Munc-18 interacting protein 1 (Mint1) is an adaptor protein primarily localized in the brain. It possesses phosphotyrosine-binding (PTB) domains and PDZ (PSD95, Dlg1 and zo-1) domains which are common to its family.
Spécificité
Detects rat munc-18 interacting protein 1 (mint1) using rat brain extract and extract from HEK293 cells overexpressing the rat gene.
Immunogène
synthetic peptide corresponding to amino acid residues 1-17 from rat mint1.
Actions biochimiques/physiologiques
Munc-18 interacting protein 1 (Mint1) binds to amyloid-β precursor protein (APP) and also associates with calcium/calmodulin-dependent serine protein kinase (CASK).
Forme physique
Solution in phosphate buffered saline containing 1.0 mg/mL bovine serum albumin and 0.05% sodium azide.
Vous ne trouvez pas le bon produit ?
Essayez notre Outil de sélection de produits.
Code de la classe de stockage
10 - Combustible liquids
Faites votre choix parmi les versions les plus récentes :
The Journal of biological chemistry, 275(51), 39803-39806 (2000-10-19)
Mint1 (X11/human Lin-10) and Mint2 are neuronal adaptor proteins that bind to Munc18-1 (n/rb-sec1), a protein essential for synaptic vesicle exocytosis. Mint1 has previously been characterized in a complex with CASK, another adaptor protein that in turn interacts with neurexins.
Biochemical and biophysical research communications, 320(3), 717-721 (2004-07-09)
Munc-18-interacting (Mint) proteins are adaptors involved in regulation of synaptic vesicle exocytosis. We have investigated expression and cellular localization of Mint1 in pancreatic islets with special reference to insulin-secreting beta-cells. Western blotting showed that Mint1 was expressed in hamster (HIT-T15)
The Journal of neuroscience : the official journal of the Society for Neuroscience, 22(17), 7340-7351 (2002-08-28)
Mints/X11s are neuron-specific (Mints 1 and 2) and ubiquitous (Mint 3) adaptor proteins composed of isoform-specific N-terminal sequences and common C-terminal phosphotyrosine-binding (PTB) and PDZ domains. We now show that all three Mints bind to the cytoplasmic tail of amyloid-beta
Questions
Reviews
★★★★★ No rating value
Active Filters
Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..