• Species Reactivity

  Human

• Specificity

  Detects human HSP27 when dually phosphorylated at S78/S82 in Western blots.    
   

• Source

  Recombinant Monoclonal Rabbit IgG Clone # 1026B

• Purification

  Protein A or G purified from cell culture supernatant

• Immunogen

  Phosphopeptide containing the human HSP27 S78/S82 site

  Accession # P04792

• Formulation

  Supplied as a 0.2 μm filtered solution in PBS containing BSA, Glycerol and Sodium Azide. *Small pack size (SP) is supplied as a 0.2 µm filtered solution in PBS.

• Label

  Unconjugated

Applications

• Recommended    
  Concentration

  Sample

• Western Blot

  1:1000 dilution

  See below

• 
  

• Immunocytochemistry

  1:100 dilution

  See below

• 
  

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Data Examples

Preparation and Storage

• Shipping

  The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C

• Stability & Storage

• 12 months from date of receipt, -20 °C as supplied.

• 1 month, 2 to 8 °C under sterile conditions after opening.

• 6 months, -20 °C under sterile conditions after opening.

Background: HSP27

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. Ser78 and Ser82 of HSP27 are phosphorylated in vivo in response to growth factors or heat shock, and the extent of phosphorylation plays a role in determining specific functions. HSP27 forms a large oligomer and 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.

• References:

1. Gusev, N.B. et al. (2002) Biochemistry (Moscow) 67:511.

2. Garrido, C. et al. (2001) Biochem. Biophys. Res. Commun. 286:433.

3. Garrido, C. (2002) Cell Death Diffr. 9:483.

4. Brvey, J-M. et al. (2000) Nat. Cell Biol. 2:645.

• Long Name:

  Heat Shock Protein 27

• Entrez Gene IDs:

  3315 (Human); 15510 (Mouse); 24471 (Rat)

• Alternate Names:

  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