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Mouse Anti-NALCN Recombinant Antibody (N28-9) (CBMAB-V0058-LY)

This product is antibody recognizes NALCN. The antibody N28-9 immunoassay techniques such as: WB, IHC-P, FC.
See all NALCN antibodies

Summary

Host Animal
Mouse
Specificity
Human
Clone
N28-9
Antibody Isotype
IgG1
Application
WB, IHC-P, FC

Basic Information

Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Purity
> 95% Purity determined by SDS-PAGE.
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Sodium Leak Channel, Non-Selective
Introduction
This gene encodes a voltage-independent, nonselective cation channel which belongs to a family of voltage-gated sodium and calcium channels that regulates the resting membrane potential and excitability of neurons. This family is expressed throughout the nervous system and conducts a persistent sodium leak current that contributes to tonic neuronal excitability. The encoded protein forms a channelosome complex that includes G-protein-coupled receptors, UNC-79, UNC-80, NCA localization factor-1, and src family tyrosine kinases. Naturally occurring mutations in this gene are associated with infantile neuroaxonal dystrophy, infantile hypotonia with psychomotor retardation and characteristic facies (IHPRF) syndrome, and congenital contractures of the limbs and face with hypotonia and developmental delay (CLIFAHDD) syndrome. A knockout of the orthologous gene in mice results in paralysis with a severely disrupted respiratory rhythm, and lethality within 24 hours after birth. [provided by RefSeq, Apr 2017]
Entrez Gene ID
UniProt ID
Alternative Names
Sodium Leak Channel, Non-Selective; Voltage Gated Channel Like 1; VGCNL1; CanIon; Sodium Leak Channel Non-Selective Protein; Four Repeat Voltage-Gated Ion Channel; Voltage Gated Channel-Like Protein 1;
Function
Voltage-gated ion channel responsible for the resting Na+ permeability that controls neuronal excitability (PubMed:17448995, PubMed:31409833).

NALCN channel functions as a multi-protein complex, which consists at least of NALCN, NALF1, UNC79 and UNC80 (PubMed:32494638, PubMed:33203861).

NALCN is the voltage-sensing, pore-forming subunit of the NALCN channel complex (PubMed:17448995).

NALCN channel complex is constitutively active and conducts monovalent cations but is blocked by physiological concentrations of extracellular divalent cations (PubMed:32494638).

In addition to its role in regulating neuronal excitability, is required for normal respiratory rhythm, systemic osmoregulation by controlling the serum sodium concentration and in the regulation of the intestinal pace-making activity in the interstitial cells of Cajal (By similarity).

NALCN channel is also activated by neuropeptides such as neurotensin and substance P (SP) through a SRC family kinases-dependent pathway (By similarity).

