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.
Spezifität
Detects rat munc-18 interacting protein 1 (mint1) using rat brain extract and extract from HEK293 cells overexpressing the rat gene.
Immunogen
synthetic peptide corresponding to amino acid residues 1-17 from rat mint1.
Biochem./physiol. Wirkung
Munc-18 interacting protein 1 (Mint1) binds to amyloid-β precursor protein (APP) and also associates with calcium/calmodulin-dependent serine protein kinase (CASK).
Physikalische Form
Solution in phosphate buffered saline containing 1.0 mg/mL bovine serum albumin and 0.05% sodium azide.
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.
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
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)
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