Recombinant Human HSPB11 Protein (His Tag) | PKSH032522

Recombinant Human HSPB11 Protein (His Tag) | PKSH032522 | Gentaur US, UK & Europe Disrtribition

Synonyms: Heat Shock Protein Beta-11; Hspb11; Placental Protein 25; PP25; HSPB11; C1orf41

Active Protein: N/A

Activity: 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.

Protein Construction: 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.

Fusion Tag: N-6His

Species: Human

Expressed Host: E.coli

Shipping: This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at<-20°C.

Purity: > 95 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.

Molecular Mass: 18.5 kDa

Formulation: Supplied as a 0.2 μm filtered solution of 20mM TrisHCl, 100mM NaCl, 2mM DTT, 10% Glycerol, pH 8.0.

Reconstitution: Not Applicable

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.

Research Area: Signal Transduction,