Anti-TXNDC17 Antibody Picoband® Fluoro488 Conjugated

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. .

Amino Acid Metabolism, Amino Acids, Cancer, Channels, Metabolic Signaling Pathways, Metabolism, Pathways and Processes, Plasma Membrane, Signal Transduction

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.

1. Hong, S., Huh, J.-E., Lee, S. Y., Shim, J.-K., Rhee, S. G., Jeong, W. TRP14 inhibits osteoclast differentiation via its catalytic activity. Molec. Cell. Biol. 34: 3515-3524, 2014. 2. Jeong, W., Chang, T.-S., Boja, E. S., Fales, H. M., Rhee, S. G. Roles of TRP14, a thioredoxin-related protein in tumor necrosis factor-alpha signaling pathways. J. Biol. Chem. 279: 3151-3159, 2004. 3. Jeong, W., Yoon, H. W., Lee, S.-R., Rhee, S. G. Identification and characterization of TRP14, a thioredoxin-related protein of 14 kDa: new insights into the specificity of the thioredoxin function. J. Biol. Chem. 279: 3142-3150, 2004.