Human HSPA1A ELISA Kit

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Product name Human HSPA1A ELISA Kit
Short Description Human ELISA Kit to HSPA1A
Description The kit is a sandwich enzyme immunoassay for in vitro quantitative measurement of HSP-70 in human serum, plasma and other biological fluids
Applications ELISA
Dilution range 0.781--50ng/mL
Protein Name Heat shock 70 kDa protein 1A
Heat shock 70 kDa protein 1
HSP70-1
HSP70.1
Storage Instruction Store at 4°C for 6 months.
Note For Research Use Only (RUO).
Validated Application ELISA
Conjugation Unconjugated
Concentration 50ng/mL
Gene ID 3303
Gene Symbol HSPA1A
Molecular Weight 70.1 kDa
Database Links HGNC:5232
OMIM:140550
Reactome:R-HSA-168330
Alternative Names Heat shock 70 kDa protein 1A
Heat shock 70 kDa protein 1
HSP70-1
HSP70.1
Function Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes, Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation, This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones, The co-chaperones have been shown to not only regulate different steps of the ATPase cycle, but they also have an individual specificity such that one co-chaperone may promote folding of a substrate while another may promote degradation, The affinity for polypeptides is regulated by its nucleotide bound state, In the ATP-bound form, it has a low affinity for substrate proteins, However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins, It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release, The co-chaperones are of three types: J-domain co-chaperones such as HSP40s (stimulate ATPase hydrolysis by HSP70), the nucleotide exchange factors (NEF) such as BAG1/2/3 (facilitate conversion of HSP70 from the ADP-bound to the ATP-bound state thereby promoting substrate release), and the TPR domain chaperones such as HOPX and STUB1 In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell.
Post-translational Modifications In response to cellular stress, acetylated at Lys-77 by NA110 and then gradually deacetylated by HDAC4 at later stages, Acetylation enhances its chaperone activity and also determines whether it will function as a chaperone for protein refolding or degradation by controlling its binding to co-chaperones HOPX and STUB1, The acetylated form and the non-acetylated form bind to HOPX and STUB1 respectively, Acetylation also protects cells against various types of cellular stress,
Cellular Localization Cytoplasm
Tissue Specificity Serum, Plasma, Biological Fluids
Swiss-Prot Key P0DMV8
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