Rat HSP90 alpha Monoclonal Antibody | anti-HSP86; Heat shock protein 90 alpha antibody

HSP90 alpha monoclonal antibody (9D2)

Cat. Num. AAA565149

• Gene Names: HSP90AA1; EL52; HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; LAP-2; HSP89A; HSP90A; HSP90N; HSPCAL1; HSPCAL4; HEL-S-65p
• Reactivity: Human, Chicken
• Applications: Flow Cytometry, Functional Assay, Immunocytochemistry, Immunohistochemistry, Immunoprecipitation, Western Blot
• Purity: Protein G affinity purified.
• Synonyms: HSP90 alpha; Monoclonal Antibody; HSP90 alpha monoclonal antibody (9D2); anti-HSP86; Heat shock protein 90 alpha antibody

• Host: Rat
• Reactivity: Human, Chicken
• Clonality: Monoclonal
• Isotype: IgG2a
• Clone Number: 9D2
• Specificity: Recognizes human and chicken HSP90alpha. Detects a band of ~90kDa by Western blot.
• Purity/Purification: Protein G affinity purified.
• Form/Format: Liquid. In PBS, pH 7.2, containing 50% glycerol and 0.09% sodium azide.
• Sequence Length: 732

• Applicable Applications for anti-HSP86; Heat shock protein 90 alpha antibody: Flow Cytometry (FC/FACS), Immunocytochemistry (ICC), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB)
• Application Notes: Flow Cytometry (1:100); Western Blot (1:1,000, colorimetric); Suggested dilutions/conditions may not be available for all applications.; Detects a band of ~90kDa by Western blot.
• Immunogen: Purified Hsp90 isolated from human therapeutic orchiectomy specimens.
• Preparation and Storage: Long term storage: -20 degree C; Avoid freeze/thaw cycles.

Western Blot (WB)

Related Product Information for anti-HSP86; Heat shock protein 90 alpha antibody

The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

Product Categories/Family for anti-HSP86; Heat shock protein 90 alpha antibody

Protein Synthesis & Folding; Proteolysis & Protein Degradation; Cell Death

NCBI and Uniprot Product Information

• NCBI GI #: 92090606
• NCBI GeneID: 3320
• UniProt Accession #: P07900; Q2PP14; Q5CAQ6; Q5CAQ7; Q9BVQ5; A8K500; B3KPJ9
• Molecular Weight: 98,161 Da
• NCBI Official Full Name: Heat shock protein HSP 90-alpha
• NCBI Official Synonym Full Names: heat shock protein 90kDa alpha family class A member 1
• NCBI Official Symbol: HSP90AA1
• NCBI Official Synonym Symbols: EL52; HSPN; LAP2; HSP86; HSPC1; HSPCA; Hsp89; Hsp90; LAP-2; HSP89A; HSP90A; HSP90N; HSPCAL1; HSPCAL4; HEL-S-65p
• NCBI Protein Information: heat shock protein HSP 90-alpha
• UniProt Protein Name: Heat shock protein HSP 90-alpha
• UniProt Gene Name: HSP90AA1
• UniProt Synonym Gene Names: HSP90A; HSPC1; HSPCA; HSP 86; HSP86; LAP-2; LPS-associated protein 2
• UniProt Entry Name: HS90A_HUMAN

NCBI Description

The protein encoded by this gene is an inducible molecular chaperone that functions as a homodimer. The encoded protein aids in the proper folding of specific target proteins by use of an ATPase activity that is modulated by co-chaperones. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2012]

Uniprot Description

Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved for instance in cell cycle control and signal transduction. Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity. This cycle probably induces conformational changes in the client proteins, thereby causing their activation. Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11274138, PubMed:11276205, PubMed:15577939, PubMed:15937123, PubMed:27353360).