Recombinant Human Heat Shock Protein β-11/HSPB11

Instruction Manual!

Product name:	Recombinant Human Heat Shock Protein β-11/HSPB11
Source:	E.coli
Purity:	Greater than 95% as determined by reducing SDS-PAGE.
Buffer Formulation:	Supplied as a 0.2 μm filtered solution of 20mM TrisHCl, 100mM NaCl, 2mM DTT, 10% Glycerol, pH 8.0.
Applications:	Applications:SDS-PAGE; WB; ELISA; IP.
Storage:	Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months.
UOM:	100ug/50ug/200ug/1mg/1g

Source	E.coli
Description	Recombinant Human Heat Shock Protein beta-11 is produced by our E.coli expression system and the target gene encoding Met1-Ser144 is expressed with a 6His 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 TrisHCl, 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) as determined by LAL test.
Amino Acid Sequence	MGSSHHHHHHSSGLVPRGSHMRKIDLCLSSEGSEVILATSSDEKHPPENIIDGNPETFWTTTGMF PQEFIICFHKHVRIERLVIQSYFVQTLKIEKSTSKEPVDFEQWIEKDLVHTEGQLQNEEIVAHDG SATYLRFIIVSAFDHFASVHSVSAEGTVVSNLSS
Background	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.