Abcam, ab216949, Mouse Hsp27 ELISA Kit

Size: 1 x 96Tests
Mouse Hsp27 ELISA Kit is a single-wash 90-min Simplestep used to quantify Mouse Hsp27 with a sensitivity of 72 pg/ml. The assay uses a simple mix-wash-read protocol with just one incubation and one wash step. - Colorimetric Sandwich ELISA - 450 nm readout : works on any standard plate reader - Design your own immunoassay: we also offer the conjugation-ready antibody pair
Key facts
Detection method:Colorimetric,
Sample types:Cell culture extracts,
Reacts with:Mouse,
Assay type:Sandwich (quantitative),
Sensitivity:= 72 pg/mL,
Range:0.23 - 15 ng/mL,
Assay time:1h 30m,
Assay Platform:Pre-coated microplate (12 x 8 well strips)

Product details:
Mouse Hsp27 ELISA Kit (ab216949) is a single-wash 90 min sandwich ELISA designed for the quantitative measurement of Hsp27 protein in cell culture extracts. It uses our proprietary SimpleStep ELISA® technology. Quantitate Mouse Hsp27 with 72 pg/ml sensitivity.
SimpleStep ELISA® technology employs capture antibodies conjugated to an affinity tag that is recognized by the monoclonal antibody used to coat our SimpleStep ELISA® plates. This approach to sandwich ELISA allows the formation of the antibody-analyte sandwich complex in a single step, significantly reducing assay time. See the SimpleStep ELISA® protocol summary in the image section for further details. Our SimpleStep ELISA® technology provides several benefits:
- Single-wash protocol reduces assay time to 90 minutes or less
- High sensitivity, specificity and reproducibility from superior antibodies
- Fully validated in biological samples
- 96-wells plate breakable into 12 x 8 wells strips
A 384-well SimpleStep ELISA® microplate (
ab203359
) is available to use as an alternative to the 96-well microplate provided with SimpleStep ELISA® kits.
Heat shock proteins (HSPs) are molecular chaperones that facilitate the proper folding and function of proteins within the cell. Heat shock protein 27 (Hsp27), also known as heat shock protein beta-1 (HspB1) is a 209 amino acid protein encoded by the HSPB1 gene. Hsp27 a member of the sHsp (small heat shock protein) group, whose functions are chaperone activity, thermotolerance, inhibition of apoptosis, and regulation of cellular development and differentiation. Hsp70 member proteins may assist inhibition of apoptosis by acting on the caspase-dependent pathway and against agents such as tumor necrosis factor-alpha, staurosporine, and doxorubicin. Hsp27 can form oligomers depending on the phosphorylation state of the protein and during heat shock. The oligomers are connected to the chaperone activity, while dimers have limited activity. Hsp27 interacts with actin and intermediate filaments, which provides protection to actin filaments from fragmentation.
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-+4°C, Appropriate long-term storage conditions-+4°C, Storage information-+4°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Hsp27 also known as HSPB1 is a small heat shock protein with a molecular weight of approximately 27 kilodaltons. This protein is expressed in various tissues including muscle heart and brain. It functions as a molecular chaperone that stabilizes unfolded proteins preventing their aggregation. Hsp27 undergoes phosphorylation at specific residues which modulates its chaperone activity and interaction with other proteins.
Biological function summary
Hsp27 plays a critical role in cellular stress response by regulating actin cytoskeleton dynamics and inhibiting apoptosis. It forms part of a complex that includes other proteins such as alphaB-crystallin. This complex facilitates the reorganization of proteins under stress conditions enhancing cell survival during oxidative stress or thermal shock. Hsp27 also modulates inflammatory responses and has been shown to affect cell migration.
Pathways
Hsp27 integrates into the apoptosis and inflammation pathways. It interacts with apoptotic machinery such as caspase proteins to protect cells by hindering apoptosome formation. Additionally Hsp27 can engage with pathways involving the nuclear factor-kappa B (NF-kB) impacting inflammatory signaling. CPTC (carboxyl-pyrene-trioctylamine) can modulate these pathways by altering Hsp27 function and interactions.
Hsp27 has connections to neurodegenerative diseases and cancer. In neurodegenerative conditions such as Alzheimer's disease its chaperone activity is thought to protect neurons from misfolded protein aggregates. In cancer Hsp27 supports tumor cell survival and resistance to chemotherapy by interacting with proteins like Akt and p53. These interactions highlight the complex role of Hsp27 in modulating cellular responses in various pathological states.