The Mercodia Porcine Insulin ELISA is a species-optimized, high quality enzyme immunoassay for the quantification of porcine insulin in serum or plasma.
For information about available Control sets please contact us
Read the Directions for Use
Available Control sets:
Mercodia Insulin Control Animal Low, Medium & High 10-1221-01
Mercodia Porcine Insulin ELISA provides a method for the quantitative determination of insulin in porcine serum and plasma.
Format: 1 x 96 wells
Specificity: Porcine C-peptide:<0.001% Porcine proinsulin: <0.2 %
Samples: Serum, plasma
Sample volume: 25 μL
Assay range: 0.02 - 1.5 μg/L
Detection limit: ≤ 0.01 μg/L
Incubation (min): 120+15
The detection limit is ≤ 0.01 μg/L as determined with the
methodology described in ISO11843-Part 4.
Recovery upon addition is 100 - 111 % (105 %).
Recovery upon dilution is 90 - 112 % (97 %).
Each sample was analyzed in 4 replicates on 13 different
|Sample||Mean Value||Coefficient of variation|
|(μg/L)||within assay %||between assay %||total assay %|
Serum or plasma, sample volume: 25μL.
Grossly lipemic, icteric or haemolyzed samples do not interfere
in the assay.
Mercodia Porcine Insulin ELISA is a solid phase two-site enzyme
immunoassay based on the sandwich technique, in which two
monoclonal antibodies are directed against separate antigenic
determinants on the insulin molecule. Insulin in the sample
reacts with anti-insulin antibodies bound to microtitration
wells and peroxidase-conjugated anti-insulin antibodies in the
Summary of protocol
The following cross-reactions have been tested:
|Porcine C-peptide||< 0.001 %|
|Porcine proinsulin||< 0.2 %|
|Human insulin||22 %|
|Human C-peptide||< 0.01 %|
|Human proinsulin||< 0.1 %|
n.d.= not detected
Kemter, E., Cohrs, C.M., Schäfer, M. et al. Diabetologia (2017) 60: 1152. https://doi.org/10.1007/s00125-017-4250-2
Lindqvist, A, Spegel, P, Ekelund, M (2014)
Gastric bypass improves ss-cell function and increases beta-cell mass in a porcine model
Kelly, A, C, Steyn, L (2014)
Function and expression of sulfonylurea, adrenergic, and glucagon-like peptide 1 receptors in isolated porcine islets
SoRelle, J, A, Kanak, M (2014)
Comparison of surface modification chemistries in mouse, porcine, and human islets