APBA3/Mint-3 Antibody Summary
| Immunogen |
Synthetic peptide corresponding to residues M(1) E F L P E P Q H P P G P P T M D L E(19) of rat Mint3.
|
| Specificity |
NB120-3450 detects munc-18 interacting protein 3 (Mint3) from mouse cells and rat brain samples.
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| Isotype |
IgG
|
| Clonality |
Polyclonal
|
| Host |
Rabbit
|
| Gene |
APBA3
|
| Purity |
Immunogen affinity purified
|
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|
Applications/Dilutions
| Dilutions |
|
| Application Notes |
WB: Detects an approx. 86 kDa protein representing Mint 3 from AtT20 cell extract.
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Packaging, Storage & Formulations
| Storage |
Store at -20C. Avoid freeze-thaw cycles.
|
| Buffer |
PBS
|
| Preservative |
0.05% Sodium Azide
|
| Concentration |
1 mg/ml
|
| Purity |
Immunogen affinity purified
|
Alternate Names for APBA3/Mint-3 Antibody
- Adapter protein X11gamma
- amyloid beta (A4) precursor protein-binding, family A, member 3 (X11-like 2)
- amyloid beta (A4) precursor protein-binding, family A, member 3
- APBA3
- MGC:15815
- MINT3
- mint-3
- Neuronal Munc18-1-interacting protein 3
- Neuron-specific X11L2 protein
- phosphotyrosine-binding/-interacting domain (PTB)-bearing protein
- X11L2
- X11L2amyloid beta A4 precursor protein-binding family A member 3
- X11-like 2 protein
Background
The munc-18 interacting (Mint) protein family is a group of evolutionarily conserved adaptor proteins that function in membrane transport and organization. In mammals, there exist three mint isoforms, Mint 1, 2, and 3. Although there is little amino acid sequence conservation in the amino-terminal half, the carboxy-terminal half of these proteins is highly conserved. Within this conserved portion there exists a phosphotyrosine-binding (PTB) and a PSD-95/DLG-A/ZO-1 (PDZ) domain, which function as protein interaction modules. Mint 1 and 2 appear to be expressed exclusively in the brain and are found to bind to munc-18, an essential component of the synaptic vesicle fusion machinery. Mint 3 is ubiquitously expressed in all tissues and is expressed at the lowest levels in the brain and testis. Studies show that Mint 3 does not interact with munc-18. Mint 3 has been found to interact with the Alzheimers Disease-related amyloid precursor protein (APP) and does so through its PTB and PDZ domains. It has been suggested that Mint 3 links APP to other transport machinery components, thereby regulating it transport, endocytosis, and metabolism. Abnormal APP metabolism has been shown to be the cause of an early-onset type of Alzheimers disease.
