HSP90AA1 Antibody (OABB01548)

Catalog No: OABB01548

Size:100UG

Anti-Hsp90 Picoband antibody
All lanes: Anti-HSP90(OABB01548) at 0.5ug/ml
Lane 1: Rat Liver Tissue Lysate at 40ug
Lane 2: Hela Whole Cell Lysate at 40ug
Lane 3: MCF-7 Whole Cell Lysate at 40ug
Lane 4: Raji Whole Cell Lysate at 40ug
Predicted bind size: 83 kDa
Observed bind size: 83 kDa

Anti-Hsp90 Picoband antibody
IHC(P): Human Intestinal Cancer Tissue

Anti-Hsp90 Picoband antibody
IHC(P): Mouse Brain Tissue

Anti-Hsp90 Picoband antibody
IHC(P): Rat Brain Tissue

Anti-Hsp90 Picoband antibody
ICC: A549 Cell

Anti-Hsp90 Picoband antibody
ICC: MCF-7 Cell

Product Info

• Tested Species Reactivity: Human, Mouse, Rat
• Predicted Species Reactivity: Human|Mouse|Rat
• Product Format: Lyophilized. Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.
• Clonality: Polyclonal
• Clone: Polyclonal
• Isotype: Rabbit IgG
• Host: Rabbit
• Application: Flow cytometry|Immunocytochemistry|Immunofluorescence|Immunohistochemistry|Western blot
• Additional Information: Notes: WB: The detection limit for Hsp90 is approximately 0.25ng/lane under reducing conditions.
  Tested Species: In-house tested species with positive results.
  By Heat: Boiling the paraffin sections in 10mM citrate buffer, pH6.0, for 20mins is required for the staining of formalin/paraffin sections.
  Other applications have not been tested.
  Optimal dilutions should be determined by end users.
  Background: Heat shock protein HSP 90-alpha is a protein that in humans is encoded by the HSP90AA1 gene. The gene, HSP90AA1, encodes the human stress-inducible 90-kDa heat shock protein alpha (Hsp90A). Complemented by the constitutively expressed paralog Hsp90B which shares over 85% amino acid sequence identity, Hsp90A expression is initiated when a cell experiences proteotoxic stress. Once expressed Hsp90A dimers operate as molecular chaperones that bind and fold other proteins into their functional 3-dimensional structures. This molecular chaperoning ability of Hsp90A is driven by a cycle of structural rearrangements fueled by ATP hydrolysis. Current research on Hsp90A focuses in its role as a drug target due to its interaction with a large number of tumor promoting proteins and its role in cellular stress adaptation.
• Reconstitution and Storage: 2°C to 8°C|-20°C
• Immunogen: E.coli-derived human Hsp90 alpha recombinant protein (Position: P2-V365). Human Hsp90 alpha shares 99% amino acid (aa) sequence identity with both mouse and rat Hsp90 alpha.
• Purification: Affinity Purified
• Concentration: 500 ug/ml
• Specificity: No cross reactivity with other proteins.
• Application Info: Western blot: 0.1-0.5 ug/ml: Human, Rat
  Immunohistochemistry (Paraffin-embedded Section): 0.5-1 ug/ml: Human, Mouse, Rat: By Heat
  Immunocytochemistry : 0.5-1 ug/ml: Human
  Immunocytochemistry/Immunofluorescence: 5 ug/ml: Human
  Flow Cytometry: 1-3 ug/1x10^6 cells: Human
• Storage Buffer: Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.
• Description: Rabbit IgG polyclonal antibody for Heat shock protein HSP 90-alpha(HSP90AA1) detection. Tested with WB, IHC-P, ICC, ICC/IF, FCM in Human;Mouse;Rat.

Target Info

• Gene Symbol: HSP90AA1
• Gene Full Name: heat shock protein 90 alpha family class A member 1
• Alias Symbols: EL52;epididymis luminal secretory protein 52;epididymis secretory sperm binding protein Li 65p;heat shock 86 kDa;heat shock 90kD protein 1, alpha;heat shock 90kD protein 1, alpha-like 4;heat shock 90kD protein, alpha-like 4;heat shock 90kDa protein 1, alpha;heat shock protein 90kDa alpha (cytosolic), class A member 1;heat shock protein 90kDa alpha family class A member 1;heat shock protein HSP 90-alpha;HEL-S-65p;HSP 86;Hsp103;HSP86;Hsp89;HSP89A;Hsp90;HSP90A;HSP90N;HSPC1;HSPCA;HSPCAL1;HSPCAL4;HSPN;LAP2;LAP-2;lipopolysaccharide-associated protein 2;LPS-associated protein 2;renal carcinoma antigen NY-REN-38.
• NCBI Gene Id: 3320
• Protein Name: Heat shock protein HSP 90-alpha
• Description of Target: 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 (PubMed:11274138, PubMed:15577939, PubMed:15937123, PubMed:27353360, PubMed:29127155). Engages with a range of client protein classes via its interaction with various co-chaperone proteins or complexes, that act as adapters, simultaneously able to interact with the specific client and the central chaperone itself (PubMed:29127155). Recruitment of ATP and co-chaperone followed by client protein forms a functional chaperone. After the completion of the chaperoning process, properly folded client protein and co-chaperone leave HSP90 in an ADP-bound partially open conformation and finally, ADP is released from HSP90 which acquires an open conformation for the next cycle (PubMed:27295069, PubMed:26991466). Apart from its chaperone activity, it also plays a role in the regulation of the transcription machinery. HSP90 and its co-chaperones modulate transcription at least at three different levels (PubMed:25973397). In the first place, they alter the steady-state levels of certain transcription factors in response to various physiological cues(PubMed:25973397). Second, they modulate the activity of certain epigenetic modifiers, such as histone deacetylases or DNA methyl transferases, and thereby respond to the change in the environment (PubMed:25973397). Third, they participate in the eviction of histones from the promoter region of certain genes and thereby turn on gene expression (PubMed:25973397). Binds bacterial lipopolysaccharide (LPS) and mediates LPS-induced inflammatory response, including TNF secretion by monocytes (PubMed:11276205). Antagonizes STUB1-mediated inhibition of TGF-beta signaling via inhibition of STUB1-mediated SMAD3 ubiquitination and degradation (PubMed:24613385).
• Uniprot ID: P07900
• Molecular Weight: 84660 MW