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Merck

SAB4200494

Sigma-Aldrich

Anti-IAPP (N-terminal) antibody produced in rabbit

enhanced validation

~1.0 mg/mL, affinity isolated antibody

Synonym(e):

Anti-Amylin, Anti-DAP, Anti-Diabetes-associated peptide, Anti-IAP, Anti-Islet amyloid polypeptide

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About This Item

UNSPSC-Code:
51111800
NACRES:
NA.41

Biologische Quelle

rabbit

Konjugat

unconjugated

Antikörperform

affinity isolated antibody

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Speziesreaktivität

human

Erweiterte Validierung

independent ( Antibodies)
Learn more about Antibody Enhanced Validation

Konzentration

~1.0 mg/mL

Methode(n)

western blot: 5-10 μg/mL using formalin-fixed paraffin-embedded human pancreas.

UniProt-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

human ... IAPP(3375)

Allgemeine Beschreibung

Islet amyloid polypeptide (IAPP), also known as amylin, is a 37 amino acid peptide hormone co-secreted with insulin from the pancreatic Β-cells. IAPP is processed from an 89-amino acid precursor pro-islet amyloid polypeptide (proIAPP) in pancreatic Β-cells that undergoes complex posttranslational modifications including protease cleavage, C-terminal amidation and formation of an intramolecular disulfide bridge to produce the mature IAPP.
The IAPP gene is mapped on the human chromosome at 12p12.1.

Spezifität

Anti-IAPP(N-terminal) specifically recognizes human IAPP.

Immunogen

synthetic peptide corresponding to a sequence at the N-terminus of human pro-IAPP (GeneID 3375), conjugated to KLH.

Anwendung

Anti-IAPP (N-terminal) antibody produced in rabbit may be used in immunohistochemistry.

Biochem./physiol. Wirkung

Islet amyloid polypeptide (IAPP)/Amylin plays a role in glycemic regulation by slowing gastric emptying and promoting satiety, thereby preventing post-prandial spikes in blood glucose levels. The human IAPP (20-29) region that has been found to be essential to amyloid formation is thought to be a key factor in the initiation of amyloid aggregation. Amyloid deposits deriving from IAPP are commonly found in pancreatic islets of patients suffering of T2DM, or containing an insulinoma cancer. IAPP, like β-amyloid peptide associated with Alzheimer′s disease, can induce apoptosis in insulin producing β-cells, an effect that is relevant to the development of type 2 diabetes.

Physikalische Form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Lagerung und Haltbarkeit

For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing, or storage in “frost-free” freezers,is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.

Haftungsausschluss

Unless otherwise stated in our catalog, our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Lagerklassenschlüssel

10 - Combustible liquids

WGK

WGK 2

Flammpunkt (°F)

Not applicable

Flammpunkt (°C)

Not applicable


Analysenzertifikate (COA)

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In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.

Die Dokumentenbibliothek aufrufen

Causative factors for formation of toxic islet amyloid polypeptide oligomer in type 2 diabetes mellitus
Jeong HR, et al.
Clinical Interventions in Aging, 10, 1873-1873 (2015)
Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology
Akter R et al.
Journal of Diabetes Research (2016)
Amylin-mediated control of glycemia, energy balance, and cognition
Mietlicki-Baase EG, et al.
Physiology & Behavior, 162, 130-130 (2016)
Amylin Uncovered: A Review on the Polypeptide Responsible for Type II Diabetes
Pillay K, et al.
BioMed Research International (2013)

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