HSP90AB1 Rabbit Polyclonal Antibody

CAT#: TA326919

Rabbit anti-HSP90AB1 Polyclonal Antibody

Product Images

Western blot analysis of extracts of variouscell lines, using HSP90AB1 antibody.

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  Immunohistochemistry of paraffin-embedded human breast cancer using HSP90AB1 antibody at dilution of 1:500 (200x lens).

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  Immunohistochemistry of paraffin-embedded rat pancreas using HSP90AB1 antibody at dilution of 1:500 (200x lens).

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  Immunohistochemistry of paraffin-embedded mouse kidney using HSP90AB1 antibody at dilution of 1:500 (200x lens).

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  Immunofluorescence analysis of U2OS cell using HSP90AB1 antibody. Blue: DAPI for nuclear staining.

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Specifications

Product Data

• Applications: ICC/IF, IHC, WB
• Recommended Dilution: WB 1:500 - 1:2000;IHC 1:50- 1:200;IF 1:50- 1:200
• Reactivities: Human, Mouse, Rat, Monkey
• Host: Rabbit
• Isotype: IgG
• 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: Store at -20°C as received.
• Stability: Stable for 12 months from date of receipt.
• Gene Name: heat shock protein 90kDa alpha family class B member 1
• Database Link:
  NP_031381
  Entrez Gene 15516 MouseEntrez Gene 301252 RatEntrez Gene 702293 MonkeyEntrez 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