HSC82

  • Official Full Name

    Hsp90 family chaperone HSC82
  • Overview

    The budding yeast Saccharomyces cerevisiae has two genes, HSP82 and HSC82, that encode homologues of HSP90. HSC82 is a molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control. Cells overexpressing Hsc82 are hypersensitive to various stresses including high concentrations of NaCl. The phenotypes associated with the sensitivity to salt stress of Hsc82-overexpressing cells are similar to those of calcineurin-defective mutants.
  • Synonyms

    HSP90;Hsp90 family chaperone HSC82;82 kDa heat shock cognate protein;ATP-dependent molecular chaperone HSC82;Heat shock protein Hsp90 constitutive isoform
Cat.# Product name Source (Host) Species Tag Protein Length Price

    Involved Pathway

    HSC82 involved in several pathways and played different roles in them. We selected most pathways HSC82 participated on our site, such as , which may be useful for your reference. Also, other proteins which involved in the same pathway with HSC82 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.

    Pathway Name Pathway Related Protein

    Protein Function

    HSC82 has several biochemical functions, for example, . Some of the functions are cooperated with other proteins, some of the functions could acted by HSC82 itself. We selected most functions HSC82 had, and list some proteins which have the same functions with HSC82. You can find most of the proteins on our site.

    Function Related Protein

    Interacting Protein

    HSC82 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with HSC82 here. Most of them are supplied by our site. Hope this information will be useful for your research of HSC82.

    Resources

    References

    • Kawano, T; Kobayakawa, T; et al. A comprehensive study on the immunological reactivity of the Hsp90 molecular chaperone. JOURNAL OF BIOCHEMISTRY 136:711-722(2004).

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