Description
SCN7A Antibody | 13-423 | Gentaur UK, US & Europe Distribution
Host: Rabbit
Reactivity: Human, Mouse
Homology: N/A
Immunogen: Recombinant fusion protein containing a sequence corresponding to amino acids 265-368 of human SCN7A (NP_002967.2) .
Research Area: Neuroscience
Tested Application: WB
Application: WB: 1:500 - 1:2000
Specificiy: N/A
Positive Control 1: HeLa
Positive Control 2: HT-1080
Positive Control 3: Mouse heart
Positive Control 4: N/A
Positive Control 5: N/A
Positive Control 6: N/A
Molecular Weight: Observed: 260kDa
Validation: N/A
Isoform: N/A
Purification: Affinity purification
Clonality: Polyclonal
Clone: N/A
Isotype: IgG
Conjugate: Unconjugated
Physical State: Liquid
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Concentration: N/A
Storage Condition: Store at -20˚C. Avoid freeze / thaw cycles.
Alternate Name: NaG, Nav2.1, Nav2.2, SCN6A, sodium channel protein type 7 subunit alpha, putative voltage-gated sodium channel subunit alpha Nax, sodium channel protein cardiac and skeletal muscle subunit alpha, sodium channel protein type VII subunit alpha, sodium channel, voltage-gated, type VI, alpha polypeptide, sodium channel, voltage-gated, type VII, alpha subunit, voltage-dependent sodium channel alpha subunit
User Note: Optimal dilutions for each application to be determined by the researcher.
BACKGROUND: This gene encodes one of the many voltage-gated sodium channel proteins. For proper functioning of neurons and muscles during action potentials, voltage-gated sodium channels direct sodium ion diffusion for membrane depolarization. This sodium channel protein has some atypical characteristics; the similarity between the human and mouse proteins is lower compared to other orthologous sodium channel pairs. Also, the S4 segments, which sense voltage changes, have fewer positive charged residues that in other sodium channels; domain 4 has fewer arginine and lysine residues compared to other sodium channel proteins. Several alternatively spliced transcript variants exist, but the full-length natures of all of them remain unknown.