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Dog/Canine Heat Shock Protein 70 HSP70 ELISA Kit
BG-CAN11212
Dog/Canine Heat Shock Protein 70 ELISA KitFor research use only. Not for use in diagnostic procedures.For general protocol and instruction, please click the following links:Quantitative Elisa Kit InstructionSandwich ELISA kit general instruction
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Dog/Canine Heat Shock Protein 70 ELISA Kit
| Assay principle | The Canine HSP70 ELISA Kit is based on standard sandwich enzyme-linked immunosorbent assay technology. Anti-Canine HSP70 specific antibody has been pre-coated onto 96-well plate. Canine HSP70 present in the standards/ samples bind to the capture antibody. Subsequently, biotinylated anti-Canine HSP70 detection antibody is added to form an Ab-Ag-Ab sandwich. After a washing step, streptavidin-HRP is added and the unbound conjugate is removed with wash buffer. Next, addition of HRP substrate, TMB, results in the production of a blue colored product that changes to yellow after the addition of acidic Stop Solution. The density of yellow color is directly proportional to the amount of Canine HSP70 captured on plate. |
| Sample Type | Cell lysates, serum/ plasma and other suitable sample solution. |
| Assay Time | 4.5 Hours |
| Assay Range | 0.125 – 8 ng/mL |
| Sensitivity | 17.5 pg/mL |
| Specificity | No cross reactivity with relevant targets |
| Sample Level | May varies from condtion to condition |
| Dilution Factor | 1/2- 1/8 |
| Background | The heat shock proteins are a highly conserved family of stress response proteins. The Hsp70 family of heat shock protiens contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. 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. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway. |
Different lot may vary, please follow the instruction coming with the kit.