Rabbit anti-Human DNM2 Polyclonal Antibody

Uniprot Id

P50570

Target Species

Human

Target Name

DNM2

Target Full Name

Dynamin-2

Target Function

Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones. Plays an important role in vesicular trafficking processes, in particular endocytosis. Involved in cytokinesis. Regulates maturation of apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the phagosome membrane.

Target Involvement

Myopathy, centronuclear, 1 (CNM1); Lethal congenital contracture syndrome 5 (LCCS5); Charcot-Marie-Tooth disease, dominant, intermediate type, B (CMTDIB); Charcot-Marie-Tooth disease 2M (CMT2M)

Target Subcellular Location

Cytoplasm. Cytoplasm, cytoskeleton. Cell junction. Membrane, clathrin-coated pit. Cell junction, synapse, postsynaptic density. Cell junction, synapse. Midbody. Cell projection, phagocytic cup. Cytoplasmic vesicle, phagosome membrane; Peripheral membrane protein.

Target Protein Families

TRAFAC class dynamin-like GTPase superfamily, Dynamin/Fzo/YdjA family

Target Tissue Specificity

Ubiquitously expressed.

Target Synonyms

CMT2M; CMTDI1; CMTDIB; DI CMTB; Dnm2; DYN II; DYN2; DYN2_HUMAN; Dynamin II; Dynamin-2; Dynamin2; DynaminII; DYNII

Target Background

Dynamins represent one of the subfamilies of GTP-binding proteins. These proteins share considerable sequence similarity over the N-terminal portion of the molecule, which contains the GTPase domain. Dynamins are associated with microtubules. They have been implicated in cell processes such as endocytosis and cell motility, and in alterations of the membrane that accompany certain activities such as bone resorption by osteoclasts. Dynamins bind many proteins that bind actin and other cytoskeletal proteins. Dynamins can also self-assemble, a process that stimulates GTPase activity. Five alternatively spliced transcripts encoding different proteins have been described. Additional alternatively spliced transcripts may exist, but their full-length nature has not been determined.