rev:  December 23, 2003

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  ANTIBODIES  

                                                       (anti-Human and others as indicated)
RDI Divison of researchd Industries Intl  offers a wide line of  antibodies. Since no one antibody works best for all applications (neutralization, blotting, ELISA, etc), we offer many different types of antibodies to help solve this problem. Please inquire for other applications or types of antibodies not listed below.

Anti-Amylin Peptide

cat# RDI-AMYLINPabm   $500.00/vial

Specificity:* recognizes Human Islet amyloid peptide

Presentation: 1 ml lyophilized supernatant with 15mM sodium azide added.

Clone: R10/99

Isotype: mIgG1k

Antigen: synthetic peptide sequence (CATQRLANFLV) coupled to tuberculin

Hybridoma: mouse myeloma (SP2/0)

USES: -frozen section (not evaluated)

            -Paraffin sections

            -typical dilutions:1:50-1:100, 60 minute incubation at 25 DEG C. ABC detection

              -western blot:not evaluated

Stain: cytoplasmic

Pos Controls: pancreas

Reconstitution: 1 ml distilled water. Let set at least 30 minutes. Tighten cap and mix gently.

Storage: Store lyophilized material at 4 DEG C. Store reconstituted material at 4 DEG C for immediate use. For long term use, recommend aliquoting and store at -20 DEG C. Avoid frequent freeze thaw cycles.

Background:Amylin is a pancreatic islet peptide with a role in the maintenance of glucose homostasis. It is predominantly found in the beta cells of the pancreas and to a lesser extent in the gastrointestinal tract and nervous system. Amylin appears to work with insulin to regulate plasma/glucose concentrations in the bloodstream, suppressing secretion of glucagon after eating and restraining the rate of gastric emptying. Patients with diabetes mellitus have a deficiency in the secretion of glucagon that parallels the deficiency of insulin secretion. Amylin, when administered to diabetics, restore, in a dose dependent way, those functions previously suppressed. Two fragments of amylin have ben identified in vivo. One fragment contains residues 17 to 37 of human amylin and the other contains residues 24 to 37. Amylin (24-37) peptide fragment forms amyloid deposits, however, smaller fragments eg residues 20 to 29, are also capable of generating amyloid. A soluble factor from pancreatic carcinoma cells selectively stimulates amylin secretion from islet cells, explaining the detection of excessive quantities of amylin found in cases of pancreatic cancer. As this increase in amylin concentration is an early feature of pancreatic cancer. This antibody may prove of value in studies to determine the level of staining for amylin in normal and diabetic pancreas and pancreatic carcinomas.

References:

-Kruger D F et al, Clinical implications of amylin and amylin deficiency. Diabetes Educ 25(3):389-397 (1999)

-Nilsson MR et al, Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin. J Mol Biol 294(5):1375-1385 (1999)

-Ding X et al, Pancreatic cancer cells selectively stimulate islet beat cells to secrete amylin.. Gastroenterology 114(1):130- 138 91998)

-Guldobono, F. Amylin and Gastrointestinal activity. Gen Pharmacol 31(2):173-177 (1998)

FOR IN VITRO RESEARCH USE ONLY-NOT FOR USE IN DIAGNOSTICSFOR IN VITRO RESEARCH USE ONLY-NOT FOR USE IN DIAGNOSTICS

RDI Divison of researchd Industries Intl

San Jose, 95123 CA Snell ave 658

USA

or 408-780-0908

EMAIL:margaret@cellular-research.com

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