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Human Monoclonal IAPP Primary Antibody pour 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. dans Veterinary pathology 2008
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Dog (Canine) Polyclonal IAPP Primary Antibody pour 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. dans The Journal of cell biology 2001
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Human Monoclonal IAPP Primary Antibody pour IHC (fro), IF - ABIN2477416
Deering, Shalloway: GelMetric: semi-automated electrophoretic mobility analysis. dans Computer applications in the biosciences : CABIOS 1991
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Human Polyclonal IAPP Primary Antibody pour WB - ABIN516766
Ladiwala, Bhattacharya, Perchiacca, Cao, Raleigh, Abedini, Schmidt, Varkey, Langen, Tessier: Rational design of potent domain antibody inhibitors of amyloid fibril assembly. dans 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 (Montrer DNAJC5 Anticorps)), 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 (Montrer ITM2B Anticorps) BRICHOS domain is a potent inhibitor of IAPP fibril formation.IAPP colocalizes with Bri2 (Montrer ITM2B Anticorps) both intracellularly and in islet amyloid deposits.
Insulin (Montrer INS Anticorps) 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 (Montrer DNAJC5 Anticorps) residues rather than two Cys (Montrer DNAJC5 Anticorps) 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 (Montrer APP Anticorps) 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 (Montrer APP Anticorps) 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 (Montrer HMBS Anticorps) bilayers.
Data suggest that hybrid insulin (Montrer INS Anticorps) peptides (HIPs), formed in insulin (Montrer INS Anticorps)-secreting-cells by fusion of insulin (Montrer INS Anticorps) C-peptide fragments to peptide fragments of chromogranin A (Montrer CHGA Anticorps) or islet amyloid polypeptide, and reactivity of CD4 (Montrer CD4 Anticorps)+-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 (Montrer CA2 Anticorps)+) cycling do not require diabetic remodeling of the myocardium.
Results suggest that amylin directly acts, through a p-ERK (Montrer EPHB2 Anticorps)-mediated process, on POMC (Montrer POMC Anticorps) neurons to enhance arcuate nucleus-paraventricular nucleus alphaMSH (Montrer POMC Anticorps) 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 (Montrer IL1A Anticorps) may be important therapeutic targets to prevent amyloid-associated beta cell dysfunction.
Hypothalamic amylin is transcriptionally regulated by leptin (Montrer LEP Anticorps), that it can act directly on ObRb (Montrer LEPR Anticorps) neurons in concert with leptin (Montrer LEP Anticorps), and that it regulates feeding.
Matrix Metalloproteinase-9 (Montrer MMP9 Anticorps) Protects Islets from Amyloid-induced Toxicity.
Data indicate that T-cell receptors that react to chromogranin A (ChgA (Montrer CHGA Anticorps)) and islet amyloid polypeptide precursor (IAPP) autoantigens were impaired when the thymic stromal cells lacked thymus-specific serine protease (TSSP (Montrer PRSS16 Anticorps)).
Study the physiologic actions of IAPP on pancreatic beta cells, which secrete this peptide together with insulin (Montrer INS Anticorps) upon glucose stimulation. Explore the signaling pathways and mitogenic actions of IAPP on beta cells.
deletion of the DeltaN isoforms of p63 (Montrer CKAP4 Anticorps) or p73 (Montrer ARHGAP24 Anticorps) leads to metabolic reprogramming and regression of p53 (Montrer TP53 Anticorps)-deficient tumours through upregulation of IAPP, the gene that encodes amylin, a 37-amino-acid peptide co-secreted with insulin (Montrer INS Anticorps) 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