHTPLLDSER KDVLREAEIL HKARFSYILP ILGICNEPEF LGIVTEYMPN GSLNELLHRK TEYPDVAWPL RFRILHEIAL GVNYLHNMTP PLLHHDLKTQ NILLDNEFHV KIADFGLSKW RMMSLSQSRS SKSAPEGGTI IYMPPENYEP GQKSRASIKH DIYSYAVITW EVLSRKQPFE DVTNPLQIMY SVSQGHRPVI NEESLPYDIP HRARMISLIE SGWAQNPDER PSFLKCLIEL EPVLRTFEEI TFLEAVIQLK KTKLQSVSSA IHLCDKKKME LSLNIPVNHG PQEESCGSSQ LHENSGSPET SRSLPAPQDN DFLSRKAQDC YFMKLHHCPG NHSWDSTISG SQRAAFCDHK TTPCSSAIIN PLSTAGNSER LQPGIAQQWI QSKREDIVNQ MTEACLNQSL DALLSRDLIM KEDYELVSTK PTRTSKVRQL LDTTDIQGEE FAKVIVQKLK DNKQMGLQPY PEILVVSRSP SLNLLQNKSM
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
65.2 kDa
Sequence Positions
1-540aa; Full Length
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
OMIM
603455
3D Structure
ModBase 3D Structure for O43353
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 support@mybiosource.com for more details.

Product Categories/Family for RIPK2 recombinant protein

ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

Product References and Citations for RIPK2 recombinant protein

RICK, a novel protein kinase containing a caspase recruitment domain, interacts with CLARP and regulates CD95-mediated apoptosis.Inohara N., del Peso L., Koseki T., Chen S., Nunez G.J. Biol. Chem. 273:12296-12300(1998) RIP2 is a novel NF-kappaB-activating and cell death-inducing kinase.McCarthy J.V., Ni J., Dixit V.M.J. Biol. Chem. 273:16968-16975(1998) Identification of CARDIAK, a RIP-like kinase that associates with caspase-1.Thome M., Hofmann K., Burns K., Martinon F., Bodmer J.-L., Mattmann C., Tschopp J.Curr. 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.

Other Notes

Small volumes of RIPK2 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Searchable Terms for RIPK2 purchase

MBS1174923 is a recombinant protein targeting RIPK2. Also known as Recombinant Human Receptor-interacting serine/threonine-protein kinase 2 (RIPK2). Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for RIPK2. It may not necessarily be applicable to this product.

NCBI GI #
NCBI GeneID
NCBI Accession #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
GenBank Nucleotide #
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
UniProt Protein Name
Receptor-interacting serine/threonine-protein kinase 2
UniProt Synonym Protein Names
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)
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 Protein Information
receptor-interacting serine/threonine-protein kinase 2

NCBI Summary for RIPK2

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]
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UniProt Comments for RIPK2

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
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Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

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