Mouse GIP (Total) ELISA - Cosmo Bio Co.,Ltd.

Antibodies

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Mouse GIP (Total) ELISA

Catalog No.: YII-YK255-EX
Size: 1KIT
Price: ¥79000
$1054
@
Purpose: This ELISA kit is used for quantitative determination of mouse total GIP in plasma and culture mediumsupernatant. The kit is characterized by its sensitive quantification and high specificity. In addition, ithas no influence by other components in samples. GIP standard is highly purified synthetic product.
< Specificity >
This ELISA kit has high specificity to mouse GIP(1-42) and GIP(3-42), and shows no cross reactivity toGlucagon, GLP-1(7-37), GLP-1(7-36) NH2, GLP-1(9-36) NH2 and mouse GLP-2.
component: 1) Antibody coated plate
2) Standard
3) HRP labeled antibody solution
4) Enzyme substrate solution (TMB)
5) Stopping solution
6) Buffer solution
7) Washing solution (concentrated)
8) Adhesive foil

Other:

 Background 
The incretin hormones, glucose-dependent insulinotropic polypeptide (GIP) and glucagons-like
peptide-1 (GLP-1), are a group of gastrointestinal hormones that cause an increase in the amount of
insulin released from the beta cellsof the islets of Langerhans after ingestion of food.
The intestinal peptide GIP was first isolated from porcine upper small intestine1). The sequences of
porcine2) 3), bovine4) and human GIP5) have been determined, each has 42 amino acids, and thesequences
is highly conserved. The porcine and bovine peptides differ from the human at two and three site,
respectively. Takeda et al. have isolated a human cDNA encoding the GIP precursor and confirming that
GIP belongs to the vasoactive intestinal peptide (VIP)/Glucagon/secretin family6). GIP is a
gastrointestinal peptide hormone that is released from duodenal endocrine K cells after absorption of
glucose or fat7). GIP is a potent releaser of insulin in experimental animals8) and in man9,10) provided
that the blood glucose is above basal level. Plasma level of GIP is elevated after an oral glucose load or a
meal in normal man. This increase after a meal is below normal in newly diagnosed insulin?dependent
diabetics11). It is nowbeing recognized that GIP receptor is also expressed in organs and cells such as
duodenum, small intestine, pancreatic alpha-cell, adipocyte and osteoblast. These results demonstrate
GIP may have a lot of physiological effect in addition to theirglucoregulatory effects12,13,14,15).
GIP is rapidly inactivated by the enzyme dipeptidyl peptidase- 4 (DPP- 4) to GIP (3-42) with a blood
half-life of only several minutes. DPP- 4 inhibitor can prolong the half-life of GIP, that expecting
treatment of incretin effect.
The kit can be used for measurement of total GIP [both GIP (1-42) and GIP (3-42)] in mouse plasma
with high sensitivity. It will be a specifically useful tool for incretin research.
 Principle 
This ELISA kit for determination of mouse total GIP is based on a sandwich enzyme immunoassay. To
the wells of plate coated with highly purified mouse monoclonal antibody against mouse GIP, standards
or samples are added for the 1st step immunoreaction. After the 1st step incubation and plate washing,
HRP labeled antibody solution against mouse GIP is added as the 2nd step to form antibody - antigen -
labeled antibody complex on the surface of the wells. After the 2nd step incubation and rinsing out
excess labeled antibody, Finally, HRP enzyme activity is determined by 3,3f,5,5f-Tetramethylbenzidine
(TMB) and the concentration of mouse total GIP is calculated.



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Performance Characteristics

Reference:

1. Brown,J.C., et. al., (1970) J.Physiol. 209, 57-64
2. Jornvall H, et. al., (1981) FEBS Lett. 123, 205-210.
3. Moody,A.J., et. al., (1981)Diabetologia 21, 306, abstr.
4. Carlquist M, et. al., (1984) Eur.J. Biochem. 145, 573-577
5. Moody, A. J., et. al., (1984)FEBS Lett. 172, 142-148
6. Takeda J, et. al., (1987)Proc Natl Acad Sci U S A. 84(20):7005-8.
7. Pederson, R.A. (1994) in Gut Peptides: Biochemistry and Physiology, eds, Walsh, J.H.& Dockray, G.J. (Raven, New York), pp,217-260
8. Rabinovitch, et. al., (1974)Endocrinology 94,1139-1144
9. Dupre,J., et. al., (1973)J. Clin. Endocrinol. Metab. 37, 826-828
10. Elahi, D., et. al., (1979) Am.J.Physiol. 237, E185-E191
11. Krarup T, et. al., (1983)J Clin Endocrinol Metab. 56, 1306-12.
12. Naitoh R, et. al., (2008) Biochem Biophys Res Commun. 376, 21-5.
13. Miyawaki K, et. al., (1999) Proc Natl Acad Sci U S A. 96, 14843-7.
14. Miyawaki K, et. al., (2002) et. al., Nat Med. 8, 738-42.
 
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