Anti-Secretogranin II (SCG2)

SCG2 is a member of the chromogranin/secretogranin family of neuroendocrine secretory proteins. Studies in rodents suggest that the full-length protein, secretogranin II, is involved in the packaging or sorting of peptide hormones and neuropeptides into secretory vesicles. The full-length protein is cleaved to produce the active peptide secretoneurin, which exerts chemotaxic effects on specific cell types, and EM66, whose function is unknown.SCG2 also has 9 potential dibasic cleavage sites, an N-glycosylation site not found in the bovine protein, and a putative sulfation site (tyr121). SCG2 was predicted to assume a secondary structure of alternating helix and turn structures over 45% and 40% of its length, respectively. The authors suggested that this structure may coordinate calcium.

Western blotting: 1:100-400, Immunocytochemistry in formalin fixed cells: 1:100-500, Immunohistochemistry in formalin fixed frozen section: 1:100-500, Immunohistochemistry in paraffin section: 1:50-417

SN, SgII, CHGC, Chromogranin C, Secretoneurin

Mouse