Anti-alpha1-Syntrophin

Antibodies

Syntrophin alpha 1, Syntrophin-1, 59 kDa dystrophin-associated protein A1 acidic component 1

Shipped at room temperature. Product as supplied can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C

Lyophilized powder. Reconstituted antibody contains phosphate buffered saline (PBS), pH 7.4

Syntrophin alpha 1, Syntrophin-1, 59 kDa dystrophin-associated protein A1 acidic component 1 - A Rabbit Polyclonal Antibody to α1-Syntrophin (SNTA1)

Mouse, human - identical

Confirmed by amino acid analysis and mass spectrometry

0.8 mg/ml

Intracellular, PH1 domain

Mouse

41116161

α1-Syntrophin is a component of the dystrophin scaffold-protein complex that acts in recruiting proteins through their multiple protein-protein interaction motifs to the cytoplasmic side of plasma membranes. Proteins interacting with α1-syntrophin include voltage-gated sodium channels, neuronal nitric oxide synthase, calmodulin, ankyrin repeat-rich membrane spanning protein, G-proteins and more. The syntrophin family comprises five members: α1-syntrophin, β1-syntrophin, β2-syntrophin, γ1-syntrophin, and γ2-syntrophin1.α1-Syntrophin is a peripheral cytoplasmic membrane protein in skeletal and cardiac muscle cells1.The α1-syntrophin structure contains four conserved domains, two pleckstrin homology domains (PH1 and PH2), a PSD95-disks large-ZO1 (PDZ) domain and a syntrophin unique (SU) COOH-terminal domain2. The pleckstrin domains are responsible for the recruitment of proteins to the sarcolemma. The PDZ domain is inserted within the PH1 domain and binds to NOS-1 in skeletal muscle. This domain also binds to the C-terminus of the Kir2.1 channel and also to NaV1.5 and so allowing them to interact. The SU domain binds syntrophin to dystrophin2, 3. α1-Syntrophin is also responsible for the site-specific anchoring of AQP4 protein. α1-Syntrophin deletion leads to the disruption of the polarized subcellular expression of AQP4 in the perivascular membranes4. Several studies have shown that syntrophin-deficiency in Duchenne muscular dystrophy can ultimately lead to muscle degeneration. Syntrophin-deficiency was also shown to reduce levels of nNOS in mice5, 6.