- CITATIONS: 1
|Application ||WB, IHC-P, FC, E|
|Other Accession||P34058, P11499, Q4R4T5, Q04619, Q76LV1, Q9GKX8|
|Predicted||Bovine, Chicken, Horse, Monkey, Mouse, Rat|
|Calculated MW||83264 Da|
|Antigen Region||438-465 aa|
|Other Names||Heat shock protein HSP 90-beta, HSP 90, Heat shock 84 kDa, HSP 84, HSP84, HSP90AB1, HSP90B, HSPC2, HSPCB|
|Target/Specificity||This HSP90AB1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 438-465 amino acids from the Central region of human HSP90AB1.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||HSP90AB1 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||HSP90B, HSPC2, HSPCB|
|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.|
|Cellular Location||Cytoplasm. Melanosome. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV|
Provided below are standard protocols that you may find useful for product applications.
HSPCB are highly conserved molecular chaperones that have key roles in signal transduction, protein folding, protein degradation, and morphologic evolution. This protein normally associate with other cochaperones and play important roles in folding newly synthesized proteins or stabilizing and refolding denatured proteins after stress.
Hoffmann T., Hovemann B.Gene 74:491-501(1988)
Mason A., O'Connor D., Greenhalf W.Submitted (JUN-2000)
Wright L., Barril X., Dymock B.,Chem. Biol. 11:775-785(2004)
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