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product summary
company name : 
Boster
product type : 
antibody
product name : 
Anti-Hsp90 alpha/HSP90AA1 Antibody Picoband™
catalog : 
PB9089
quantity : 
100μg/vial
clonality : 
polyclonal
host : 
domestic rabbit
conjugate : 
nonconjugated
reactivity : 
human, mouse, rat
application : 
western blot, immunocytochemistry, flow cytometry, immunohistochemistry - paraffin section
product information
SKU : 
PB9089
Product Name : 
Anti-Hsp90 alpha/HSP90AA1 Antibody Picoband™
Size : 
100μg/vial
Clonality : 
Polyclonal
Host : 
Rabbit
Reactivity : 
Human, Mouse, Rat
Application(s) : 
Flow Cytometry, IF, IHC-P, ICC, WB
Application Details : 
Western blot, 0.1-0.5µg/ml, Human, Rat.
Immunohistochemistry (Paraffin-embedded Section), 0.5-1µg/ml, Human, Mouse, Rat, By Heat. 
Immunocytochemistry , 0.5-1µg/ml, Human.
Immunocytochemistry/Immunofluorescence, 5µg/ml, Human.
Flow Cytometry, 1-3μg/1x10^6 cells, Human.
Application 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.
Description : 
Boster Bio Anti-Hsp90 alpha/HSP90AA1 Antibody Picoband™ catalog # PB9089. Tested in Flow Cytometry, IF, IHC-P, ICC, WB applications. This antibody reacts with Human, Mouse, Rat.
Concentration : 
Adding 0.2 ml of distilled water will yield a concentration of 500 μg/ml.
Gene Name : 
HSP90AA1
Uniprot ID : 
P07900
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.
Form : 
Lyophilized
Contents : 
Each vial contains 5mg BSA, 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.
Purification : 
Immunogen affinity purified.
Cross-reactivity : 
No cross reactivity with other proteins
Storage : 
Store at -20˚C for one year from date of receipt. After reconstitution, at 4˚C for one month. It can also be aliquotted and stored frozen at -20˚C for six months. Avoid repeated freeze-thaw cycles.
Reconstitution : 
Add 0.2ml of distilled water will yield a concentration of 500ug/ml.
Gene Full Name : 
Heat shock protein HSP 90-alpha
Synonyms : 
Heat shock protein HSP 90-alpha; Heat shock 86 kDa; HSP 86; HSP86; Lipopolysaccharide-associated protein 2; LAP-2; LPS-associated protein 2; Renal carcinoma antigen NY-REN-38; HSP90AA1; HSP90A, HSPC1, HSPCA;
Protein Name : 
Heat shock protein HSP 90-alpha
Molecular Weight : 
84660 MW
Protein Function : 
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. 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.
Subcellular Localization : 
Cytoplasm. Melanosome. Cell membrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Recommended Detection Systems : 
Boster recommends Enhanced Chemiluminescent Kit with anti-Rabbit IgG (EK1002) for Western blot, and HRP Conjugated anti-Rabbit IgG Super Vision Assay Kit (SV0002-1) for IHC(P) and ICC.
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.
Research Category : 
Cancer, Chaperones, Heat Shock Proteins, Protein Trafficking, Signal Transduction, Tumor Biomarkers
company information
Boster
3942 B Valley Ave
Pleasanton, CA 94566
Pleasanton, CA 94566
boster@bosterbio.com
https://www.bosterbio.com925.485.4527
headquarters: USA
Premium Provider of Antibodies and ELISA Kits
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