Synapsin I (C-terminal region) Antibody

Synapsins are important peripheral membrane proteins involved in synaptic vesicle release during neurotransmission between neurons. Several synapsin variants are generated by alternative splicing of the mRNA from three different genes: synapsin I, II, and III. Synapsins bind to synaptic vesicles via their conserved N-terminal domains. Regulation of synapsins may occur through PKA and CAM kinase I phosphorylation. This regulation occurs concomitantly with membrane excitation and neurotransmitter release into the synaptic cleft. Synapsins bundle actin filaments and interact with multiple calcium binding proteins. Thus, synapsins may crosslink vesicles or other proteins to actin filaments at the presynaptic terminal. In addition, synapsins may interact with each other, since synapsin III has been shown to form heteromultimers with both synapsin I and synapsin II. All synapsins contain a central ATP binding domain and variable C-terminal domains that facilitate distinct regulatory functions.

Clone M365 was generated from a sequence corresponding to amino acids in the C-terminal region of mouse synapsin I. This sequence has high homology to human and rat synpasin I.