HSP90AB1 Protein (full length)

Produktnummer ABIN1686667

Produktdetails

Target: HSP90AB1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1))

Protein-Typ: Recombinant

Biologische Aktivität: Active

Proteineigenschaft: full length

Spezies: Human

Quelle: Baculovirus infected Insect Cells

Applikation: Western Blotting (WB), ELISA, SDS-PAGE (SDS), Functional Studies (Func), Protein Complex Immunoprecipitation (Co-IP), Surface Plasmon Resonance (SPR)

Sequenz: MPEEVHHGEE EVETFAFQAE IAQLMSLIIN TFYSNKEIFL RELISNASDA LDKIRYESLT DPSKLDSGKE LKIDIIPNPQ ERTLTLVDTG IGMTKADLIN NLGTIAKSGT KAFMEALQAG ADISMIGQFG VGFYSAYLVA EKVVVITKHN DDEQYAWESS AGGSFTVRAD HGEPIGRGTK VILHLKEDQT EYLEERRVKE VVKKHSQFIG YPITLYLEKE REKEISDDEA EEEKGEKEEE DKDDEEKPKI EDVGSDEEDD SGKDKKKKTK KIKEKYIDQE ELNKTKPIWT RNPDDITQEE YGEFYKSLTN DWEDHLAVKH FSVEGQLEFR ALLFIPRRAP FDLFENKKKK NNIKLYVRRV FIMDSCDELI PEYLNFIRGV VDSEDLPLNI SREMLQQSKI LKVIRKNIVK KCLELFSELA EDKENYKKFY EAFSKNLKLG IHEDSTNRRR LSELLRYHTS QSGDEMTSLS EYVSRMKETQ KSIYYITGES KEQVANSAFV ERVRKRGFEV VYMTEPIDEY CVQQLKEFDG KSLVSVTKEG LELPEDEEEK KKMEESKAKF ENLCKLMKEI LDKKVEKVTI SNRLVSSPCC IVTSTYGWTA NMERIMKAQA LRDNSTMGYM MAKKHLEINP DHPIVETLRQ KAEADKNDKA VKDLVVLLFE TALLSSGFSL EDPQTHSNRI YRMIKLGLGI DEDEVAAEEP NAAVPDEIPP LEGDEDASRM EEVD

Spezifität: ~90 kDa

Aufreinigung: Affinity Purified | Endotoxin-free

Reinheit: >90%

Biological Activity Comment: ATPase active

Anwendungsinformationen

Applikationshinweise: Optimal working dilution should be determined by the investigator.

Kommentare:

This product has been certified >90% pure using SDS-PAGE analysis.

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Konzentration: Lot specific

Buffer: 20 mM Tris, pH 7.5, 175 mM NaCl, 0.1 mM EDTA, 10 % glycerol, 1 mM DTT

Lagerung: -20 °C

Referenzen

Hunter, OHagan, Kenyon, Dhanani, Prinsloo, Edkins: "Hsp90 binds directly to fibronectin (FN) and inhibition reduces the extracellular fibronectin matrix in breast cancer cells." in: PLoS ONE, Vol. 9, Issue 1, pp. e86842, (2014) (PubMed).

Tsou, Lin, Chang, Lin, Shao, Yu, Liu, Chitra, Sia, Chow: "Heat shock protein 90: role in enterovirus 71 entry and assembly and potential target for therapy." in: PLoS ONE, Vol. 8, Issue 10, pp. e77133, (2013) (PubMed).

Prinsloo, Kramer, Edkins, Blatch: "STAT3 interacts directly with Hsp90." in: IUBMB life, Vol. 64, Issue 3, pp. 266-73, (2012) (PubMed).

Antigendetails

Target: HSP90AB1 (Heat Shock Protein 90kDa alpha (Cytosolic), Class B Member 1 (HSP90AB1))

Andere Bezeichnung: Hsp90 beta (HSP90AB1 Produkte)

Synonyme: D6S182 Protein, HSP84 Protein, HSP90B Protein, HSPC2 Protein, HSPCB Protein, GRP94 Protein, TRA1 Protein, hsp90b Protein, 90kDa Protein, AL022974 Protein, C81438 Protein, Hsp84 Protein, Hsp84-1 Protein, Hsp90 Protein, Hspcb Protein, Hsp70 Protein, Hsp70-1 Protein, Hsp70.1 Protein, hsp68 Protein, HSP90-BETA Protein, hsp90beta Protein, wu:fa29f01 Protein, wu:fa91e11 Protein, wu:fd59e11 Protein, wu:gcd22h07 Protein, HSP90 Protein, heat shock protein 90 alpha family class B member 1 Protein, heat shock protein 90 beta family member 1 Protein, Heat Shock Protein 90, endoplasmic reticulum Protein, heat shock protein 90B Protein, heat shock protein 90 alpha (cytosolic), class B member 1 Protein, heat shock protein 1B Protein, heat shock protein 90kDa alpha family class B member 1 S homeolog Protein, heat shock protein 90, alpha (cytosolic), class B member 1 Protein, HSP90AB1 Protein, HSP90B1 Protein, HSP90B Protein, hsp90ab1 Protein, Hsp90ab1 Protein, Hspa1b Protein, hsp90ab1.S Protein

Hintergrund: HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (1-4). Despite its label of being a heat-shock protein, HSP90 is one of the most highly expressed proteins in unstressed cells (1-2 % of cytosolic protein). It carries out a number of housekeeping functions - including controlling the activity, turnover, and trafficking of a variety of proteins. Most of the HSP90-regulated proteins that have been discovered to date are involved in cell signaling (5-6). The number of proteins now know to interact with HSP90 is about 100. Target proteins include the kinases v-Src, Wee1, and c-Raf, transcriptional regulators such as p53 and steroid receptors, and the polymerases of the hepatitis B virus and telomerase.5. When bound to ATP, HSP90 interacts with co-chaperones Cdc37, p23, and an assortment of immunophilin-like proteins, forming a complex that stabilizes and protects target proteins from proteasomal degradation. In most cases, HSP90-interacting proteins have been shown to co-precipitate with HSP90 when carrying out immunoadsorption studies, and to exist in cytosolic heterocomplexes with it. In a number of cases, variations in HSP90 expression or HSP90 mutation has been shown to degrade signaling function via the protein or to impair a specific function of the protein (such as steroid binding, kinase activity) in vivo. Ansamycin antibiotics, such as geldanamycin and radicicol, inhibit HSP90 function (7). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.

Molekulargewicht: approx. 90 kDa

Gen-ID: 3326

NCBI Accession: NP_031381

UniProt: P08238

Pathways: Regulation of Cell Size