HSPA1A ELISA Kit (Bovine)
Referencia OKEH00647
embalaje : 96Wells
Marca : Aviva Systems Biology
Contact local distributor :
Teléfono : +1 850 650 7790
HSPA1A ELISA Kit (Bovine) (OKEH00647)
| Datasheets/Manuals | Printable datasheet for HSPA1A ELISA Kit (Bovine) (OKEH00647) |
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| Predicted Species Reactivity | Bos taurus|Bovine | ||||||||||||||||||||||
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| Application | ELISA-Sandwich | ||||||||||||||||||||||
| ELISA Kit Detection Method | Colorimetric, OD450 nm | ||||||||||||||||||||||
| ELISA Kit Duration | ~ 3 Hours | ||||||||||||||||||||||
| ELISA Kit Principle | Aviva Systems Biology HSPA1A ELISA Kit (Bovine) (OKEH00647) is based on standard sandwich enzyme-linked immuno-sorbent assay technology. An antibody specific for HSPA1A has been pre-coated onto a 96-well plate (12 x 8 Well Strips) and blocked. Standards or test samples are added to the wells, incubated and removed. A biotinylated detector antibody specific for HSPA1A is added, incubated and followed by washing. Avidin-Peroxidase Conjugate is then added, incubated and unbound conjugate is washed away. An enzymatic reaction is produced through the addition of TMB substrate which is catalyzed by HRP generating a blue color product that changes yellow after adding acidic stop solution. The density of yellow coloration read by absorbance at 450 nm is quantitatively proportional to the amount of sample HSPA1A captured in well. | ||||||||||||||||||||||
| ELISA Kit Range | 0.78-50ng/mL | ||||||||||||||||||||||
| ELISA Kit Recovery | Mean recovery when spiking into sample matrices at concentrations within the dynamic range: 106% | ||||||||||||||||||||||
| ELISA Kit Reproducibility | Mean Intra-assay CV%: < 5.5% (n = 20) Mean Inter-assay CV%: < 8.9% (n = 20) | ||||||||||||||||||||||
| ELISA Kit Component |
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| Reconstitution and Storage | Store as indicated in product manual. | ||||||||||||||||||||||
| Sample Type | Serum, Plasma, Tissue homogenates, Cell culture supernates, Other biological fluids | ||||||||||||||||||||||
| Sensitivity | 0.23 ng/mL | ||||||||||||||||||||||
| Specificity | Natural and recombinant Bovine Heat shock 70 kDa protein 1A | ||||||||||||||||||||||
| Assay Info | Assay Methodology: Quantitative Sandwich ELISA |
| Gene Symbol | HSPA1A |
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| Gene Full Name | heat shock protein family A (Hsp70) member 1A |
| Alias Symbols | 70 kda heat shock protein-2, chaperone, heat shock 70 kD protein 1, heat shock 70 kD protein 2, heat shock 70 kDa protein 1, heat shock 70 kDa protein 1A, heat shock 70 kDa protein 1B, heat shock 70 kDa protein 2, heat shock 70kDa protein 1A, heat shock 70kDa protein 1B, Heat Shock Protein 70, heat-shock 70-kilodalton protein 1A, heat-shock 70-kilodalton protein 1B, HSP70, HSP70-1, HSP70-2, HSP70.1, HSP70.2, HSPA1, HSPA1B, HSPA2. |
| NCBI Gene Id | 282254 |
| Protein Name | Heat shock 70 kDa protein 1A |
| Description of Target | 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. 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. 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. Enhances STUB1-mediated SMAD3 ubiquitination and degradation and facilitates STUB1-mediated inhibition of TGF-beta signaling. Essential for STUB1-mediated ubiquitination and degradation of FOXP3 in regulatory T-cells (Treg) during inflammation. Negatively regulates heat shock-induced HSF1 transcriptional activity during the attenuation and recovery phase period of the heat shock response. |
| Uniprot ID | Q27975 |
| Protein Accession # | NP_776975.1 |
| Nucleotide Accession # | NM_174550.1 |
| Protein Size (# AA) | 641 |
| Molecular Weight | 70 kDa |
