Anti-TXNDC17 Antibody Picoband® (Dylight488 Conjugate)

Disulfide reductase. May participate in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions. Modulates TNF-alpha signaling and NF-kappa-B activation. Has peroxidase activity and may contribute to the elimination of cellular hydrogen peroxide.

ATP synthase F (0) complex subunit C1,2,3, mitochondrial; ATP synthase lipid-binding protein; ATP synthase membrane subunit c locus 1,2,3; ATP synthase proteolipid P1; ATP synthase proton-transporting mitochondrial F (0) complex subunit C1,2,3; ATPase protein 9; ATPase subunit c; ATP5MC1,2,3; ATP5G1,2,3

Highly expressed in thymus, uterus and testis. Detected at lower levels in brain, mammary gland, prostate, salivary gland and fetal spleen. In brain, highest expression in thalamus, hippocampus and amygdala. .

Mitochondrial membrane ATP synthase (F1F0 ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core and F0 - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F0 domain. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.

At -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freezing and thawing.