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[pSer78]HSP27 (human), ELISA kit

Most comprehensive portfolio of heat shock protein (chaperone) products commercially available.
 
ADI-900-165 96 wells 342.00 USD
Do you need bulk/larger quantities?
 
  • Ultra-sensitive and specific - be confident with your results and use less sample per test
  • Quantitative - obtain statistically significant results compared to semi-quantitative Western blot analysis
  • Higher throughput - assay up to 40 samples in duplicate in just 3 hours
The [pSer78]HSP27 (human), EIA kit is a colorimetric immunometric enzyme immunoassay kit with results in 3 hours.

Product Specification

Alternative Name:Heat shock protein 27
 
Sensitivity:4.30 pg/ml (range 31.25 - 1000 pg/ml)
 
Assay Time:3 hours
 
Applications:ELISA, Colorimetric detection
 
Application Notes:For the quantitative determination of human [pSer78]HSP27 in cell lysates, plasma, and serum.
 
Species reactivity:Human
 
Crossreactivity:Phospho HSP27 (Ser78) (100%), HSP27 (non-phospho) (0.1%) and <0.03%: HSP25, HSP40, HSP70, HSP90, αB Crystallin, αA Crystallin
 
Use/Stability:Store all components at +4°, except standard at -20°.
 
Shipping:Shipped on Blue Ice
 
Kit/Set Contains:Microtiter plate, Conjugate, Antibody, Assay buffer 27, Wash buffer concentrate, Standard, TMB Substrate, 5X Extraction reagent, Stop solution 2
 
Scientific Background:Hsp27 is one of the most common members of the highly conserved and ubiquitously expressed family of small heat shock proteins (sHsp), which also includes αB-crystallin. It is characterized by a conserved C-terminal alpha-crystallin domain consisting of two anti-parallel beta-sheets that promote oligomer formation required for its primary chaperone function as inhibitor of irreversible protein aggregation. Hsp27 oligomerization is modulated by post-translational phosphorylation of Hsp27 at three serine residues, Ser15, Ser78, and Ser82, by a variety of protein kinases including MAPKAPK-3, PKAc-α, p70 S6K, PKD I, and PKC-δ;. Hsp27 has been shown to inhibit actin polymerization by binding of unphosphorylated Hsp27 monomers to actin intermediate filaments. Anti-apoptotic functions of Hsp27 have also been identified through interactions with DAXX7, activation of Akt, and inhibition of apoptosome formation. Evidence suggests altered expression of Hsp27 is implicated in the pathogenesis of breast, ovarian, and prostate cancer.
 
UniProt ID:P04792
 
GenBank ID:L39370
 

Product Literature References

Release of Phosphorylated HSP27 (HSPB1) from Platelets Is Accompanied with the Acceleration of Aggregation in Diabetic Patients: H. Tokuda, et al.; PLoS One 10, e0128977 (2015), Application(s): ELISA using human supernatant, Abstract; Full Text

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