Recombinant Human HSP27 Protein, CF

Catalog # Availability Size / Price Qty
1580-HS-050
R&D Systems Recombinant Proteins and Enzymes
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Recombinant Human HSP27 Protein, CF Summary

Product Specifications

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.
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.
Source
E. coli-derived human HSP27 protein
Thr2-Lys205, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
Thr2
Predicted Molecular Mass
23.6 kDa
SDS-PAGE
28 kDa, reducing conditions

Product Datasheets

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1580-HS

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

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.
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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
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

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Recombinant Human HSP27 Protein, CF
By Anonymous on 11/07/2018
Application: In vitro bioactivity in cell culture