由来生物
rabbit
品質水準
結合体
unconjugated
抗体製品の状態
affinity isolated antibody
抗体製品タイプ
primary antibodies
クローン
polyclonal
形状
buffered aqueous solution
分子量
antigen ~130 kDa
化学種の反応性
rat
テクニック
western blot: 1 μg/mL using rat forebrain postnuclear supernatant
UniProtアクセッション番号
輸送温度
dry ice
保管温度
−20°C
ターゲットの翻訳後修飾
unmodified
遺伝子情報
rat ... Apba1(83589)
詳細
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.
特異性
Detects rat munc-18 interacting protein 1 (mint1) using rat brain extract and extract from HEK293 cells overexpressing the rat gene.
免疫原
synthetic peptide corresponding to amino acid residues 1-17 from rat mint1.
生物化学的/生理学的作用
Munc-18 interacting protein 1 (Mint1) binds to amyloid-β precursor protein (APP) and also associates with calcium/calmodulin-dependent serine protein kinase (CASK).
物理的形状
PBS溶液(1.0mg/mL BSA, 0.05%アジ化ナトリウム含有)。
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保管分類コード
10 - Combustible liquids
試験成績書(COA)
製品のロット番号・バッチ番号を入力して、試験成績書(COA) を検索できます。ロット番号・バッチ番号は、製品ラベルに「Lot」または「Batch」に続いて記載されています。
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
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