Anti-CHIP (N-terminal) antibody produced in rabbit

Anti-CHIP (N-terminal) antibody produced in rabbit is suitable for immunoblotting at a working concentration of 1-2 μg/mL using HEK-293T cells lysate and mouse brain extract (S2 fraction). It was used for western blotting of the eluted immunoprecipitates of PHF-1 antibody or anti-FLAG M2 in a study.

CHIP is a dual-function chaperone/E3 ubiquitin ligase that plays a crucial role in regulating protein quality control at multiple levels. It is comprised of a N-terminal tetratricopeptide repeat (TPR), a U-box at its C-terminus and a highly charged internal region. It ubiquitinates Hsp70, a cytosolic chaperone and enhances refolding of stress damaged proteins. Additionally, it has E3 ubiquitin ligase activity and triggers proteasome degradation of irreversibly damaged proteins to prevent cellular toxicity. The ubiquitination, aggregation and degradation of several proteins involved in neurodegenerative disorders including tau, huntingtin, Cu/Zn SOD1, ataxin-1, and α-synuclein are regulated by CHIP and Hsp70. The aggregation and toxicity of polyglutamine (polyQ) expanded proteins is suppressed by CHIP. It also regulates stress-dependent apoptosis.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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