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Amylin (1-13) Fluorescent EIA Kit Maximize

Amylin (1-13) Fluorescent EIA Kit

Human Amylin (1-13) Fluorescent EIA Kit (FEK-017-06) is a quantitative method to detect  levels of human amylin (1-13).

More details

FEK-017-06

96 wells

£ 480.00

Human Amylin (1-13) Fluorescent EIA

Specificity : Human
Sensitivity : 36.8 pg/ml
Linear Range: 36.8-1050 pg/ml
Range: 0-10000 pg/ml
Size: 96 tests

Reagents Supplied:
- 96 well immunoplate (1 plate)
- 20x assay buffer concentrate (50ml)
- Standard peptide (1 vial).
- Primary antibody (rabbit anti-peptide IgG) (1 vial).
- Positive control (1 vial).
- Acetate plate sealer (APS), (3 pieces)
- Streptavidin-horseradish peroxidase (SA-HRP) (30μl)
- Substrate solution (12ml)
- Biotinylated peptide (1 vial).
- Stable peroxide solution (1.5ml)
- Stop solution (12ml)
- General protocol (1 book).
- Assay diagram (1 sheet).

Intended Use:
Human Amylin Fluorescent EIA kit is intended to determine levels of human amylin (1-13) amide using serum, any biological fluid samples, plasma, urine or CSF samples.

Assay Principle:
1. Human amylin fluorescent EIA has been pre-coated with secondary antibody and also the non-specific binding sites have been blocked.
2. Secondary antibody is able to bind with the Fc fragment of the primary antibody, the Fab segment is competitively bound by both biotinylated peptides and the peptide standard or the targeted peptide in samples.
3. Biotinylated peptide can then interact with the SA-HRP, which then catalyzes the substrate solution.
4. Fluorescence intensity is directly proportional to the amount of biotinylated peptide-SA-HRP complex but inversely proportional to the amount of the peptide in standard solutions or samples.
5. Unknown concentration in samples can then be determined by using this human amylin fluorescent EIA kit to extrapolation from a standard curve.

Cross Reactivity:
Amylin (1-13) (Human) 100%.
Amylin (Rat, Mouse) 3.5%.
Amylin free acid (Human) 17.9%.
Amylin-Amide (Human) 2.5%.
VIP (Mouse, Human, Porcine) 0%.
Calcitonin (Human) 0%.
Pancreastatin (Porcine) 0%.
Insulin (Human) 0%.
Pancreastatin (Porcine) 0%.
Pancreatic Polypeptide (Human) 0%
Pro-Insulin (Human) 0%.
CGRP(Human, Rat) 0%.
NPY (Porcine) 0%.
Somatostatin-28 0%.
Glucagon 0%.
Pro-Insulin 0%.

Background:
Amylin is a 37-residue peptide hormone which is known to be secreted by pancreatic β-cells at the same time as insulin and has a  vital function along side the endocrine pancreas which contributes to glycemic control. It also has a number of functions which include; promoting satiety, slowing gastric emptying, inhibiting the secretion of glucagon during hyperglycemia, thus leading to reduction of the total insulin demand.

References
1. Diabetes. (1990) 39: 260–265. Induction of insulin resistance in vivo by amylin and calcitonin gene-related peptide. Molina J.M., et al.
2. Diabetologia. (1978) 15 :417–421. The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus. Westermark P. and Wilander E.
3. Proc. Natl. Acad. Sci. USA. (1989) 86: 3127–3130. Rat amylin: cloning and tissue-specific expression in pancreatic islets. Leffert J.D., et al.
4. Proc. Natl. Acad. Sci. U.S.A.. (1987) 84: 3881–3885. Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Westermark, P., et al.
5. J. Biol. Chem. (1988) 263: 17243–17246. An islet amyloid peptide is derived from an 89-amino acid precursor by proteolytic processing. Sanke T., et al.
6. Nature. (1988) 335: 632–635. Pancreatic amylin and calcitonin gene-related peptide cause resistance to insulin in skeletal muscle in vitro. Leighton B. and Cooper G.J.S.
7. Diabetes. (1991) 40: 1005–1009. Release of amylin from perfused rat pancreas in response to glucose, arginine, β-hydroxybutyrate, and gliclazide. Inoue K., et al.

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