Technical Data
Insulin is a 51-amino acid polypeptide composed of A and B chains connected through the C-peptide. Proinsulin, which has very little biological activity, is cleaved by proteases within its cell of origin into the insulin molecule and the C-terminal basic residue. Insulin enhances membrane transport of glucose, amino acids, and certain ions. It also promotes glycogen storage, formation of triglycerides, and synthesis of proteins and nucleic acids. The main storage site for insulin is the pancreatic islets. Antibodies to insulin are important as â-cell of islets of Langerhans and tumor (insulinoma) marker.

Cellular Localization: Secreted

Positive Control: Pancreas

Suitable for use in ELISA, Western Blot, Immunohistochemistry (paraffin-embedded sections) and Immunocytochemistry. Other applications not tested.

Recommended Dilution:
Optimal dilutions to be determined by the researcher.

Storage and Stability:

May be stored at 4C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and store at -20C. Aliquots are stable for at least 12 months at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
500ul-20CBlue IcePorcineMouse
Not determined
Full length Swine Insulin protein.
Supplied as a liquid in PBS, pH 7.2.
The antibody recognizes the biologically most active forms of insulin on the C terminal end. It does not react with pro-insulin, C-peptide, thyroglobulin, albumin and insulin from rat, rabbit and/or guinea-pig (evaluated by simple-binding ELISA). The antibody labels the cytoplasm of beta cells in pancreatic islands and insulinomas (tested on formalin-fixed, paraffin-embedded tissue sections using the Streptavidin-biotinylated peroxidase method). Species Crossreactivity: Crossreacts with Human, bovine, Rabbit, Rat and Pig.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
i) Keilacker et al. Biomed Biochem Acta 45: 1093, 1986. ii) Madsen J. Diabetes 36: 1203, 1987.
iii) Witt et al. Acta Histochem suppl. XXXV, 217, 1988.