CSPS/MPST Polyclonal Antibody, AbBy Fluor™ 647 Conjugated

Cysteine string proteins (CSPs) are synaptic vesicle-associated, secretory vesicle proteins that are involved in Ca2+-regulated exocytosis of synaptic vesicles and modulation of presynaptic transmembrane calcium fluxes in neuroendocrine and endocrine cell types. CSP contains a J-domain that binds HSP 70/HSC 70 chaperone ATPases and a membrane-targeting, palmitoylated cysteine-rich string region. CSPs may act as molecular chaperones in synapses, and mediate conformational folding of components of the vesicular exocytotic machinery. CSP is involved in the fine tuning of neurotransmission through its interaction with receptor-coupled trimeric GTP binding proteins (G proteins) and N-type Ca2+ channels. Two variants of CSP have been described: CSP1; and the 31 amino acid, C-terminally truncated isoform, CSP2. Subcellular fractionation of insulinoma cells shows CSP1 in granular fractions, while the membrane and cytosol fractions contain predominantly CSP2. The fractions also contain additional proteins, presumably CSP dimers. Furthermore, in various mammalian cell lines (including rat brain) CSP1 expression predominates CSP2 expression.

Aryl sulfotransferase 1A3/1A4; Aryl sulfotransferase; Catecholamine Sulfating Phenol Sulfotransferase; Catecholamine-sulfating phenol sulfotransferase; Dopamine specic sulfotransferase; FLJ54864; HAST; HAST3; M PST; M-PST; Monoamine preferring sulfotransferase; Monoamine sulfating phenosulfotransferase; monoamine-preferring; Monoamine-sulfating phenol sulfotransferase; MPST; Phenol sulfotransferase 1A5; Placental estrogen sulfotransferase; ST1A3/ST1A4; ST1A3_HUMAN; ST1A5; STM; Sulfokinase; Sulfotransferase 1A3/1A4; Sulfotransferase; Sulfotransferase family cytosolic 1A phenol preferring member 3; Sulfotransferase family cytosolic 1A phenol preferring member 4; Sulfotransferase monoamine preferring; SULT1A 3; SULT1A4; Thermolabile monoamine M form phenol sulfotransferase; Thermolabile phenol sulfotransferase; TL PST; TL-PST; TLPST.