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Human HSPA1B (Heat Shock 70kDa Protein 1B) ELISA Kit
Human HSPA1B (Heat Shock 70kDa Protein 1B) ELISA Kit
The Human (HSPA1B) Heat Shock 70kDa Protein 1B ELISA Kit measures Heat Shock 70Kda Protein 1B in samples. The plate has been pre-coated with Human HSPA1B antibody. HSPA1B present in the sample is added and binds to antibodies coated on the wells. And then biotinylated Human HSPA1B Antibody is added and binds to HSPA1B in the sample. Then Streptavidin-HRP is added and binds to the Biotinylated HSPA1B antibody. After incubation unbound Streptavidin-HRP is washed away during a washing step. Substrate solution is then added and color develops in proportion to the amount of Human HSPA1B. The reaction is terminated by addition of acidic stop solution and absorbance is measured at 450 nm.
Catalog No:
E6896Hu
Regular price
$595.00 USD
Regular price
$458.00 USD
Sale price
$595.00 USD
Unit price
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per
2.5 weeks
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Product Details
Species Reactivity
Human
Sensitivity
0.098 ng/mL
Detection Range
0.2-70 ng/mL
Sample Type
Serum, plasma, cell culture supernates
Incubation(s)
1.5 hour(s)
Research Areas
Neuroscience
Background
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 (PubMed: 24012426, PubMed: 26865365, PubMed: 24318877). Maintains protein homeostasis during cellular stress through two opposing mechanisms: protein refolding and degradation. Its acetylation/deacetylation state determines whether it functions in protein refolding or protein degradation by controlling the competitive binding of co-chaperones HOPX and STUB1. During the early stress response, the acetylated form binds to HOPX which assists in chaperone-mediated protein refolding, thereafter, it is deacetylated and binds to ubiquitin ligase STUB1 that promotes ubiquitin-mediated protein degradation (PubMed: 27708256). Regulates centrosome integrity during mitosis, and is required for the maintenance of a functional mitotic centrosome that supports the assembly of a bipolar mitotic spindle (PubMed: 27137183). Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling (PubMed: 24613385). Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation (PubMed: 23973223). (Microbial infection) In case of rotavirus A infection, serves as a post-attachment receptor for the virus to facilitate entry into the cell. Source: UniProt Consortium (2025)
Shipping Condition
Shipped on cold gel packs.
Storage Condition and Shelf Life
2-8C
Analyte
Heat Shock 70Kda Protein 1B
Regulatory Status
For Research Use Only
