84-1130-39　Heat Shock Protein 90, P. falciparum (hsp90) 25ug　H1831-58L

特徴

• HSP90 is an abundantly and ubiquitously expressed heat shock protein.
• It is understood to exist in two principal forms A and B, which share 85% sequence amino acid homology.
• The two isoforms of Hsp90 are expressed in the cytosolic compartment (1).
• Despite the similarities, HSP90a exists predominantly as a homodimer while HSP90b 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).
• Applications:Suitable for use in Immunofluorescence and Western Blot.
• Other applications not tested.
• Recommended Dilution:Immunofluorescence:1:50 Western Blot:1:2000Optimal dilutions to be determined by the researcher.
• Storage and Stability:May be stored at 4°C for short-term only.
• Aliquot to avoid repeated freezing and thawing.
• Store at -20°C.
• Aliquots are stable for at least 12 months.
• For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.