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Human Monoclonal IAPP Primary Antibody for ICC, IHC (fro) - ABIN153560
Nakamura, Okabayashi, Ageyama, Koie, Sankai, Ono, Fujimoto, Terao: Transthyretin amyloidosis and two other aging-related amyloidoses in an aged vervet monkey. in Veterinary pathology 2008
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Dog (Canine) Polyclonal IAPP Primary Antibody for WB - ABIN610646
Cifuentes-Diaz, Frugier, Tiziano, Lacène, Roblot, Joshi, Moreau, Melki: Deletion of murine SMN exon 7 directed to skeletal muscle leads to severe muscular dystrophy. in The Journal of cell biology 2001
Show all 2 Pubmed References
Human Monoclonal IAPP Primary Antibody for IHC (fro), IF - ABIN2477416
Deering, Shalloway: GelMetric: semi-automated electrophoretic mobility analysis. in Computer applications in the biosciences : CABIOS 1991
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Human Polyclonal IAPP Primary Antibody for WB - ABIN516766
Ladiwala, Bhattacharya, Perchiacca, Cao, Raleigh, Abedini, Schmidt, Varkey, Langen, Tessier: Rational design of potent domain antibody inhibitors of amyloid fibril assembly. in Proceedings of the National Academy of Sciences of the United States of America 2012
In this work, the decisive roles of peptide structures on amyloid self-assembly and morphological diversity were investigated by the design of eight amyloidogenic peptides derived from islet amyloid polypeptide.
The molecular dynamics simulations also demonstrate that the beta-sheet intermediates induce more perturbation on the membrane than the alpha-helical and disordered states and thus pose higher disruption ability.
these findings highlighted a novel role of sub-toxic concentrations of human amylin in promoting the secretion of proteic factors by endothelial cells (HspB5 and VEGF) that support the survival and proliferation of neuron-like cells.
Mass spectrometry has been applied to determine the deamidation sites and the aggregation region of the deamidated human islet amyloid polypeptide (hIAPP). Mutant hIAPP with iso-aspartic residue mutations at possible deamidation sites showed very different fibril formation behaviour, which correlates with the observed deamidation-induced acceleration of hIAPP aggregation.
this paper shows that human amylin induces CD4+Foxp3+ regulatory T cells and decrease in the incidence of diabetes in nod mice
In conclusion, IAPP/amylin directly interacts with NLRP3 to activate NLRP3 inflammasome, and this interaction could be an attractive drug target to avoid inflammation and beta-cell death during therapy for diabetes, although there are mechanisms in NLRP3 inflammasome and diabetes pathology in human tissues that still require elucidation.
These findings suggest that increased membrane permeation induced by oligomeratization of amylin peptide in cell sarcolemma contributes to Ca(2+) dysregulation in pre-diabetes.
down-regulation of IAPP expression induces the death of human annulus fibrosus cells via mitochondrial and death receptor pathways, potentially offering a novel therapeutic target for the treatment of intervertebral disc degeneration.
This study highlights that with positional scanning of the split-tetracysteine motif (Cys-Cys), the fluorogenic probe fluorescein arsenical hairpin detection method offers unique time-dependent conformational insights on the proteospecies assembled throughout the amyloidogenic pathway of IAPP.
Bri2 BRICHOS domain is a potent inhibitor of IAPP fibril formation.IAPP colocalizes with Bri2 both intracellularly and in islet amyloid deposits.
Insulin resistance in rheumatoid arthritis does not appear to be mediated by amylin. This would imply that the mechanisms associated with IR in RA patients differ from those at work in type 2 diabetes.
During aggregation, the nucleating NFGAIL region remains flexible and accessible within this isolated intermediate, suggesting a mechanism by which membrane-associated aggregation may be propagated.
Study presents a new Zn(2+) binding site in the N-terminus of fibrillary amylin with three different coordination modes. Simulations showed that Zn(2+) ions bind to polymorphic amylin fibrils with a preference to bind to four Cys residues rather than two Cys residues of two neighboring amylin monomers.
The IAPP beta-hairpin can serve as a molecular recognition motif enabling control of IAPP aggregation.
cholesterol significantly modulates the ability of model membranes to induce IAPP amyloid formation and IAPP-mediated membrane damage.
point mutations within the central aggregation-prone regions contribute to the reduction of the overall amyloidogenic potential of IAPP but do not completely abolish the formation of IAPP amyloid fibrils.
Using the Tg2576 AD mouse model, a single intraperitoneal injection of amylin significantly increased Abeta serum levels, and the effect was abolished by AC253, an amylin receptor antagonist, suggesting that amylin effect could be mediated by its receptor. Subsequent mechanistic studies showed amylin enhanced Abeta transport across a cell-based model of the blood-brain barrier.
