assay
≥90% (SDS-PAGE)
form
lyophilized powder
mol wt
75 kDa by SDS-PAGE (very hydrophilic protein), apparent mol wt ~48 kDa by amino acid sequence
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
cow ... CHGA(281070)
Biochem/physiol Actions
Chromogranin A, a high-capacity low-affinity Ca2+ binding protein, is a major protein in secretory vesicles. It is a precursor of biologically active peptides (Pancreasatin) and is involved in the sorting of secretory proteins and granules biogenesis. Chromogranin A interacts with membrane proteins, including the inositol 1,4,5-triphosphate receptor/Ca2+ channel.
Packaging
Package size based on protein content
Preparation Note
When reconstituted to 200 μl with distilled water, solution will contain 20 mM Tris, pH 7.4, 100 mm KCl, 0.1 mM DTT and 10% trehalose.
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The chromogranins A and B: the first 25 years and future perspectives.
H Winkler et al.
Neuroscience, 49(3), 497-528 (1992-08-01)
J Sigafoos et al.
Journal of anatomy, 183 ( Pt 2), 253-264 (1993-10-01)
The adrenal medulla chromaffin vesicle (CV) contains, on a weight basis, as much soluble protein and peptide as catecholamine. The bulk of the protein is accounted for by chromogranins (Cgr) A, B and C. Additionally, a large variety of neuropeptides
S H Yoo et al.
Biochemistry, 34(2), 632-638 (1995-01-17)
The secretory vesicles of adrenal chromaffin cells have previously been identified as a major inositol 1,4,5-trisphosphate (IP3)-sensitive Ca2+ store, and their Ca2+ store role has been attributed to the presence of chromogranin A, a high capacity, low affinity Ca2+ binding
W B Huttner et al.
Trends in biochemical sciences, 16(1), 27-30 (1991-01-01)
The chromogranins/secretogranins, referred to in abbreviated form as granins, are a family of acidic secretory proteins that are found in the secretory granules of a wide variety of endocrine cells and neurons, being stored together with many different peptide hormones
S H Yoo et al.
The Journal of biological chemistry, 265(24), 14414-14421 (1990-08-25)
Chromogranin A, the most abundant protein in bovine adrenal chromaffin granules, bound calmodulin in a Ca2(+)-dependent manner, and the calmodulin-binding property was utilized to purify chromogranin A. Chromogranin A has been described in the past as a "random-coil polypeptide" with
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