HSP10 Rabbit Polyclonal Antibody

SKU AP06170PU-N

HSP10 rabbit polyclonal antibody, Aff - Purified

Product Data

• Application: ELISA, IHC, WB
• Recommended Dilution:

  Western blot: 1/500-1/1000.; Immunohistochemistry on paraffin sections: 1/50-1/200.; Immunofluorescence: 1/50-1/200.

• Reactivity: Human, Mouse, Rat
• Antibody Host: Rabbit
• Clonality: Polyclonal
• Immunogen: Synthetic peptide, corresponding to amino acids 30-100 of Human HSP10.
• Specificity: This antibody detects endogenous levels of HSP10 protein.; (region surrounding Lys80)
• Buffer: Phosphate buffered saline (PBS), pH 7.2.; State: Aff - Purified; State: Liquid purified Ig fraction; Preservative: 0.05% sodium azide
• Concentration: 1.0 mg/ml
• Purification: Affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE)
• Conjugation: Unconjugated
• Storage: Store undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer.; Avoid repeated freezing and thawing.
• Stability: Shelf life: one year from despatch.
• Shipping: Blue Ice
• Predicted Protein Size: ~ 10 kDa
• Background: The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, including the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the low molecular weight HSPs, the immunophilins and the HSP 110 family. The low molecular weight family includes HSP 10, HSP 20, HSP 27 (Heme Oxygenase 1), HSP 32 and HSP 40. Chaperonins are ubiquitous, indispensable proteins that facilitate protein folding in an ATP-dependent manner, enhancing the yield of properly folded substrate protein under conditions where spontaneous folding does not occur. Chaperonins are typified by the E. coli heat-shock proteins GroEL and GroES (HSP 10). HSP 10 is a heptameric ring of identical 10 kDa subunits that binds to each end of GroEL to form a symmetric, functional heterodimer.

Reference Data