Antibody Details
Product Details
ImmunogenFull-length Hsp90 purified from chicken brain
Product PreparationPurified by Protein G affinity chromatography
Storage and HandlingThis antibody is stable for at least one (1) year at -20°C. This antibody recognizes human, mouse, rat, rabbit, bovine, porcine, and chicken Hsp90alpha (90 kDa).
Regulatory StatusFor in vitro investigational use only. Not for
use in therapeutic or diagnostic procedures.
Applications and Recommended Usage?
Quality Tested by LeincoImmunoblotting: use at 1-5ug/mL. A band of ~90 kDa is detected.
Immunoprecipitation: 5ug on 20ul Protein A-Sepharose + 100ul sample.
These are recommended concentrations. User should determine optimal concentrations for their application.
Positive control: Heat-shocked HeLa cell lysate.
Each investigator should determine their own optimal working dilution for specific applications. See directions on lot specific datasheets, as information may periodically change.
Description
SpecificityThis antibody recognizes human, mouse, rat, rabbit, bovine, porcine, and chicken Hsp90alpha (90 kDa).
BackgroundHsp90 and the 94 kDa glucose-regulated protein, Grp94, are major molecular chapeones of the cytosol and endoplasmic reticulum. In mammalian cells, there are at least two Hsp90 isoforms, Hsp90alpha and Hsp90beta, which are encoded by separate genes. All known members of the Hsp90 family are highly conserved, especially in the N-terminal and C-terminal regions. In the absence of stress, Hsp90 is an essential component of cellular processes such as hormone signaling and cell cycle control. Several regulatory proteins such as steroid receptors, cell cycle kinases and p53 have been identified as substrates of Hsp90.
Antigen Details
FunctionMolecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate rUniProtKB:P07900}.
Research AreaHeat Shock & Stress Proteins
References & Citations
Schuh S et al. 1985 J Biol Chem 260: 14292-14296
Sullivan WP et al. 1985 Biochemistry 24: 4214-4222.