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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
Show all 6 Pubmed References
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
Show all 3 Pubmed References
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
This study highlights that with positional scanning of the split-tetracysteine motif (Cys-Cys (show DNAJC5 Antibodies)), 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 (show ITM2B Antibodies) BRICHOS domain is a potent inhibitor of IAPP fibril formation.IAPP colocalizes with Bri2 (show ITM2B Antibodies) both intracellularly and in islet amyloid deposits.
Insulin (show INS Antibodies) 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.
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 (show DNAJC5 Antibodies) residues rather than two Cys (show DNAJC5 Antibodies) 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 (show APP Antibodies) 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 (show APP Antibodies) 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 (show HMBS Antibodies) bilayers.
Data suggest that hybrid insulin (show INS Antibodies) peptides (HIPs), formed in insulin (show INS Antibodies)-secreting-cells by fusion of insulin (show INS Antibodies) C-peptide fragments to peptide fragments of chromogranin A (show CHGA Antibodies) or islet amyloid polypeptide, and reactivity of CD4 (show CD4 Antibodies)+-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 (show CA2 Antibodies)+) cycling do not require diabetic remodeling of the myocardium.
Results suggest that amylin directly acts, through a p-ERK (show EPHB2 Antibodies)-mediated process, on POMC (show POMC Antibodies) neurons to enhance arcuate nucleus-paraventricular nucleus alphaMSH (show POMC Antibodies) 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 (show IL1A Antibodies) may be important therapeutic targets to prevent amyloid-associated beta cell dysfunction.
Hypothalamic amylin is transcriptionally regulated by leptin (show LEP Antibodies), that it can act directly on ObRb (show LEPR Antibodies) neurons in concert with leptin (show LEP Antibodies), and that it regulates feeding.
Matrix Metalloproteinase-9 (show MMP9 Antibodies) Protects Islets from Amyloid-induced Toxicity.
Data indicate that T-cell receptors that react to chromogranin A (ChgA (show CHGA Antibodies)) and islet amyloid polypeptide precursor (IAPP) autoantigens were impaired when the thymic stromal cells lacked thymus-specific serine protease (TSSP (show PRSS16 Antibodies)).
Study the physiologic actions of IAPP on pancreatic beta cells, which secrete this peptide together with insulin (show INS Antibodies) upon glucose stimulation. Explore the signaling pathways and mitogenic actions of IAPP on beta cells.
deletion of the DeltaN isoforms of p63 (show CKAP4 Antibodies) or p73 (show ARHGAP24 Antibodies) leads to metabolic reprogramming and regression of p53 (show TP53 Antibodies)-deficient tumours through upregulation of IAPP, the gene that encodes amylin, a 37-amino-acid peptide co-secreted with insulin (show INS Antibodies) 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.
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