Western blot shows lysates of HeLa human cervical epithelial carcinoma cell line and C2C12 mouse myoblast cell line untreated (-) or treated (+) with 100 J/m2UV-C for 30 minutes. PVDF membrane was probed with 0.1 µg/mL ...read more
HSP27 phosphorylated at S78/S82 was detected in immersion fixed HeLa human cervical epithelial carcinoma cell line unstimulated (lower panel) or stimulated with 20 mJ/cm2ultraviolet radiation (upper panel) using Rabbit ...read more
Enrichment of TICs decreases PP2A activity and increases Hsp27 activation in other solid tumors.CCS and HCW colorectal cancer cells, A549 lung cancer cells, HTB186 medulloblastoma cells and SAS, oral cancer cells were ...read more
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
Preservative
No Preservative
Concentration
LYOPH
Reconstitution Instructions
Reconstitute at 0.2 mg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for HSP27 [p Ser78, p Ser82, p Ser82] Antibody [Unconjugated]
28 kDa heat shock protein
DKFZp586P1322
Estrogen-regulated 24 kDa protein
Heat shock 27 kDa protein
heat shock 27kD protein 1
heat shock 27kDa protein 1
heat shock protein beta-1
HMN2B
HS.76067
HSP25
HSP27
HSP27HSP 27
HSP28CMT2F
HSPB1
SRP27
Stress-responsive protein 27
Background
Heat shock proteins (HSPs) are a family of highly conserved stress response proteins. Heat shock proteins function primarily as molecular chaperones by facilitating the folding of other cellular proteins, preventing protein aggregation or targeting improperly folded proteins to specific degradative pathways. HSPs are typically expressed at low levels under normal physiological conditions but are dramatically up-regulated in response to cellular stress. Elevated levels of HSPs have been observed in association with ischemia/reperfusion, cancer, and chronic heart failure. HSP27 is a member of the small heat shock protein family, which also includes HSP25 and the alpha -crystallins. HSP27 forms a large oligomer and the extent of phosphorylation plays a role in determining specific functions. HSP27 also functions as an anti-apoptotic molecule, regulating apoptosis through direct interaction with key components of the apoptotic pathway. HSP27 binds and sequesters cytochrome c released from the mitochondria in response to an apoptotic stimulus. This prevents the proper assembly of the apoptosome and subsequently, the activation of procaspase-9 and procaspase-3.
Gusev, N.B. et al. (2002) Biochemistry (Moscow) 67:511.
Garrido, C. et al. (2001) Biochem. Biophys. Res. Commun. 286:433.
Garrido, C. (2002) Cell Death Diffr. 9:483.
Brvey, J-M. et al. (2000) Nat. Cell Biol. 2:645.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
Caspase 8 - a key mediator of apoptosis Programmed cell death via apoptosis is a key controlled physiological process instigated by the cell death receptor family, their ligands, and the caspase cysteine protease family. All caspases exist in a precursor form that contains a prodomain, a... Read full blog post.
FLICE, FLICE, baby Cell death via apoptosis is a fundamental cellular function triggered by the cell death receptor family and their ligands which signal through downstream adaptor molecules and the caspase protease family. All caspases exist in a precursor form compose... Read full blog post.
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