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BD Transduction Laboratories™ Purified Mouse Anti-Acetylcholine Receptor α
クローン 26/Acetylcholine Receptor α
(RUO)Western blot analysis of Acetylcholine Receptor α on BC3H1 lysate. Lane 1: 1:250, lane 2: 1:500, lane 3: 1:1000 dilution of Acetylcholine Receptor α.
BC3H1
BD Pharmingen™ Purified Mouse Anti-Acetylcholine Receptor α
BD Pharmingen™ Purified Mouse Anti-Acetylcholine Receptor α
Regulatory Statusの凡例
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation and Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
Acetylcholine is an amine neurotransmitter at the neuromuscular junction. It is released from the presynaptic membrane of a cholinergic synapse into the synaptic cleft. It diffuses across the cleft and binds acetylcholine receptors (AChR) on the postsynaptic membrane. Receptor binding induces postsynaptic membrane depolarization and the generation of an action potential that produces effects such as muscle contraction. The AChR is a 250kDa pentameric complex of four transmembrane subunits in a stoichiometry of α2βγδ. In response to ligand binding, all subunits participate in the formation of an integral cation channel. However, the acetylcholine binding site is primarily within the α subunit. Myasthenia gravis (MG) is an autoimmune condition in which AchR levels are decreased. Autoantibodies bind and crosslink the AchRs leading to their internalization and degradation. This results in a decreased number of functional AChRs. Patients develop muscular weakness and some voluntary muscle fatigue. However, development of MG is also affected by genetic factors. One of the allelic forms of the AChRα gene appears to significantly contribute to MG susceptibility.
Development References (5)
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Garchon HJ, Djabiri F, Viard JP, Gajdos P, Bach JF. Involvement of human muscle acetylcholine receptor alpha-subunit gene (CHRNA) in susceptibility to myasthenia gravis. Proc Natl Acad Sci U S A. 1994; 91(11):4668-4672. (Biology). View Reference
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Kincer JF, Uittenbogaard A, Dressman J, et al. Hypercholesterolemia promotes a CD36-dependent and endothelial nitric-oxide synthase-mediated vascular dysfunction. J Biol Chem. 2002; 277(26):23525-23533. (Clone-specific: Western blot). View Reference
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Schroder B, Reinhardt-Maelicke S, Schrattenholz A. Monoclonal antibodies FK1 and WF6 define two neighboring ligand binding sites on Torpedo acetylcholine receptor alpha-polypeptide. J Biol Chem. 1994; 269(14):10407-10416. (Biology). View Reference
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Spencer MJ, Guyon JR, Sorimachi H. Stable expression of calpain 3 from a muscle transgene in vivo: immature muscle in transgenic mice suggests a role for calpain 3 in muscle maturation. Proc Natl Acad Sci U S A. 2002; 99(13):8874-8879. (Clone-specific: Immunohistochemistry, Western blot). View Reference
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Tsim KW, Greenberg I, Rimer M, Randall WR, Salpeter MM. Transcripts for the acetylcholine receptor and acetylcholine esterase show distribution differences in cultured chick muscle cells. J Cell Biol. 1992; 118(5):1201-1212. (Biology). View Reference
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