Product Pathways - Protein Stability
HSP90β (D3F2) Rabbit mAb #7411
|7411S||100 µl (10 western blots)||---||In Stock||---|
|7411||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey, Bovine, Pig||Endogenous||90||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting
Species predicted to react based on 100% sequence homology: Chicken, Horse.
Specificity / Sensitivity
HSP90β (D3F2) Rabbit mAb recognizes endogenous levels of total HSP90β protein. This antibody does not cross-react with HSP90α.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Glu471 of human HSP90β protein.
Western blot analysis of extracts from various cell lines using HSP90β (D3F2) Rabbit mAb.
Isoform specificity of HSP90 antibodies using human recombinant HSP90α and HSP90β expressed in Spodoptera frugiperda cells. Purified proteins (100 ng each) were resolved by SDS-PAGE and detected by western blot using HSP90β (D3F2) Rabbit mAb (left panel), HSP90β Antibody #5087 (center panel), or HSP90 Antibody #4874 (right panel).
HSP70 and HSP90 are molecular chaperones expressed constitutively under normal conditions to maintain protein homeostasis and are induced upon environmental stress (1). Both HSP70 and HSP90 are able to interact with unfolded proteins to prevent irreversible aggregation and catalyze the refolding of their substrates in an ATP- and co-chaperone-dependent manner (1). HSP70 has a broad range of substrates including newly synthesized and denatured proteins, while HSP90 tends to have a more limited subset of substrates, most of which are signaling molecules. HSP70 and HSP90 often function collaboratively in a multi-chaperone system, which requires a minimal set of co-chaperones: HSP40, Hop, and p23 (2,3). The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments (1,4). When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome (4). The biological functions of HSP70/HSP90 extend beyond their chaperone activity. They are essential for the maturation and inactivation of nuclear hormones and other signaling molecules (1,3). They also play a role in vesicle formation and protein trafficking (2).
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For Research Use Only. Not For Use In Diagnostic Procedures.
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