Certificate of Analysis and Data Sheet

Source:
E.Coli

Catalog No.
HSP-090

Description :

HSP90 has been identified in the cytosol, nucleus and endoplasmic reticulum, and is reported to exist in many tissue types. In several tissues, including smooth muscle, HSP-90 comprises up to 2% of total cellular protein. HSP90 functions as a dimer, assembled as part of heterocomplex. It possesses ATP-binding site and low ATPase activity. HSP90 is able to associate with actin filaments in certain conditions. Another important property of HSP90 is the binding of unoccupied steroid hormone receptors. HSP90 has been characterized as a molecular chaperone able to keep the target protein in a folding-competent state. It has an enhanced chaperone activity in oligomeric form at high temperatures. HSP90 function is sensitive to bivalent cations concentration.
Recombinant HSP-90 produced in E.Coli is a single,non-glycosylated polypeptide chain containing 732 amino acids and having a molecular mass of 86.8kDa.
Recombinant HSP-90 is expressed with a -6xHis tag and purified by proprietary chromatographic techniques.

Physical Appearance:

Sterile filtered clorless solution.

Formulation:

The protein (1mg/ml) contains 20mM Tris-HCl, pH 7.4 and 100mM NaCl.

Stability:

Store at 4蚓 if entire vial will be used within 2-4 weeks.
Store, frozen at -20蚓 for longer periods of time.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.

Purity:

Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by reducing and non-reducing SDS-PAGE Coomassie.

Usage:

This material is offered by ProSpec-TechnoGene for research, laboratory or further evaluation purposes.

Latest Publications:

1. Glioma: What is the role of c-Myc, hsp90 and telomerase?
Mol Cell Biochem 2006 Feb;283(1-2):1-9
2. Targeting chaperones in transformed systems--a focus on Hsp90 and cancer.
Expert Opin Ther Targets 2006 Feb;10(1):37-50
3. The carboxy-terminal domain Of Hsp90: Modulation of chaperone function and cochaperone interaction by novobiocin. Evidence that coumarin antibiotics disrupt Hsp90 dimerization.
J Biol Chem 2006 Jan 17;
4. Correlation between crystal violet dissolution assay and manual colony counting on the in vitro effects of Hsp90-in hibitors.
J Exp Ther Oncol 2005;5(1):9-13
5. The phosphatase Ppt1 is a dedicated regulator of the molecular chaperone Hsp90.
EMBO J 2006 Jan 25;25(2):367-76
6. Substrate transfer from the chaperone hsp70 to hsp90.
J Mol Biol 2006 Feb 24;356(3):802-11