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Merck

S6936

Sigma-Aldrich

Anti-Sodium Channel, Pan antibody produced in rabbit

affinity isolated antibody, lyophilized powder

Sinónimos:

Anti-SP19

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

lyophilized powder

species reactivity

rat

technique(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
immunoprecipitation (IP): suitable
western blot (chemiluminescent): 1:200-1:600

UniProt accession no.

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

General description

Voltage-gated sodium channels (VGSC) are membrane proteins that are usually present in excitable cells. These sodium channels regulate neurological functions such as the generation of action potentials in nerve cells. Alterations in neurological sodium ion channels have been associated with epilepsy, whereas mutations in cardiac sodium channels have been linked to long QT syndrome . Anti-Sodium Channel, Pan antibody is specific for the α subunit of VGSC in rats.

Immunogen

synthetic peptide corresponding to amino acids 1491-1508 of the α subunit of rat type I voltage-gated sodium channel (VGSC, SP19) (with additional C-terminal cysteine). The epitope corresponds to the sequence in the intracellular loop between the III and IV domains of the VGSC α subunit.This epitope is identical in vertebrates, and highly homologous in mollusks and insects.

Application

Anti-Sodium Channel, Pan antibody is suitable for use in immunohistochemistry (formalin-fixed, paraffin-embedded sections), immunoprecipitation and chemiluminescent western blot.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Immunofluorescence (1 paper)
Immunohistochemistry (1 paper)

Physical form

Lyophilized from phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin, and 0.05% sodium azide.

Disclaimer

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.

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Optional

pictograms

Skull and crossbones

signalword

Danger

Hazard Classifications

Acute Tox. 3 Dermal - Acute Tox. 4 Inhalation - Acute Tox. 4 Oral - Aquatic Chronic 3

Storage Class

6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

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G M Vincent et al.
Cardiology in review, 7(1), 44-55 (1999-06-01)
The inherited long QT syndrome is caused by mutations of at least 5 ion channel genes. Mutations of the cardiac sodium ion channel gene and 3 potassium channel genes have been identified to this time. A genetic locus on chromosome
Megan Oliva et al.
Epilepsia, 53(11), 1849-1859 (2012-08-22)
Voltage-gated sodium channels (VGSCs) are integral membrane proteins. They are essential for normal neurologic function and are, currently, the most common recognized cause of genetic epilepsy. This review summarizes the neurobiology of VGSCs, their association with different epilepsy syndromes, and
Ricardo Scott et al.
Cerebral cortex (New York, N.Y. : 1991), 29(2), 586-597 (2018-01-05)
Contactin-associated protein-like 2 (Caspr2) is found at the nodes of Ranvier and has been associated with physiological properties of white matter conductivity. Genetic variation in CNTNAP2, the gene encoding Caspr2, has been linked to several neurodevelopmental conditions, yet pathophysiological effects
Dipankar J Dutta et al.
Frontiers in cellular neuroscience, 15, 576609-576609 (2021-04-06)
In the central nervous system, myelin is attached to the axon in the paranodal region by a trimolecular complex of Neurofascin155 (NF155) in the myelin membrane, interacting with Caspr1 and Contactin1 on the axolemma. Alternative splicing of a single Neurofascin
X Liu et al.
Respiratory physiology & neurobiology, 178(3), 362-369 (2011-03-15)
Experiments in recent years have revealed labile electrophysiological and neurochemical phenotypes in primary afferent neurons exposed to specific stimulus conditions associated with the development of chronic pain. These studies collectively demonstrate that the mechanisms responsible for functional plasticity are primarily

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