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Key Documents

AB3532P

Sigma-Aldrich

Anti-Epithelial Sodium Channel-β Antibody

Chemicon®, from rabbit

Synonym(s):

ENaC-beta

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

affinity purified immunoglobulin

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

rat, mouse

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... SCNN1B(6338)

Specificity

Recognizes rat Epithelial Sodium Channel beta (ENaC beta). The immunogen shows no significant sequence homology with other ENaC subunits.

Immunogen

A 20 amino acid peptide sequence near the N-terminus of rat ENaC beta. The immunogen sequence is 100% conserved in mouse, 94% in rabbit, 81% in human, 76% in ovine and 64% in xenopus.

Application

Research Category
Neuroscience
Research Sub Category
Ion Channels & Transporters

Neuroinflammation & Pain
This Anti-Epithelial Sodium Channel-β Antibody is validated for use in ELISA, WB for the detection of Epithelial Sodium Channel-β.
Western blot: 1-10 μg/mL using ECL. 83-90kDa bands, membrane preparations are recommended (Masilamani et al., 1999).

ELISA: 0.5-1.0 mg/mL using 1 mg/mL control peptide to coat plate.

Optimal working dilutions must be determined by the end user.

Physical form

Affinity purified immunoglobulin in PBS containing 0.1% BSA.

Storage and Stability

Maintain at -20°C in undiluted aliquots for up to 6 months from date of receipt. Avoid repeated freeze/thaw cycles.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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N Voilley et al.
Genomics, 28(3), 560-565 (1995-08-10)
Three subunits of the amiloride-sensitive Na+ channel, named alpha, beta, and gamma, have previously been cloned in rat colon. The human lung alpha chain (SCNN1A) has also been cloned and its gene localized on chromosome 12p13. We now report the
J H Hansson et al.
Nature genetics, 11(1), 76-82 (1995-09-01)
Sensitivity of blood pressure to dietary salt is a common feature in subjects with hypertension. These features are exemplified by the mendelian disorder, Liddle's syndrome, previously shown to arise from constitutive activation of the renal epithelial sodium channel due to
S S Chang et al.
Nature genetics, 12(3), 248-253 (1996-03-01)
Autosomal recessive pseudohypoaldosteronism type I is a rare life-threatening disease characterized by severe neonatal salt wasting, hyperkalaemia, metabolic acidosis, and unresponsiveness to mineralocorticoid hormones. Investigation of affected offspring of consanguineous union reveals mutations in either the alpha or beta subunits
R Kreutz et al.
Hypertension (Dallas, Tex. : 1979), 29(1 Pt 1), 131-136 (1997-01-01)
The pathophysiological basis of Liddle's syndrome, a rare autosomal dominant form of arterial hypertension, has been found to rest on missense mutations or truncations of the beta- and gamma-subunits of the epithelial sodium channel. The hypothesis has been advanced that
Epithelial sodium channels: function, structure, and regulation
Garty, H. and Palmer, L.G.
Physiological Reviews, 77(2), 359-396 (1997)

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