|Application ||WB, IHC-P, FC, E|
|Other Accession||Q66HA8, Q60446, Q0IIM3|
|Predicted||Bovine, Hamster, Rat|
|Calculated MW||96865 Da|
|Antigen Region||549-579 aa|
|Other Names||Heat shock protein 105 kDa, Antigen NY-CO-25, Heat shock 110 kDa protein, HSPH1, HSP105, HSP110, KIAA0201|
|Target/Specificity||This HSPH1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 549-579 amino acids from the Central region of human HSPH1.|
|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||HSPH1 Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||HSP105, HSP110, KIAA0201|
|Function||Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release (PubMed:24318877). Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities (By similarity).|
|Tissue Location||Highly expressed in testis. Present at lower levels in most brain regions, except cerebellum. Overexpressed in cancer cells.|
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abgent to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
HSPH1 prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. This protein inhibits HSPA8/HSC70 ATPase and chaperone activities.
Ishihara K., Yasuda K., Hatayama T.Biochim. Biophys. Acta 1444:138-142(1999)
Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y.,DNA Res. 3:321-329(1996)
The MGC Project Team Genome Res. 14:2121-2127(2004)
Miyazaki M., Nakatsura T., Yokomine K., Senju S., Monji M., Hosaka S.,Cancer Sci. 96:695-705(2005)
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