These results suggest that protein segment structures represent polymorphs of their parent protein and that segment 19-29 S20G may serve as a model for the toxic spine of human IAPP.
All-atom explicit-water molecular dynamics (MD) simulations studying adsorption, orientation, and surface interaction of hIAPP aggregates with different sizes (monomer to tetramer) and conformations (monomer with alpha-helix and tetramer with beta-sheet-rich U-turn) upon adsorption. hIAPP monomer with alpha-helical conformation and hIAPP pentamer with beta-sheet conformation can adsorb on both POPC and POPC/POPE bilayers.
The aggregation of rhIAPP also occurred significantly faster when compared with that of the chemically synthesized peptide.
These data provide for the first time evidences for the toxic nature of oligomeric assemblies of murine amylin and its existence in wild-type, non-transgenic mice.
n T2 mice, the mRNA expression of Retn showed a moderate up-regulation (fold change=8.32; p=0.0019) in the adipose tissues. Iapp expression was also significantly up-regulated (fold change=9.78; p=0.012). Moreover, a 6.36-fold up-regulation for Drd5 was observed in the adipose tissues of T2 mice
Data suggest that hybrid insulin peptides (HIPs), formed in insulin-secreting-cells by fusion of insulin C-peptide fragments to peptide fragments of chromogranin A or islet amyloid polypeptide, and reactivity of CD4+-T-lymphocytes to HIPs may act as biomarkers of autoimmunity in type 1 diabetes.
Circulating aggregated amylin accumulates preferentially in male vs. female hearts and its effects on myocyte Ca(2+) cycling do not require diabetic remodeling of the myocardium.
Results suggest that amylin directly acts, through a p-ERK-mediated process, on POMC neurons to enhance arcuate nucleus-paraventricular nucleus alphaMSH pathway development.
These data suggest participation by both soluble and fibrillar aggregates in IAPP-induced islet inflammation. IAPP-induced activation of TLR2 and secretion of IL-1 may be important therapeutic targets to prevent amyloid-associated beta cell dysfunction.
Hypothalamic amylin is transcriptionally regulated by leptin, that it can act directly on ObRb neurons in concert with leptin, and that it regulates feeding.
Matrix Metalloproteinase-9 Protects Islets from Amyloid-induced Toxicity.
Data indicate that T-cell receptors that react to chromogranin A (ChgA) and islet amyloid polypeptide precursor (IAPP) autoantigens were impaired when the thymic stromal cells lacked thymus-specific serine protease (TSSP).
Study the physiologic actions of IAPP on pancreatic beta cells, which secrete this peptide together with insulin upon glucose stimulation. Explore the signaling pathways and mitogenic actions of IAPP on beta cells.
deletion of the DeltaN isoforms of p63 or p73 leads to metabolic reprogramming and regression of p53-deficient tumours through upregulation of IAPP, the gene that encodes amylin, a 37-amino-acid peptide co-secreted with insulin by the beta cells of the pancreas
The stability, conformational dynamics and association force of different single-layer models of the full-length wild-type and glycine mutants of amylin, were investigated.
studies have identified a novel TXNIP/miR-124a/FoxA2/IAPP signaling cascade linking the critical beta-cell signaling pathways of TXNIP and IAPP
MMP-9 constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP.
Data suggest that amylin and leptin play additive roles in regulating energy homeostasis via activation of overlapping signalling pathways; mechanisms may be different in hypothalamus, muscle, and liver and in cases of endoplasmic reticulum stress.
These findings point to a potential for Drosophila melanogaster to serve as a model system for studies of hproIAPP and hIAPP expression with subsequent aggregation and developed pathology.
MCP-1 induces amylin expression through ERK1/2/JNK-AP1 and NF-kappaB related signaling pathways independent of CCR2. Amylin upregulation by MCP-1 may contribute to elevation of plasma amylin in obesity and insulin resistance
This study demonstrated that amylin inactivation leads to a low bone mass due to an increase in bone resorption whereas bone formation is unaffected.
Fatty acids differently regulate amylin and insulin expression and induce both amylin and insulin release
Amylin/leptin's marked weight- and fat-reducing effects are due to activation of intrinsic synergistic neuronal signaling pathways.
Data indicated that a novel stable dimer was observed in pIAPP(20-29) solution, whereas hIAPP(20-29) exists mostly as monomers and trimers.
Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism.
Islet amyloid polypeptide (diabetes-associated peptide; amylin)
, diabetes-associated peptide
, insulinoma amyloid peptide
, islet amyloid polypeptide
, amyloid protein