HSP90AB1 Protein (full length)

Catalog No. ABIN1686667

This Recombinant HSP90AB1 protein is expressed in Baculovirus infected Insect Cells and has been mentioned in 3+ publications.

Quick Overview for HSP90AB1 Protein (full length) (ABIN1686667)

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

Protein Type: Recombinant

Biological Activity: Active

Origin: Human

Source: Baculovirus infected Insect Cells

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

Purity: >90%

Product Details

Protein Characteristics: full length

Sequence: 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

Specificity: ~90 kDa

Purification: Affinity Purified | Endotoxin-free

Biological Activity Comment: ATPase active

Application Details

Application Notes: Optimal working dilution should be determined by the investigator.

Comment:

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

Restrictions: For Research Use only

Handling

Concentration: Lot specific

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

Storage: -20 °C

References

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).

Target Details

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

Alternative Name: Hsp90 beta

Background: 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.

Molecular Weight: approx. 90 kDa

Gene ID: 3326

NCBI Accession: NP_031381

UniProt: P08238

Pathways: Regulation of Cell Size