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Key Documents

M217

Sigma-Aldrich

Monoclonal Anti-Nicotinic Acetylcholine Receptor (α1, α3, α5 Subunits) antibody produced in rat

clone mAb 35, purified immunoglobulin, buffered aqueous solution

Synonym(s):

Anti-ACHR

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About This Item

MDL number:
UNSPSC Code:
12352203

biological source

rat

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

mAb 35, monoclonal

form

buffered aqueous solution

species reactivity

human, chicken, eel

should not react with

Xenopus

technique(s)

immunohistochemistry (frozen sections): 1:3,000

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

Specificity

Binds to the main immunogenic region on the extracellular surface of the α1 subunit of muscle AChR′s and to homologous regions on α3 and α5 subunits of neuronal AChR′s. The epitope is located on the extracellular surface of the α1 subunit of the muscle nicotinic acetylcholine receptor. The antibody binds to denatured chick α5 AChR, but does not bind well to denatured α3, α4, α7, α8, and β2. It may also bind β3 due to homology of main immunogenic region. May be used to localize and detect the α1, α3 and α5 subunits of the nicotinic acetylcholine receptor (AChR).

Immunogen

nicotinic acetylcholine receptor from the electric eel Electrophorus.

Physical form

Solution in 20 mM Na3PO4, pH 7.2, containing 150 mM NaCl and 0.05 % sodium azide.

Legal Information

Sold with permission of the Salk Institute

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 Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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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P J Whiting et al.
Biochemistry, 25(8), 2082-2093 (1986-04-22)
Immunohistochemical studies have previously shown that both the chick brain and chick ciliary ganglion neurons contain a component which shares antigenic determinants with the main immunogenic region of the nicotinic acetylcholine receptor from electric organ and skeletal muscle. Here we
H Gu et al.
Journal of neurochemistry, 66(4), 1454-1461 (1996-04-01)
Adrenal chromaffin cells contain at least two subtypes of nicotinic acetylcholine receptors (nAChRs). These studies were designed to identify and characterize the subtype of nAChR mediating adrenal catecholamine release using the monoclonal antibody mAb35, which recognizes the alpha-subunit of muscle
Jee-Young Park et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 34(31), 10211-10218 (2014-08-01)
Mutations in AChR subunits, expressed as pentamers in neuromuscular junctions (NMJs), cause various types of congenital myasthenic syndromes. In AChR pentamers, the adult ε subunit gradually replaces the embryonic γ subunit as the animal develops. Because of this switch in
W G Conroy et al.
Neuron, 9(4), 679-691 (1992-10-01)
The acetylcholine receptor (AChR) alpha 5 gene has been classified as a member of the AChR gene family based on sequence homology. Expression studies, however, have yet to identify a function for the alpha 5 gene product or even to
M S Saedi et al.
FEBS letters, 267(1), 55-59 (1990-07-02)
The main immunogenic region (MIR) of the acetylcholine receptor (AChR) is the target for the majority of high-affinity autoantibodies produced in myasthenia gravis patients. Some monoclonal antibodies (mAbs) to the MIR bind specifically, but with low affinity, to synthetic AChR

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