A portion of amino acids 35-64 from the human protein was used as the immunogen for this Insulin antibody.
After removal of the precursor signal peptide, proinsulin is post-translationally cleaved into three peptides: the B chain and A chain peptides, which are covalently linked via two disulfide bonds to form insulin, and C-peptide. Binding of insulin to the insulin receptor (INSR) stimulates glucose uptake. A multitude of mutant alleles with phenotypic effects have been identified. There is a read-through gene, INS-IGF2, which overlaps with this gene at the 5 region and with the IGF2 gene at the 3 region. Alternative splicing results in multiple transcript variants. [provided by RefSeq].
