COX6c Polyclonal Antibody

Cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. It is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may be involved in the regulation and assembly of the complex. This nuclear gene encodes subunit VIc, which has 77% amino acid sequence identity with mouse subunit VIc. COX6C is up-regulated in prostate cancer cells. A pseudogene has been found on chromosomes 16p12.

The COP1 Polyclonal Antibody is a highly specific and sensitive antibody designed for use in various research applications. This antibody is produced by immunizing rabbits with a synthetic peptide corresponding to the C-terminus of the COP1 protein. The COP1 Polyclonal Antibody has been extensively validated for its specificity and sensitivity in Western blotting, immunohistochemistry, and immunofluorescence assays.

The COP1 protein is a key regulator of various cellular processes, including cell cycle progression, DNA damage response, and apoptosis. Dysregulation of COP1 has been implicated in the development and progression of various diseases, including cancer. The COP1 Polyclonal Antibody is an essential tool for researchers studying the role of COP1 in these processes.

The COP1 Polyclonal Antibody is supplied as a purified IgG fraction, which has been affinity-purified using immobilized protein A. This antibody is provided in a liquid format, which is ready to use for various applications. The COP1 Polyclonal Antibody is highly specific and sensitive, with minimal cross-reactivity with other proteins.

In summary, the COP1 Polyclonal Antibody is a highly specific and sensitive antibody that is essential for researchers studying the role of COP1 in various cellular processes. This antibody is extensively validated and supplied in a purified IgG fraction, making it an ideal tool for various research applications.