Render Target: STATIC
Render Timestamp: 2025-01-24T12:00:28.013Z
Commit: 8d9f38232df81570bbc23eaa560b31cb39dd8776
XML generation date: 2024-09-30 01:53:58.478
Product last modified at: 2025-01-01T09:06:12.351Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Na Channel β1 Subunit (D4Z2N) Rabbit mAb #13950

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY H M R
    SENSITIVITY Endogenous
    MW (kDa) 38
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • H-Human 
    • M-Mouse 
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Na Channel β1 Subunit (D4Z2N) Rabbit mAb recognizes endogenous levels of total sodium channel β1 subunit protein.

    Species Reactivity:

    Human, Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human sodium channel β1 subunit protein.

    Background

    Mammalian voltage-gated sodium channels (VGSCs) are composed of a pore-forming α subunit and one or more regulatory β subunits (1). Four separate genes (SCN1B-SCN4B) encode the five mammalian β subunits β1, β1B, β2, β3, and β4. In general, β subunit proteins are type I transmembrane proteins, with the exception of secreted β1B protein (reviewed in 2). β subunits regulate α subunit gating and kinetics, which controls cell excitability (3,4). Sodium channel β subunits also function as Ig superfamily cell adhesion molecules that regulate cell adhesion and migration (5,6). Additional research reveals sequential processing of β subunit proteins by β-secretase (BACE1) and γ secretase, resulting in ectodomain shedding of β subunit and generation of an intracellular carboxy-terminal fragment (CTF). Generation of the CTF is thought to play a role in cell adhesion and migration (7,8). Multiple studies demonstrate a link between β subunit gene mutations and a number of disorders, including epilepsy, cardiac arrhythmia, multiple sclerosis, neuropsychiatric disorders, neuropathy, inflammatory pain, and cancer (9-13).
    The sodium channel β1 subunit (SCN1B) plays a crucial role in neuronal migration and pathfinding during brain development (14). Mutations in the corresponding SCN1B gene are associated with generalized epilepsy with febrile seizures plus 1 (15), Brugada syndrome (16), and familial atrial fibrillation (17). A SCN1B loss of function mutation results in a severe form of pediatric epileptic encephalopathy known as Dravet syndrome (18).
    1. Catterall, W.A. (1992) Physiol Rev 72, S15-48.
    2. Catterall, W.A. (2012) J Physiol 590, 2577-89.
    3. Isom, L.L. et al. (1992) Science 256, 839-42.
    4. Brackenbury, W.J. and Isom, L.L. (2011) Front Pharmacol 2, 53.
    5. Isom, L.L. et al. (1995) Cell 83, 433-42.
    6. Malhotra, J.D. et al. (2000) J Biol Chem 275, 11383-8.
    7. Wong, H.K. et al. (2005) J Biol Chem 280, 23009-17.
    8. Kim, D.Y. et al. (2005) J Biol Chem 280, 23251-61.
    9. Wallace, R.H. et al. (1998) Nat Genet 19, 366-70.
    10. Lopez-Santiago, L.F. et al. (2007) J Mol Cell Cardiol 43, 636-47.
    11. Chioni, A.M. et al. (2009) Int J Biochem Cell Biol 41, 1216-27.
    12. O'Malley, H.A. et al. (2009) Mol Cell Neurosci 40, 143-55.
    13. Valdivia, C.R. et al. (2010) Cardiovasc Res 86, 392-400.
    14. Brackenbury, W.J. et al. (2013) Proc Natl Acad Sci U S A 110, 1089-94.
    15. Meadows, L.S. et al. (2002) J Neurosci 22, 10699-709.
    16. Hu, D. et al. (2012) Heart Rhythm 9, 760-9.
    17. Li, R.G. et al. (2013) Int J Mol Med 32, 144-50.
    18. Patino, G.A. et al. (2009) J Neurosci 29, 10764-78.
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