Histone H2A (Xenopus, recombinant)
Histone H2A (Xenopus, recombinant)
Histone H2A is a core histone that forms a dimer with histone H2B.{46631} Two histone H2A/H2B dimers form an octameric...
€818.00
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€365.00 €310.25
€365.00 €310.25
Heat shock protein 90 ? (Hsp90?) is the constitutively active cytosolic isoform of Hsp90 that is encoded by HSP90AB in humans.{17930} Hsp90 is a multidomain protein that functions as a molecular chaperone to assist in folding and activation of nascent peptides, refolding unfolded or misfolded proteins, and preventing protein aggregation.{15502} C-terminal dimerization of Hsp90, coupled with ATPase molecular clamp activity induces a conformational change in the N-terminal nucleotide binding domain that facilitates substrate binding and initiates the chaperone cycle.{17932} Hsp90 interacts with many co-chaperones during its chaperone cycle including p23 and Sba1, which help recruit substrates to the Hsp90 complex, Hsp70 (Item Nos. 22739 | 23002), which loads nascent polypeptides onto the Hsp90 dimer, and the ATPase activator Aha1 that promotes ATP hydrolysis and substrate release.{17931,41851} Hsp90 is overexpressed in cancer cells and stabilizes client proteins that promote oncogenesis, including transcription factors, signaling proteins, and kinases.{17930,41851} Hsp90 also decreases ?-synuclein fibril formation and toxicity as well as Q35 aggregation in in vitro models of Parkinson’s and Huntington’s disease, respectively, implying a role in neurodegenerative disease.{41852}
Territorial Availability: Available through Bertin Technologies only in France
| Size | 50 µg |
|---|---|
| Shipping | dry ice |
| Molecular weight | 0 |
| Purity | ≥65% as estimated by SDS-PAGE |
| Custom code | 3504.00 |
| UNSPSC code | 12352204 |
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Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.
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