CSP Polyklonale Antilichaam, PE-Cy5,5 Vervoeging

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.

CLN 4; CLN4; CLN4B; CSP; cysteine string protein alpha; Cysteine string protein; DJC5; DnaJ Hsp40 homolog subfamily C member 5; DnaJ homolog subfamily C member 5; DNAJC 5; Dnajc5; DNAJC5A; DNJC5_HUMAN; NCL.

80331

Cell membrane

Human, Rat

1-100/198

CSP

PE-Cy5.5

KLH conjugated synthetic peptide derived from human CSP

WB

Purified by Protein A.

488nm/694nm

1µg/µl

WB (1:300-5000)

Aqueous buffered solution containing 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Unmodified

Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.

80331

Mouse, Cow, Sheep, Pig, Horse, Rabbit, GuineaPig