HSP70 High Sensitivity
|Product Name||HSP70 High Sensitivity ELISA kit|
|Description||Sandwich High Sensitivity ELISA kit for Quantitative Detection of HSP70. 96wells/kit|
|Cite This Product||HSP70 High Sensitivity ELISA kit (Boster Biological Technology, Pleasanton CA, USA, Catalog # EK7009)|
|Cross Reactivity||There is no detectable cross-reactivity.|
|Pack Size||96wells/kit, with removable strips.|
*Sensitivity, or Lower Limit of Detection (LLD), is the minimum level of target protein the ELISA assay can detect. We measure 20 blank wells and if the O.D. value is 2 standard deviations higher than the blanks' average O.D. the sample can be deemed positive.
|Assay Range||0.55 - 35 ng/ml|
*This assay range is determined using common samples. For samples with low target protein concentrations, users can adjust the standard curve to extend the lower limit of assay range.
|Sample Type||Cell lysates, Plasma, Serum, Tissue|
*The above listed samples are the ones valided with the assay. If you do not see your sample of interest listed, as long as there is enough level of target protein present in the sample, this Picokine? ELISA kit should detect it.
**For protocol and tips regarding preparing your sample of interest, please check our ELISA sample preparation guide.
|Storage||Store the kit at 4°C. The reagents are stable until expiration of the kit. Do not expose reagent to heat, sun, or strong light. Avoid multiple freeze-thaw cycles(Shipped with wet ice.)|
|Anti-Hsp70 Immunoassay Plate||12x8x1 Microwells|
|Recombinant Hsp70 Standard||2 vials|
|Standard and Sample Diluent||1 vial/ 50 ml|
|10X Wash Buffer Concentrate||1 vial/100 ml|
|Anti-Hsp70 Biotinylated Antibody Concentrate||1 vial/150 ?l|
|Anti-Hsp70 Biotinylated Antibody Diluent||1 vial/ 13 ml|
|Streptavidin: HRP Concentrate||1 vial/50 ?l|
|Streptavidin: HRP Diluent||1 vial/ 13 ml|
|TMB Substrate||1 vial/ 13 ml|
|Stop Solution||1 vial/ 13 ml|
HSP70 genes encode abundant heat-inducible 70-kDa HSPs (HSP70s). In most eukaryotes HSP70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 5O% identity. The N-terminal two thirds of HSP70s are more conserved than the C-terminal third. HSP70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides. When HSC70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half. The structure of this ATP binding domain displays multiple features of nucleotide binding proteins. All HSP70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the HSP70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. The universal ability of HSP70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport.