HSP70/HSC70 | Heat shock protein 70/Heat shock cognate protein 70 (serum)
AS05 083 | Clonality: Polyclonal | Host: Rabbit | Reactivity: [global abtibody] for HSP70 and HSC70 in fish, mammals and fungi
|Data sheet||Product citations||Protocols||Add review|
10 µg of total protein from (1) killi fish muscle, (2) bovine muscle, (3) chicken muscle, (4) rat liver, extracted with Protein Extration Buffer, PEB (AS08 300) and separated on 4-12% NuPage (Invitrogen) LDS-PAGE and blotted 1h to PVDF. Blots were blocked in 5 % non-fat milk for 1h at room temperature with agitation. Blots were incubated in the primary antibody at a dilution of 1: 5000 (in blocking reagent) for 1h at room temperature with agitation. The antibody solution was decanted and the blot was rinsed briefly twice, then washed once for 15 min and 3 times for 5 min in TBS-T at room temperature with agitation. Blots were incubated in secondary antibody (Agrisera anti-rabbit IgG horse radish peroxidase conjugated, AS09 602) diluted to 1:25 000 in blocking reagent for 1h at room temperature with agitation. The blots were washed as above and developed for 5 min with chemiluminescent detection reagent, according to the manufacturers instructions. Images of the blots were obtained using a CCD imager (FluorSMax, Bio-Rad) and Quantity One software (Bio-Rad). Exposure time was 5 min.
For detection of plant and algal cytoplasmic hsp70 we recommend following product: AS08 371.
Heat shock protein 70 (Hsp70) is the major stress-inducible protein in vertebrates and is highly conserved throughout evolution. It plays a role as a molecular chaperone and is important for allowing cells to cope with acute stress or insult, especially those affecting the protein machinery. Heat shock cognate protein 70 (HSC70) is a highly conserved protein and a member of the family of molecular chaperones. Alternative names: HSP70.1, HSP70-1/HSP70-2, Heat shock 70 kDa protein 8
Bessemer et al. (2014). Cardiorespiratory toxicity of environmentally relevant zinc oxide nanoparticles in the freshwater fish Catostomus commersonii. Nanotoxicology. 2014 Nov 27:1-10.
Gorovits et al. (2013). Recruitment of the host plant heat shock protein 70 by tomato yellow leaf curl virus coat protein is required for virus infection. PLoS Once, July 23;8(7).