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SAB4200494

Sigma-Aldrich

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

enhanced validation

~1.0 mg/mL, affinity isolated antibody

Synonym(s):

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

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human

enhanced validation

independent ( Antibodies)
Learn more about Antibody Enhanced Validation

concentration

~1.0 mg/mL

technique(s)

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... IAPP(3375)

General description

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.

Specificity

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.

Application

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

Biochem/physiol Actions

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.

Physical form

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

Storage and Stability

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.

Disclaimer

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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Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Robert Y L Zee et al.
Clinica chimica acta; international journal of clinical chemistry, 412(9-10), 785-787 (2011-01-12)
Islet amyloid polypeptide (IAPP) gene variation has recently been implicated in type 2 diabetes mellitus (T2D). However, to date, no prospective epidemiological data are available. The association between 10 IAPP tag-single nucleotide polymorphisms (tSNPs) and incident T2D was investigated in
Amylin-mediated control of glycemia, energy balance, and cognition
Mietlicki-Baase EG, et al.
Physiology & Behavior, 162, 130-130 (2016)
Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology
Akter R et al.
Journal of Diabetes Research (2016)
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)
Amylin Uncovered: A Review on the Polypeptide Responsible for Type II Diabetes
Pillay K, et al.
BioMed Research International (2013)

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