Mouse HSP70 ELISA Kit | HSPA1A elisa kit

Mouse HSP70 ELISA Kit

Cat. Num. AAA8291412

• Gene Names: Hspa1a; Hsp72; hsp68; Hsp70-3; Hsp70.3; hsp70A1
• Reactivity: Mouse
• Synonyms: HSP70; Mouse HSP70 ELISA Kit; HSPA1; HSX70; Heat shock 70 kDa protein 1A/1B; Heat shock 70 kDa protein 1/2; HSP70-1/HSP70-2; HSP70.1/HSP70.2; HSPA1A elisa kit

• Reactivity: Mouse
• Specificity: The Mouse HSP70 ELISA Kit allows for the detection and quantification of endogenous levels of natural and/or recombinant Mouse HSP70 proteins within the range of 156 pg/ml - 10000 pg/ml.
• Sequence Length: 641

• Samples: Cell culture supernates, serum, plasma, cell lysates, tissue homogenates
• Sensitivity: < 80 pg/ml
• Preparation and Storage: Store at 4 degree C for 6 months, store at -20 degree C for one year. Avoid freeze/thaw cycles.

Typical Testing Data/Standard Curve (for reference only)

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Related Product Information for HSPA1A elisa kit

Principle of the Assay: The Mouse HSP70 ELISA (Enzyme-Linked Immunosorbent Assay) kit is an in vitro enzyme-linked immunosorbent assay for the quantitative measurement of Mouse HSP70 in Cell Culture Supernates, Serum, Plasma, Cell Lysates, Tissue Homogenates. This assay employs an antibody specific for Mouse HSP70 coated on a 96-well plate. Standards and samples are pipetted into the wells and HSP70 present in a sample is bound to the wells by the immobilized antibody. The wells are washed and biotinylated anti-Mouse HSP70 antibody is added. After washing away unbound biotinylated antibody, HRP-conjugated streptavidin is pipetted to the wells. The wells are again washed, a TMB substrate solution is added to the wells and color develops in proportion to the amount of HSP70 bound. The Stop Solution changes the color from blue to yellow, and the intensity of the color is measured at 450 nm.

Background/Introduction: The heat shock proteins are a highly conserved family of stress response proteins. HSPs function primarily as molecular chaperones, facilitating the folding of other cellular proteins, preventing protein aggregation, or targeting improperly folded proteins to specific degradative pathways. Some HSPs are expressed at low levels under normal physiological conditions but show dramatically increased expression in response to cellular stress, others are constitutively expressed. Specific HSPs play a role in regulating apoptosis by interacting directly with key components of the apoptotic pathway.

NCBI and Uniprot Product Information

• NCBI GI #: 124339829
• NCBI GeneID: 193740
• NCBI Accession #: NP_034609.2
• NCBI GenBank Nucleotide #: NM_010479.2
• UniProt Accession #: Q61696; Q61697; Q7TQD8; Q9QWJ5
• Molecular Weight: 70,079 Da
• NCBI Official Full Name: heat shock 70 kDa protein 1A
• NCBI Official Synonym Full Names: heat shock protein 1A
• NCBI Official Symbol: Hspa1a
• NCBI Official Synonym Symbols: Hsp72; hsp68; Hsp70-3; Hsp70.3; hsp70A1
• NCBI Protein Information: heat shock 70 kDa protein 1A
• UniProt Protein Name: Heat shock 70 kDa protein 1A
• Protein Family: HSP70 co-chaperone
• UniProt Gene Name: Hspa1a
• UniProt Synonym Gene Names: Hsp70-3; Hsp70A1; HSP70.3

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.