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Rat HSP70/HSPA1A ELISA Kit

Catalog Number: AYQ-E10433
Lead time: 3-4 business days
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$0.00
Products specifications
Storage Store the unopened product at 2 - 8° C. Protect from light. Do not use past expiration date.
Gene ID 24472
Gene Symbol HSPA1A
Synonym 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
Species Rat
Specificity This assay has high sensitivity and excellent specificity for Rat HSP70/HSPA1A. No significant cross-reactivity or Rat HSP70/HSPA1Aand analogues was observed.
Kit Components 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
Notes Please contact our Technical Services with any questions regarding species reactivity
Standard Curve Range 125--8000 pg/ml
Sensitivity 100 pg/ml
Inter Assay CV%<10%
Intra Assay CV%<8%
Assay Type Sandwich ELISA
Suitable Sample Type serum, plasma, tissue homogenates, cell lysate, cell culture medium.
Sample Volume 50-100ul
Applications ELISA
Typical Data ELISA: Rat 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.
Background 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.
Assay Solution's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.