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C251
Recombinant Human HSPb11/PP25
10ug
1200
1080
现货
国产
-
C251
Recombinant Human HSPb11/PP25
50ug
3520
3168
现货
国产
-
C251
Recombinant Human HSPb11/PP25
500ug
12320
11088
现货
国产
-
C251
Recombinant Human HSPb11/PP25
1mg
17600
15840
现货
国产
-
C251
Recombinant Human PP25/Hspb11
10ug
1200
1080
现货
国产
-
C251
Recombinant Human PP25/Hspb11
50ug
3520
3168
现货
国产
-
C251
Recombinant Human PP25/Hspb11
500ug
12320
11088
现货
国产
-
C251
Recombinant Human PP25/Hspb11
1mg
17600
15840
现货
国产
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Catalog# C251 Source E.coli Description Recombinant Human Heat Shock Protein β-11/HSPB11 is produced by our E. coli expression system. The target protein is expressed with sequence (Met1-Ser144) of Human HSPB11 fused with a His tag at the N-terminus. Names Heat Shock Protein Beta-11, Hspb11, Placental Protein 25, PP25, HSPB11, C1orf41 Accession # Q9Y547 Formulation Supplied as a 0.2 μm filtered solution of 20mM Tris-HCl, 100mM NaCl, 2mM DTT, 10% Glycerol, pH 8.0 Shipping The product is shipped on dry ice/ice packs. Storage Store at < -20°C, stable for 6 months after receipt.
Please minimize freeze-thaw cycles.Purity Greater than 95% as determined by reducing SDS-PAGE. Endotoxin Less than 0.1 ng/μg (1 IEU/μg). Amino Acid Sequence MGSSHHHHHHSSGLVPRGSHMRKIDLCLSSEGSEVILATSSDEKHPPENIIDGNPETFWTTTGMF PQEFIICFHKHVRIERLVIQSYFVQTLKIEKSTSKEPVDFEQWIEKDLVHTEGQLQNEEIVAHDG SATYLRFIIVSAFDHFASVHSVSAEGTVVSNLSSBackground Heat Shock Protein β-11 (HSPB11) is a stress-responsive protein that is required to deal with proteotoxic stresses. HSPB11 is composed of an IFT complex B composed of IFT88, IFT57, TRAF3IP1, IFT52, IFT27, HSPB11 and IFT20 and is detected in placenta. HSPB11 has beeb shown to form oligomeric complexes and prevent the aggregation of in vitro denaturated aldolase and glyceraldehyde-3-phosphate dehydrogenase in accordance with the chaperone model of HSPB1 and HSPB5. HSPB11 overexpression protected against etoposide-induced cell death that correlated with a decreased release of mitochondrial Cytochrome C into the cytosol. Inhibition of HSP90 function completely abrogated the protective effect of HSPB11. This data suggests that at least in the case of HSPB11, interaction with other chaperone machines besides HSPA1A may contribute to functional specificity and cellular functioning.