Insulin is produced in a step-wise process. Preproinsulin is a biologically inactive precursor that consists of an N-terminal signal peptide followed by the proinsulin molecule. Removal of the signal peptide by signal peptidases results in proinsulin alone. Proinsulin contains the A-chain, B-chain, and a 31-amino-acid Connecting peptide or C-peptide. The C-peptide is positioned between the A-chain and the B-chain and functions to connect them. The C-peptide is removed once proinsulin is processed into insulin.
Antibodies for Insulin Detection
Human insulin monoclonal antibody may be used for the analysis of the structure, function, and metabolism of insulin. This anti-insulin antibody, also known as INS antibody, is applicable for Western blot (WB) analysis under non-reducing and non-heating conditions and for immunohistological (IHC) studies of frozen tissue sections.
Antibodies to the proinsulin C-peptide (also known as insulin C) are frequently used to study the structure, function, and metabolism of insulin as well as proinsulin. Insulin C antibodies can also be used for immunocytochemistry (ICC) and for immunohistochemical (IHC) studies of paraffin-embedded or frozen tissue sections. The following insulin C antibodies are available:
Human insulin C monoclonal antibody is generated in mouse immunized with the KLH-conjugated human insulin C-peptide (71–86) [GPGAGSLQPLALEGSL].
Mouse insulin C monoclonal antibody is generated in rat immunized with the KLH-conjugated mouse insulin C-peptide (71–84) [SPGDLQTLALEVAR].
Mouse insulin C polyclonal antibody is generated in guinea pig immunized with the KLH-conjugated mouse insulin C-peptide (71–84) [SPGDLQTLALEVAR].