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Amylin EIA Kit Maximize

Amylin EIA Kit

Human Amylin EIA Kit (EK-017-03) a method to detect quantitatively the concentrations of human amylin.

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96 wells

£ 430.00

Human Amylin EIA Kit

Specificity : Human
Sensitivity : 0.58ng/ml
Linear Range: 0.58-5.0ng/ml
Assay Range : 0-100ng/ml
Size: 96 tests.

Reagents Supplied:
- Primary antibody (rabbit anti-peptide IgG)(1 vial).
- 2N HCl (15ml).
- Standard peptide (1 vial).
- Streptavidin-horseradish peroxidase (SA-HRP)(30μl).
- Substrate solution (TMB) (12ml).
- 96 well immunoplate (1 plate).
- 20x assay buffer concentrate (50ml).
- Positive control (2 vials).
- Acetate plate sealer (APS), (3 pieces).
- Biotinylated peptide (1 vial).
- Assay diagram (1 sheet).
- General protocol (1 book).

Intended Use:
Human amylin EIA
is intended for quantitative analysis of amylin levels in any biological fluidserumplasmaurinetissue homogenate and  CSF.

Assay Principle:
1. Human Amylin EIA kit 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 TMB substrate solution and hydrogen peroxide to form a blue coloured solution.
4. Reaction is stopped by adding hydrogen chloride, which forms a yellow coloured solution.
5. Intensity of the yellow solution is inversely proportional to the amount of the peptide in standard solutions or samples.
6. Unknown concentration in samples can then be determined using this amylin EIA assay by extrapolation from a standard curve.

Cross Reactivity:
Amylin-Amide (Human) 100%.
Amylin (Human) 100%.
CGRP (Human) 1%.
CGRP (Rat) 0%.
Amylin (Rat, Feline) 0%.
Calcitonin 0%.
Insulin  0%.
NPY (Porcine) 0%.
VIP 0%.
Pancreatic Polypeptide 0%.
Glucagon  0%.
Pancreastatin (Porcine) 0%.
Pro-Insulin 0%.
Somatostatin-28 0%.

Amylin has a vital function along side the endocrine pancreas which contributes to glycemic control. As insulin lowers blood glucose and glucagon raises blood glucose, amylin supports the stability of blood glucose levels in effect by slowing the rate that digested glucose enters the bloodstream. It has many functions which include; slowing gastric emptying, promoting satiety, inhibiting the secretion of glucagon during hyperglycemia, thus leading to reduction of the total insulin demand. It is a 37-residue peptide hormone which is known to be secreted by pancreatic β-cells at the same time as insulin.

1. 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.
2. Respir Med. (2011) 105 (12): 1954-60. Plasma levels of neuropeptides and metabolic hormones, and sleepiness in obstructive sleep apnea. Sánchez de la torre M, et al. 
3. Diabetes. (1990) 39: 260–265. Induction of insulin resistance in vivo by amylin and calcitonin gene-related peptide. Molina J.M., et al.
4. Kidney Int. (2007) 72 (2): 213-8. Amylin deposition in the kidney of patients with diabetic nephropathy. Gong, et al.
5. Proc. Natl. Acad. Sci. USA. (1989) 86: 3127–3130. Rat amylin: cloning and tissue-specific expression in pancreatic islets. Leffert J.D., 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. 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.
8. 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.
9. Diabetologia. (1978) 15 :417–421. The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus. Westermark P. and Wilander E.

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