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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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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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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
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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
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 (including data from studies using tissues from transgenic mice) suggest that IL1B (show IL1B Antibodies) plays dual roles by (1) mediating islet amyloid-induced FAS (show FAS Antibodies) up-regulation and apoptosis in pancreatic beta-cells and (2) down-regulating IAPP precursor processing thereby potentiating islet amyloid formation. (IL1B (show IL1B Antibodies) = interleukin-1beta; FAS (show FAS Antibodies) = FAS (show FAS Antibodies) cell surface death receptor; IAPP = islet amyloid polypeptide)
Data suggest that single aromatic/hydrophobic amino acid residues within IAPP (islet amyloid polypeptide) amyloid core region are able to control its interaction with amyloid-beta(1-40) or amyloid-beta(1-42) but not IAPP self-assembly; four aromatic/hydrophobic residues are able to control both IAPP amyloid self-assembly and its cross-interaction with amyloid-beta(1-40) or amyloid-beta(1-42).
Data show that aluminum (Al3+) could inhibit islet amyloid polypeptide hIAPP(11-28) fibrillogenesis.
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.
studies have identified a novel TXNIP (show TXNIP Antibodies)/miR (show MLXIP Antibodies)-124a/FoxA2 (show FOXA2 Antibodies)/IAPP signaling cascade linking the critical beta-cell signaling pathways of TXNIP (show TXNIP Antibodies) and IAPP
MMP-9 (show MMP9 Antibodies) constitutes an endogenous islet protease that limits islet amyloid deposition and its toxic effects via degradation of hIAPP.
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