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48-602MAG
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sodium channel, voltage-gated, type IX, alpha subunit
Sodium channel protein type IX subunit alpha
Voltage-gated sodium channel subunit alpha Nav1.7
Peripheral sodium channel 1
sodium channel, voltage-gated, type IX, alpha polypeptide
Nav1.7
sodium channel protein type 9 subunit alpha
voltage-gated sodium channel alpha subunit Nav1.7
Neuroendocrine sodium channel
Background Information
Voltage-gated sodium channel subunit alpha Nav1.7 (Nav1.7) is a multi-pass membrane protein containing a single IQ domain that belongs to the sodium channel family. NAV1.7 localizes to the terminal ends of sensory neurons and is believed to have a role in inflammatory pain development and mechanisms. It serves to regulate excitable membrane voltage-dependent Na+ ion permeability. There is a strong probability that Nav1.7 is involved in the transmission of nociceptive information, a suggested involvement supported by its role in a variety of chronic pain neuropathies induced by damage to the peripheral nerves. Nav1.7 is predominantly observed in dorsal root ganglion, and sensory and sympathetic neurons. Lower levels of the protein have been observed in MTC cell line, C-cell carcinoma, and smooth muscle cells. Defects in Nav1.7 expression are causal to several diseases such as autosomal recessive congenital indifference pain, primary erythermalgia, and paroxysmal extreme pain disorder or PEPD.
References
Product Information
Format
Purified
Control
Rat cerebellum tissue
Presentation
Purified mouse monoclonal IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
This Anti-Sodium channel Nav1.7 Antibody, clone N68/6 is validated for use in IH, WB for the detection of Sodium channel Nav1.7.
Key Applications
Immunohistochemistry
Western Blotting
Application Notes
Western Blot Analysis: A previous lot was used by an independent laboratory in HEK293 cell lysate. (James Trimmer, UC Davis/NIH NeuroMab Facility, Department of Neurobiology, Physiology and Behavior, UC Davis, Davis CA 95616-8519. neuromab@ucdavis.edu.)
Biological Information
Immunogen
Recombinant protein corresponding to human Nav1.7.
Clone
N68/6
Concentration
Please refer to the Certificate of Analysis for the lot-specific concentration.
This gene encodes a voltage-gated sodium channel which plays a significant role in nociception signaling. Mutations in this gene have been associated with primary erythermalgia, channelopathy-associated insensitivity to pain, and paroxysmal extreme pain disorder. [provided by RefSeq].
FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. It is a tetrodotoxin-sensitive Na(+) channel isoform. Plays a role in pain mechanisms, especially in the development of inflammatory pain (By similarity). SIZE: 1988 amino acids; 226342 Da
SUBUNIT: The sodium channel consists of a large polypeptide and 2- 3 smaller ones. This sequence represents a large polypeptide. Interacts with NEDD4 and NEDD4L (By similarity).
TISSUE SPECIFICITY: Expressed strongly in dorsal root ganglion, with only minor levels elsewhere in the body, smooth muscle cells, MTC cell line and C-cell carcinoma. Isoform 1 is expressed preferentially in the central and peripheral nervous system while isoform 2 is expressed preferentially in the dorsal root ganglion.
DOMAIN: The sequence contains 4 internal repeats, each with 5 hydrophobic segments (S1,S2,S3,S5,S6) and one positively charged segment (S4). Segments S4 are probably the voltage-sensors and are characterized by a series of positively charged amino acids at every third position.
PTM: Ubiquitinated by NEDD4L; which may promote its endocytosis. Does not seem to be ubiquitinated by NEDD4 (By similarity).
DISEASE: Defects in SCN9A are the cause of primary erythermalgia [MIM:133020]. It is an autosomal dominant disease characterized by recurrent episodes of severe pain associated with redness and warmth in the feet or hands. & Defects in SCN9A are the cause of autosomal recessive congenital indifference to pain [MIM:243000]; also known as channelopathy-associated insensitivity to pain. Affected individuals have a congenital inability to perceive any form of pain, in any part of the body. All other sensory modalities are preserved and the peripheral and central nervous systems are apparently intact. Patients perceive the sensations of touch, warm and cold temperature, proprioception, tickle and pressure, but not painful stimuli. There is no evidence of a motor or sensory neuropathy, either axonal or demyelinating. & Defects in SCN9A are a cause of paroxysmal extreme pain disorder (PEPD) [MIM:167400]; previously known as familial rectal pain (FRP). PEPD is an autosomal dominant paroxysmal disorder of pain and autonomic dysfunction. The distinctive features are paroxysmal episodes of burning pain in the rectal, ocular, and mandibular areas accompanied by autonomic manifestations such as skin flushing.
SIMILARITY: Belongs to the sodium channel family. & Contains 1 IQ domain.
Molecular Weight
Observed at ~ 230 kDa
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Immunohistochemistry in rat cerebellum tissue.
Immunohistochemistry Analysis: 1:400 dilution of this antibody detected Nav1.7 in rat cerebellum tissue.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
The ability to perturb individual genes in genome-wide experiments has been instrumental in unraveling cellular and disease properties. Here we introduce, describe the assembly, and demonstrate the use of comprehensive and versatile transcription activator-like effector (TALE) libraries. As a proof of principle, we built an 11-mer library that covers all possible combinations of the nucleotides that determine the TALE-DNA binding specificity. We demonstrate the versatility of the methodology by constructing a constraint library, customized to bind to a known p53 motif. To verify the functionality in assays, we applied the 11-mer library in yeast-one-hybrid screens to discover TALEs that activate human SCN9A and miR-34b respectively. Additionally, we performed a genome-wide screen using the complete 11-mer library to confirm known genes that confer cycloheximide resistance in yeast. Considering the highly modular nature of TALEs and the versatility and ease of constructing these libraries we envision broad implications for high-throughput genomic assays.
