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

CHIP (carboxy terminus of Hsp70-interacting protein, also known as STIP1-homology and U-box containing protein 1, STUB1, HSPABP2, NY-CO-7, SDCCAG7, UBOX1), is a dual-function chaperone/E3 ubiquitin ligase. CHIP has 3 functional domains: a N-terminal tetratricopeptide repeat (TPR), a U-box at its C-terminus, and a highly charged internal region. It is located on human chromosome 16p13.3.

Anti-CHIP (C-terminal) antibody produced in rabbit has been used in western blotting and histology to stain testes and ovary sections.

Anti-CHIP (C-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).

CHIP (carboxy terminus of Hsp70-interacting protein) plays a crucial role in regulating protein quality control at multiple levels. 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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