HSP90AB1 Rabbit Polyclonal Antibody

Specifications

Product Data
Applications	WB
Recommend Dilution	WB 1:500 - 1:2000
Reactivity	Human, Mouse
Host	Rabbit
Clonality	Polyclonal
Immunogen	Recombinant protein of human HSP90AB1
Formulation	Store at -20C or -80C. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3
Concentration	lot specific
Purification	Affinity purification
Conjugation	Unconjugated
Storage Condition	Store at -20°C as received.
Gene Name	heat shock protein 90kDa alpha family class B member 1
Database Link	NP_031381 Entrez Gene 15516 MouseEntrez Gene 3326 Human UniProt ID P08238
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. 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. The co-chaperones either regulate the intrinsic ATPase activity of the chaperones or recruit chaperones to specific substrates or subcellular compartments. When the ubiquitin ligase CHIP associates with the HSP70/HSP90 complex as a cofactor, the unfolded substrates are subjected to degradation by the proteasome. 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. They also play a role in vesicle formation and protein trafficking.
Synonyms	D6S182; HSP84; HSP90B; HSPC2; HSPCB
Reference Data
Protein Families	Druggable Genome, Stem cell - Pluripotency
Protein Pathways	Antigen processing and presentation, NOD-like receptor signaling pathway, Pathways in cancer, Progesterone-mediated oocyte maturation, Prostate cancer

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