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Home / Primary Antibodies / Polyclonal Antibodies

HSP90 (P. falciparum) Antibody - SPC-187

BHA11907238
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Swissprot Q8IL32
Accession Number XP_001348591.1
Gene Id 811999
Target HSP90
Research Area Cancer, Heat Shock, Cell Signaling, Chaperone Proteins, Tumor Biomarkers, Protein Trafficking
Buffer PBS pH7.4, 50% glycerol, 0.09% sodium azide
Concentration 1.56 mg/ml
Dilutions WB (1:2000), ICC/IF (1:50); optimal dilutions for assays should be determined by the user.
Purification Protein A Purified
Scientific 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.
Shipping Temperature Blue Ice or 4°C
Specificity Detects ~ 86kDa. Specific to P. falciparum and does not cross-react to HSP90 from Human, yeast, and dictyostelium.
Storage -20ÂşC
Storage Buffer PBS pH7.4, 50% glycerol, 0.09% sodium azide *Storage buffer may change when conjugated
Storage Temperature -20°C
Applications IP, WB, ICC/IF
Description WB ; ICC ; IF ; IP
Dilution WB (1:2000), ICC/IF (1:50); optimal dilutions for assays should be determined by the user.
Product Manual SDS
SDS
Reference 1. Nemoto T., et al. (1997) J. Biol Chem. 272: 26179-26187.

2. Minami Y., et al. (1991) J. Biol Chem. 266: 10099-10103.

3. Arlander S.J.H., et al. (2003) J. Biol Chem. 278: 52572-52577.

4. Pearl H., et al. (2001) Adv Protein Chem. 59: 157-186.

5. Neckers L., et al. (2002) Trends Mol Med. 8: S55-S61.

6. Pratt W., Toft D. (2003) Exp Biol Med. 228: 111-133.

7. Pratt W., Toft D. (1997) Endocr Rev. 18: 306–360.

8. Pratt W.B. (1998) Proc Soc Exptl Biol Med. 217: 420–434.

9. Whitesell L., et al. (1994) Proc Natl Acad Sci USA. 91: 8324–8328.

10. Banumathy G., Singh V., Pavithra S.R., and Tatu U. (2003) J Biol Chem. 278(20): 18336-45.

11. Pavithra S.R, Banumathy G., Joy O., Singh V., and Tatu U. (2004) J Biol Chem. 279(45):46692-9.
Combination SKU Supplier No. Conjugate Size Your price Quantity
BHA11907238-1 SPC-187D Unconjugated 100 ug $330
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BHA11907238-2 SPC-187C Unconjugated 25 ug $167
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BHA11907238-3 SPC-187D-A390 ATTO 390 100 ug $384
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BHA11907238-4 SPC-187D-A488 ATTO 488 100 ug $383
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BHA11907238-5 SPC-187D-A594 ATTO 594 100 ug $383
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BHA11907238-6 SPC-187D-ALP Alkaline Phosphatase 100 ug $376
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BHA11907238-7 SPC-187D-APC APC 100 ug $382
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BHA11907238-8 SPC-187D-BI Biotin 100 ug $378
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BHA11907238-9 SPC-187D-FITC FITC 100 ug $374
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BHA11907238-10 SPC-187D-HRP HRP 100 ug $370
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BHA11907238-11 SPC-187D-PCP PerCP 100 ug $382
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BHA11907238-12 SPC-187D-RPE RPE 100 ug $380
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BHA11907238-13 SPC-187S Unconjugated 12 ug $44
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