Bovine Heat Shock 70kDa Protein 1A (HSPA1A) RTU ELISA Kit | HSPA1A rtu elisa kit

Bovine Heat Shock 70kDa Protein 1A (HSPA1A) ELISA Kit

Cat. Num. AAA459953

• Reactivity: Bovine
• Synonyms: Heat Shock 70kDa Protein 1A (HSPA1A); Bovine Heat Shock 70kDa Protein 1A (HSPA1A) ELISA Kit; HSP70-1; HSP-A1A; HSPA1; HSP70-2; HSX70; HSPA1A rtu elisa kit

• Reactivity: Bovine
• Sequence Length: 641

• Assay Type: Sandwich
• Samples: Serum, Plasma, Tissue Homogenates, Cell Lysates, Cell Culture Supernates or Other Biological Fluids.
• Detection Range: 1.56-100ng/mL
• Sensitivity: 0.61ng/mL
• RTU ELISA Kit's Advantage: The Ready-To-Use (RTU) Kits require fewer steps in setup and take less time to run. Detection Solutions are pre-diluted and total incubation time is shorter than many other ELISA Kits.
• Preparation and Storage: For unopened kits: All the reagents should be kept at 4 degree C upon receipt.; For opened kits: Once the kit is opened, the remaining reagents still need to be stored according to the above storage conditions. In addition, return the unused wells to the foil pouch containing the desiccant pack and reseal along entire edge of zip-seal.

Typical Testing Data/Standard Curve (for reference only)

Related Product Information for HSPA1A rtu elisa kit

Test Principle: The microtiter plate provided in this kit has been pre-coated with an antibody specific to HSPA1A. Standards or samples are then added to the appropriate microtiter plate wells with a biotin-conjugated antibody preparation specific to HSPA1A. Next, Avidin conjugated to Horseradish Peroxidase (HRP) is added to each microplate well and incubated. After TMB substrate solution is added, only those wells that contain HSPA1A, biotin-conjugated antibody and enzyme-conjugated Avidin will exhibit a change in color. The enzyme-substrate reaction is terminated by the addition of sulphuric acid solution and the color change is measured spectrophotometrically at a wavelength of 450nm ± 10nm. The concentration of HSPA1A in the samples is then determined by comparing the O.D. of the samples to the standard curve.

NCBI and Uniprot Product Information

• NCBI GI #: 40254806
• NCBI GeneID: 281825
• NCBI Accession #: NP_776975.1
• NCBI GenBank Nucleotide #: NM_174550.1
• UniProt Accession #: Q27975; Q27964; Q6DLW1; Q7YQF7
• Molecular Weight: 70,259 Da
• UniProt Protein Name: Heat shock 70 kDa protein 1A
• Protein Family: Heat shock 70 kDa protein
• UniProt Gene Name: HSPA1A
• UniProt Synonym Gene Names: HSP70-1; HSP70.1

Uniprot Description

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.