Recombinant Human HSP27 Protein, CF

R&D Systems, part of Bio-Techne | Catalog # 1580-HS

R&D Systems, part of Bio-Techne
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1580-HS-050
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Key Product Details

Source

E. coli

Accession #

P04792

Conjugate

Unconjugated

Applications

Inhibition Activity

View all HSP27 Proteins and Enzymes »

Product Specifications

Source

E. coli-derived human HSP27 protein
Thr2-Lys205, with a C-terminal 6-His tag

Purity

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.

Endotoxin Level

<1.0 EU per 1 μg of the protein by the LAL method.

N-terminal Sequence Analysis

Thr2

Predicted Molecular Mass

23.6 kDa

SDS-PAGE

28 kDa, reducing conditions

Activity

Measured by its ability to inhibit apoptosis in human neutrophils. Sheth, K. et al. (2001) J. Surg. Res. 99:129.
1 μg/mL of Recombinant Human HSP27 will reduce neutrophil apoptosis by more than 25%.
Optimal dilutions should be determined by each laboratory for each application.

Reviewed Applications

Read 1 review rated 5 using 1580-HS in the following applications:

Formulation, Preparation and Storage

1580-HS
Formulation Supplied as a 0.2 μm filtered solution in HEPES, NaCl and DTT.
Shipping The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °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. 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.

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

Alternate Names

HSP25, HSPB1

Entrez Gene IDs

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

Gene Symbol

HSPB1

UniProt

P04792

Additional HSP27 Products

Product Documents for Recombinant Human HSP27 Protein, CF

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Product Specific Notices for Recombinant Human HSP27 Protein, CF

For research use only

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