Description
Key facts
Detection method:Colorimetric,
Sample types:Tissue Extracts, Cell Lysate,
Reacts with:Mouse, Rat, Human,
Assay type:Sandwich (quantitative),
Sensitivity:= 200 pg/mL,
Range:780 - 50000 pg/mL,
Assay time:4h 30m,
Assay Platform:Microplate
Product details:
HSP70 ELISA kit is designed for the accurate quantitative measurement of HSP70 in samples from Human, Mouse and Rat origins. This assay allows for the quantitative determination of inducible HSP70 from cell lysates and tissue extracts. Please use
ab133061
for the detection of Hsp70 in serum and plasma samples.
A HSP70 monoclonal antibody has been precoated onto 96-well plates. Standards or test samples are added to the wells, incubated and then washed. A HSP70 polyclonal antibody is then added, incubated and washed. An HRP conjugated anti-IgG antibody is then added, incubated. The plate is washed once more and the TMB substrate is then added which HRP catalyzes, generating a blue coloration after incubation. A stop solution is added which generates conversion to yellow color read at 450 nm which is proportional to the amount of analyte bound.
Get higher sensitivity in only 90 minutes with Human HSP70 ELISA Kit (ab187399) from our SimpleStep ELISA
range.
Inducible heat shock protein 70 (HSP70) is a stress protein whose expression is upregulated when the cell or organism is placed under conditions of stress. HSP70 is essential for cellular recovery, survival, and maintenance of normal cellular function. It is also a molecular chaperone that prevents protein aggregation and refolds damaged proteins in response to cellular stress caused by environmental insults, pathogens, and disease. Current research is aimed at exploiting HSP70's cellular protective abilities as a therapeutic strategy against damaging cellular stress.
In most mammals, the expression of inducible HSP70 is strictly stress inducible and can only be detected following a significant stress upon the cell or organism. However, in humans and primates, inducible HSP70 is present at basal levels and is upregulated in response to stress. The role of HSP70 has been studied in a variety of medically relevant models or conditions such as hyperthermia, hypertension, toxic exposure to chemical agents, hypoxia, ischemia, inflammation, autoimmunity, apoptosis, cancer, organ transplantation, and bacterial and viral infections. HSP70 has also been studied in the normal processes of aging, spermatogenesis, menstruation, and physical activity such as exercise.
REACH authorisation
Abcam has not and does not intend to apply for the REACH Authorisation of customers' uses of products that contain European Authorisation list (Annex XIV) substances.
It is the responsibility of our customers to check the necessity of application of REACH Authorisation, and any other relevant authorisations, for their intended uses.
Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-Multi, Appropriate long-term storage conditions-Multi, Storage information-Please refer to protocols
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
HSP70 also known as Heat Shock Protein 70 is a highly conserved molecular chaperone with a mass of approximately 70 kDa. The protein plays an important role in maintaining protein homeostasis by assisting in the proper folding of nascent and stress-denatured proteins. It is ubiquitously expressed in the cytoplasm and mitochondria of both prokaryotic and eukaryotic cells. The expression of HSP70 rapidly increases in response to stressors such as heat infection and inflammation providing a protective mechanism for the cell.
Biological function summary
Heat Shock Protein 70 assists in the protection of cells from protein aggregation and assists in the degradation of unstable proteins. As part of a larger molecular chaperone complex HSP70 interacts with co-chaperones like HSP40 and Bag1 to mediate these functions. Its role extends to modulating apoptosis and initiating repair mechanisms under cellular stress. The balance between its anti-apoptotic and pro-survival functions is essential in cell survival during stress conditions.
Pathways
Heat Shock Protein 70 participates significantly in the cellular stress response and protein repair pathways. It integrates into the protein quality control pathway where it collaborates with other chaperone proteins such as HSP90. This coordination ensures proper protein folding and prevents aggregation therefore maintaining cell function and integrity. Additionally HSP70 is involved in the NF-kB signaling pathway regulating stress-induced transcription factors and influencing inflammation and immune responses.
Heat Shock Protein 70 has connections to cancer and neurodegenerative diseases. In cancer HSP70 proteins can support tumor growth by inhibiting apoptosis and may contribute to resistance against chemotherapy. They interact notably with proteins like p53 in this context. While in neurodegenerative diseases like Alzheimer's HSP70 aids in preventing the aggregation of neurotoxic proteins such as tau and amyloid-beta therefore potentially slowing disease progression. Understanding these interactions emphasizes the duality of HSP70 as both protective in normal cells and potentially harmful in pathological states.
