Description
Product Usage Information
SignalFlex™ conjugates are produced using highly validated Cell Signaling Technology ® primary antibodies and conjugation methods that have been rigorously tested, ensuring high-quality conjugates and lot-to-lot consistency. These conjugates are quality control tested by size exclusion chromatography (SEC) to determine antibody integrity. However, they are not tested on specific assays. Optimal dilutions/concentrations should be determined by the end user. When performing flow cytometry, we recommend using an isotype control conjugate at the same concentration as the antibody conjugate.
Storage
Supplied in PBS (pH 7.2), less than 0.1% sodium azide, and 2 mg/mL BSA. Store at 4°C. Do not aliquot the antibody. Protect from light. Do not freeze.
Specificity / Sensitivity
HSP90 (C45G5) Rabbit mAb (SignalFlex™ mFluor™ Red 780 Conjugate) detects endogenous levels of total HSP90 protein. This antibody does not cross-react with other HSPs.
Species Reactivity: Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide surrounding Asn300 of human HSP90.
Background
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).
Alternate Names
D6S182; EL52; epididymis luminal secretory protein 52; epididymis secretory sperm binding protein Li 65p; FLJ26984; FLJ31884; Heat shock 84 kDa; Heat shock 86 kDa; heat shock 90kD protein 1, alpha; heat shock 90kD protein 1, alpha-like 4; heat shock 90kD protein 1, beta; heat shock 90kD protein, alpha-like 4; heat shock 90kDa protein 1, alpha; heat shock 90kDa protein 1, beta; heat shock protein 90 alpha family class A member 1; heat shock protein 90 alpha family class B member 1; heat shock protein 90 kDa; heat shock protein 90kDa alpha (cytosolic), class A member 1; heat shock protein 90kDa alpha (cytosolic), class B member 1; heat shock protein 90kDa alpha family class A member 1; heat shock protein 90kDa alpha family class B member 1; heat shock protein beta; Heat shock protein HSP 90-alpha; Heat shock protein HSP 90-beta; HEL-S-65p; HS90A; HS90B; HSP 84; HSP 86; HSP 90; Hsp103; HSP84; HSP86; Hsp89; HSP89A; Hsp90; HSP90-BETA; HSP90A; HSP90AA1; HSP90AB1; HSP90B; HSP90N; HSPC1; HSPC2; HSPCA; HSPCAL1; HSPCAL4; HSPCB; HSPN; LAP-2; LAP2; Lipopolysaccharide-associated protein 2; LPS-associated protein 2; Renal carcinoma antigen NY-REN-38
