Anti-TWF2 Antibody Picoband® Fluoro488 Conjugated

Twinfilin-2 is a protein that in humans is encoded by the TWF2 gene. The protein encoded by this gene was identified by its interaction with the catalytic domain of protein kinase C-zeta. The encoded protein contains an actin-binding site and an ATP-binding site. It is most closely related to twinfilin (PTK9), a conserved actin monomer-binding protein.

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. Rohwer, A., Kittstein, W., Marks, F., Gschwendt, M. Cloning, expression and characterization of an A6-related protein. Europ. J. Biochem. 263: 518-525, 1999.