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Storage
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Store the unopened product at 2 - 8° C. Protect from light. Do not use past expiration date. |
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Gene ID
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15511 |
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Gene Symbol
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HSPA1A |
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Synonym
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dnaK-type molecular chaperone HSP70-1; FLJ54303; FLJ54370; FLJ54392; FLJ54408; FLJ75127; Heat shock 70 kDa protein 1/2; heat shock 70 kDa protein 1A/1B; heat shock 70kD protein 1A; heat shock 70kDa protein 1A; heat shock-induced protein; HSP70; HSP70.1/HSP70.2; HSP70-1; HSP70-1/HSP70-2; HSP70-1A; HSP70I; HSP72; HSPA1; HSPA1A; HSPA1B |
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Species
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Mouse |
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Specificity
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This assay has high sensitivity and excellent specificity for Mouse Total HSP70/HSPA1A. No significant cross-reactivity or Mouse Total HSP70/HSPA1A and analogues was observed. |
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Kit Components
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Assay plate (12 x 8 coated Microwells), Standard (Freeze dried), Biotin-antibody (60 x concentrate), HRP-avidin (20 x concentrate), Biotin-antibody Diluent, HRP-avidin Diluent, Sample Diluent, Wash Buffer (20 x concentrate), TMB Substrate, Stop Solution, Adhesive Strip (For 96 wells), Instruction manual |
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Notes
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Please contact our Technical Services with any questions regarding species reactivity |
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Standard Curve Range
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156.25--10000 pg/ml |
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Sensitivity
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125 pg/ml |
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Inter Assay
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CV%<10% |
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Intra Assay
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CV%<8% |
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Assay Type
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Sandwich ELISA |
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Suitable Sample Type
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serum, plasma, tissue homogenates, cell lysate, cell culture medium. |
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Sample Volume
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50-100ul |
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Applications
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ELISA |
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Typical Data
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ELISA: Mouse Total HSP70/HSPA1A ELISA Kit (Colorimetric) These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed. |
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Background
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The Hsp70 system interacts with extended peptide segments of proteins as well as partially folded proteins to prevent aggregation, remodel folding pathways, and regulate activity [7] When not interacting with a substrate peptide, Hsp70 is usually in an ATP bound state. Hsp70 by itself is characterized by a very weak ATPase activity, such that spontaneous hydrolysis will not occur for many minutes. As newly synthesized proteins emerge from the ribosomes, the substrate binding domain of Hsp70 recognizes sequences of hydrophobic amino acid residues, and interacts with them. This spontaneous interaction is reversible, and in the ATP bound state Hsp70 may relatively freely bind and release peptides. However, the presence of a peptide in the binding domain stimulates the ATPase activity of Hsp70, increasing its normally slow rate of ATP hydrolysis. When ATP is hydrolyzed to ADP the binding pocket of Hsp70 closes, tightly binding the now-trapped peptide chain. Further speeding ATP hydrolysis are the so-called J-domain cochaperones: primarily Hsp40 in eukaryotes, and DnaJ in prokaryotes. These cochaperones dramatically increase the ATPase activity of Hsp70 in the presence of interacting peptides. |