In addition, NALCN activity is enhanced/modulated by several GPCRs, such as CHRM3 (By similarity).
Biological Process
Calcium ion transmembrane transport Source: UniProtKB
Ion transmembrane transport Source: Reactome
Potassium ion transmembrane transport Source: UniProtKB
Regulation of ion transmembrane transport Source: UniProtKB-KW
Regulation of resting membrane potential Source: UniProtKB
Sodium ion transmembrane transport Source: UniProtKB
Cellular Location
Cell membrane
Involvement in disease
Hypotonia, infantile, with psychomotor retardation and characteristic facies 1 (IHPRF1):
A neurodegenerative disease characterized by variable degrees of hypotonia, speech impairment, intellectual disability, pyramidal signs, subtle facial dysmorphism, and chronic constipation. Some patients manifest neuroaxonal dystrophy, optic atrophy, unmyelinated axons and spheroid bodies in tissue biopsies.
Congenital contractures of the limbs and face, hypotonia, and developmental delay (CLIFAHDD):
A disease characterized by congenital contractures of the limbs and face, resulting in characteristic facial features, abnormal tone, most commonly manifested as hypotonia, and variable degrees of developmental delay.
Topology
Cytoplasmic: 1-36
Helical: 37-57
Extracellular: 58-65
Helical: 66-90
Cytoplasmic: 91-106
Helical: 107-129
Extracellular: 130-137
Helical: 138-158
Cytoplasmic: 159-173
Helical: 174-199
Extracellular: 200-269
Helical: 270-289
Cytoplasmic: 290-294
Helical: 295-322
Extracellular: 323-382
Helical: 383-403
Cytoplasmic: 404-416
Helical: 417-439
Extracellular: 440-447
Helical: 448-468
Cytoplasmic: 469-472
Helical: 473-492
Extracellular: 493-502
Helical: 503-530
Cytoplasmic: 531-543
Pore-forming: 544-563
Extracellular: 564-569
Helical: 570-599
Cytoplasmic: 600-886
Helical: 887-906
Extracellular: 907-915
Helical: 916-939
Cytoplasmic: 940-947
Helical: 948-972
Extracellular: 973-980
Helical: 981-1003
Cytoplasmic: 1004-1015
Helical: 1016-1039
Extracellular: 1040-1104
Pore-forming: 1105-1124
Cytoplasmic: 1125-1129
Helical: 1130-1159
Extracellular: 1160-1210
Helical: 1211-1227
Cytoplasmic: 1228-1236
Helical: 1237-1260
Extracellular: 1261-1271
Helical: 1272-1293
Cytoplasmic: 1294-1296
Helical: 1297-1318
Extracellular: 1319-1331
Helical: 1332-1357
Cytoplasmic: 1358-1378
Pore-forming: 1379-1398
Extracellular: 1399-1420
Helical: 1421-1447
Cytoplasmic: 1448-1738
PTM
Phosphorylated on tyrosine residues.

Monteil, A., Guérineau, N. C., Gil-Nagel, A., Parra-Diaz, P., Lory, P., & Senatore, A. (2024). New insights into the physiology and pathophysiology of the atypical sodium leak channel NALCN. Physiological Reviews, 104(1), 399-472.

Kschonsak, M., Chua, H. C., Weidling, C., Chakouri, N., Noland, C. L., Schott, K., ... & Payandeh, J. (2022). Structural architecture of the human NALCN channelosome. Nature, 603(7899), 180-186.

Zhou, L., Liu, H., Zhao, Q., Wu, J., & Yan, Z. (2022). Architecture of the human NALCN channelosome. Cell Discovery, 8(1), 33.

Kang, Y., & Chen, L. (2022). Structure and mechanism of NALCN-FAM155A-UNC79-UNC80 channel complex. Nature Communications, 13(1), 2639.

Kasap, M., & Dwyer, D. S. (2021). Na+ leak-current channel (NALCN) at the junction of motor and neuropsychiatric symptoms in Parkinson’s disease. Journal of Neural Transmission, 128(6), 749-762.

Xie, J., Ke, M., Xu, L., Lin, S., Huang, J., Zhang, J., ... & Yan, Z. (2020). Structure of the human sodium leak channel NALCN in complex with FAM155A. Nature communications, 11(1), 5831.

Chua, H. C., Wulf, M., Weidling, C., Rasmussen, L. P., & Pless, S. A. (2020). The NALCN channel complex is voltage sensitive and directly modulated by extracellular calcium. Science Advances, 6(17), eaaz3154.

Wie, J., Bharthur, A., Wolfgang, M., Narayanan, V., Ramsey, K., C4RCD Research Group Belnap Newell 2 Claasen Ana 2 Courtright Amanda 2 de Both Matt 2 Huentelman Matthew 2 Rangasamy Sampathkumar 2 Richholt Ryan 2 Schrauwen Isabelle 2 Siniard Ashley L. 2 Szelinger Szabolics 2, ... & Ren, D. (2020). Intellectual disability-associated UNC80 mutations reveal inter-subunit interaction and dendritic function of the NALCN channel complex. Nature communications, 11(1), 3351.

Bouasse, M., Impheng, H., Servant, Z., Lory, P., & Monteil, A. (2019). Functional expression of CLIFAHDD and IHPRF pathogenic variants of the NALCN channel in neuronal cells reveals both gain-and loss-of-function properties. Scientific reports, 9(1), 11791.

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For research use only. Not intended for any clinical use.

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