Human Hsp27 (phospho S82) Antibody Pair - BSA and Azide free is a kit containing recombinant capture and detector antibodies in a carrier-free formulation for the measurement of Human Hsp27 (phospho S82).
ELISA set
Human
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application sELISA | Reactivity Reacts | Dilution info - | Notes - |
Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state (PubMed:10383393, PubMed:20178975). Plays a role in stress resistance and actin organization (PubMed:19166925). Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (PubMed:23728742).
Heat shock protein beta-1, HspB1, 28 kDa heat shock protein, Estrogen-regulated 24 kDa protein, Heat shock 27 kDa protein, Stress-responsive protein 27, HSP 27, SRP27, HSPB1, HSP27, HSP28
Human Hsp27 (phospho S82) Antibody Pair - BSA and Azide free is a kit containing recombinant capture and detector antibodies in a carrier-free formulation for the measurement of Human Hsp27 (phospho S82).
Heat shock protein beta-1, HspB1, 28 kDa heat shock protein, Estrogen-regulated 24 kDa protein, Heat shock 27 kDa protein, Stress-responsive protein 27, HSP 27, SRP27, HSPB1, HSP27, HSP28
ELISA set
Human
Reagents
Blue Ice
+4°C
+4°C
+4°C
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.
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.
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.
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Sandwich ELISA of ab308542 with the capture antibody dilution at 2 µg/mL and detector antibody dilution at 0.5 µg/mL.
A549 + Anisomycin: A549 treated with 1 μg/ml anisomycin for 30 minutes, whole cell lysate. Serial dilutions of lysates were analyzed.
A549 Control: untreated A549, whole cell lysate. Serial dilutions of lysates were analyzed.
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