HSP90 Protein (partial)

Catalog No. ABIN1686706

Product Details

Target: HSP90 (Heat Shock Protein 90 (HSP90))

Protein Type: Recombinant

Protein Characteristics: partial

Origin: Plasmodium falciparum

Source: Escherichia coli (E. coli)

Application: SDS-PAGE (SDS), Western Blotting (WB)

Sequence: QPVLEINPNH FIIKQLNHLI QIDKMNLQNS EIAEQIFDVA SMQGGYTIDD TGLFAKRVIG MMEKNAEQYL MNVQSNISNN TLNNNTSGSE MPQNNSPNEL QSEMKSTNGI DDNSNISENK INESSSNQNN IGENSIAEEN NIKNIAESDV NKINLGENDV SQNTMHKQDS GLFNLDPSIL NSNMLSGSDK TLL

Specificity: ~21.4 kDa

Purification: Affinity Purified

Purity: >90%

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: 50 mM Tris/HCl pH 7.5, 300 mM NaCl, 10 % glycerol

Storage: -20 °C

Target Details

Target: HSP90 (Heat Shock Protein 90 (HSP90))

Alternative Name: Hsp90 (HSP90 Products)

Synonyms: EL52 Protein, HSP86 Protein, HSP89A Protein, HSP90A Protein, HSP90N Protein, HSPC1 Protein, HSPCA Protein, HSPCAL1 Protein, HSPCAL4 Protein, HSPN Protein, Hsp89 Protein, Hsp90 Protein, LAP2 Protein, git10 Protein, swo1 Protein, HSP90 Protein, htpG Protein, SCBAC25F8.08 Protein, 23.m06066 Protein, 17.m07646 Protein, HSP90-1 Protein, 143198_at Protein, 83 Protein, 83K HSP Protein, DMHSP82 Protein, E(sev)3A Protein, E(sina)2 Protein, HSP82 Protein, HSP83 Protein, ORF1 Protein, Su(Raf)3A Protein, anon-EST:Liang-2.53 Protein, anon-WO0068693 Protein, anon-WO0140519.209 Protein, clone 2.53 Protein, en(lz)3C/4C Protein, hsp84 Protein, l(3)j5C2 Protein, ms(3)08445 Protein, stc Protein, DmelCG1242 Protein, CG1242 Protein, Hsp86 Protein, Hspca Protein, 86kDa Protein, 89kDa Protein, AL024080 Protein, AL024147 Protein, Hsp86-1 Protein, hsp4 Protein, hsp86 Protein, hsp89 Protein, hsp90 Protein, hsp90a Protein, hspc1 Protein, hspca Protein, hspn Protein, lap2 Protein, Hsp90alpha Protein, heat shock protein 90 alpha family class A member 1 Protein, heat shock protein Hsp90 Protein, Hsp90 chaperone Protein, Heat shock protein 90 Protein, heat shock protein 90 Protein, chaperone protein HtpG Protein, molecular chaperone HtpG Protein, Heat Shock Protein 90 Protein, uncharacterized LOC100384473 Protein, Heat shock protein 83 Protein, heat shock protein 90, alpha (cytosolic), class A member 1 Protein, heat shock protein 90 alpha family class B member 1 Protein, heat shock protein 90kDa alpha family class A member 1 L homeolog Protein, heat shock protein HSP 90-alpha Protein, HSP90AA1 Protein, hsp90 Protein, HSP90 Protein, daf-21 Protein, htpG Protein, SCO7516 Protein, MAP_RS10510 Protein, TP04_0646 Protein, TP01_0934 Protein, APH_RS03525 Protein, GbCGDNIH1_0315 Protein, MAV_2118 Protein, HSP90C Protein, BBOV_IV008400 Protein, BBOV_III007380 Protein, ACICU_00312 Protein, ECL_01244 Protein, YE105_C1172 Protein, pco153543(105) Protein, Hsp83 Protein, Hsp90aa1 Protein, HSP90AB1 Protein, hsp90aa1.1.L Protein, LOC108698781 Protein

Background: HSP90 is an abundantly and ubiquitously expressed heat shock protein. It is understood to exist in two principal forms alpha and beta, which share 85 % sequence amino acid homology. The two isoforms of HSP90 are expressed in the cytosolic compartment (1). Despite the similarities, HSP90alpha exists predominantly as a homodimer while HSP90beta exists mainly as a monomer (2). From a functional perspective, HSP90 participates in the folding, assembly, maturation, and stabilization of specific proteins as an integral component of a chaperone complex (3-6). Furthermore, HSP90 is highly conserved between species, having 60 % and 78 % amino acid similarity between mammalian and the corresponding yeast and Drosophila proteins, respectively. HSP90 is a highly conserved and essential stress protein that is expressed in all eukaryotic cells. 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 (7-8). 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 immune adsorption 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 (9). Recently, Prof. Tatu's laboratory has shown the importance of HSP90 in parasite growth. They have shown that inhibition of P. Falciparum HSP90 (PfHSP90), blocks the erythrocytic cycle by inhibiting stage transformation, leading to inhibition of parasite growth (10, 11). Looking for more information on HSP90? Visit our new HSP90 Scientific Resource Guide at http://www.HSP90.ca.

Molecular Weight: approx. 23.4 kDa

Gene ID: 811999

NCBI Accession: XP_001348591

UniProt: Q8IL32

Pathways: M Phase, Regulation of Cell Size, Signaling Events mediated by VEGFR1 and VEGFR2, VEGFR1 Specific Signals