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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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HSP90 alpha/beta Antibody / HSP90AA1 + HSP90AB1 recognizes members of the cytosolic heat shock protein 90 family, an abundant class of ATP-dependent molecular chaperones involved in protein folding, stabilization, maturation, and cellular stress responses. The two major cytosolic HSP90 isoforms are HSP90 alpha, encoded by HSP90AA1, and HSP90 beta, encoded by HSP90AB1. These closely related proteins share extensive sequence and structural similarity but differ in aspects of their expression and regulation.
HSP90 alpha is generally considered the more stress-inducible cytosolic isoform, whereas HSP90 beta is expressed more constitutively. Both proteins function as molecular chaperones for a diverse collection of client proteins. HSP90 activity is coordinated with co-chaperones and other heat shock proteins to maintain protein homeostasis, assist conformational maturation, and protect cells from the accumulation of improperly folded proteins.
The HSP90 chaperone system participates in numerous signaling pathways by stabilizing proteins involved in cell proliferation, survival, transcription, and signal transduction. Its client proteins include protein kinases, transcription factors, steroid hormone receptors, and other regulatory molecules. ATP binding and hydrolysis drive conformational changes within the HSP90 chaperone cycle, while co-chaperones influence client recognition, ATPase activity, and progression through different stages of protein maturation.
HSP90AA1 and HSP90AB1 have substantial functional overlap, but their regulation is not identical. Increased HSP90 alpha expression is associated particularly with cellular responses to heat and other forms of stress, while HSP90 beta contributes to basal proteostasis and essential cellular functions. The abundance and broad client network of the HSP90 family have also made these molecular chaperones important subjects in cancer biology, where HSP90 can support the stability of signaling proteins required by malignant cells.
An HSP90 alpha/beta Antibody capable of recognizing HSP90AA1 and HSP90AB1 provides a means of investigating the closely related cytosolic HSP90 proteins without restricting detection to a single isoform. Studies of HSP90 biology can contribute to research into proteostasis, cellular stress, molecular chaperone activity, signal transduction, protein folding, and cancer-associated signaling.
NSJ Bioreagents offers clone EBD-8 as a rabbit monoclonal reagent for researchers studying the cytosolic HSP90 chaperone system. An HSP90 alpha/beta Antibody can support investigation of HSP90AA1 and HSP90AB1 in studies of protein homeostasis, cellular stress responses, and chaperone-dependent signaling.
Explore our Signal Transduction Antibodies page for additional reagents targeting proteins involved in intracellular signaling and regulatory pathways.
Optimal dilution of the HSP90 alpha/beta Antibody / HSP90AA1 + HSP90AB1 should be determined by the researcher.
A synthetic peptide specific to human HSP90 alpha/beta was used as the immunogen for the HSP90 alpha/beta antibody.
Store the HSP90 alpha/beta antibody at -20oC.
HSP90AA1 antibody, HSP90AB1 antibody, HSP90 alpha antibody, HSP90 beta antibody, Heat shock protein HSP 90-alpha antibody, Heat shock protein HSP 90-beta antibody, HSP90A antibody, HSP90B antibody
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