AB5164
Anti-Muscarinic Acetylcholine Receptor m1 Antibody
Chemicon®, from rabbit
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.43
Productos recomendados
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)
immunohistochemistry: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... CHRM1(1128)
Specificity
Recognizes a full length m1 protein. It has exhibited no cross reactivity with other muscarinic proteins tested so far.
Immunogen
GST fusion protein and part of i3 intercellular loop of human m1 muscarinic acetylcholine receptor (amino acids 227-353) (Accession P11229).
Application
Research Category
Neuroscience
Neuroscience
Research Sub Category
Neurotransmitters & Receptors
Neurotransmitters & Receptors
This Anti-Muscarinic Acetylcholine Receptor m1 Antibody is validated for use in IH, WB for the detection of Muscarinic Acetylcholine Receptor m1.
Western blot: 1:200 using ECL on rat brain membranes with proteinase inhibitors. M1 is approximately 60-80kDa in size, some preparations yield 125kDa dimers (photo). Heating samples to 80-90C rather than fulling boiling and adjusting sample pH to neutral can help in preventing dimer formation.
Dilutions should be made using a carrier protein such as BSA (1-3%)
Immunohistochemistry: rat frozen sections. 1:50-1:200, internal epitope; use triton X-100 in blocking buffer only; dilute primary antibody in PBS or TBS with 0.5%-1% BSA or NGS only.
Optimal working dilutions must be determined by the end user.
Dilutions should be made using a carrier protein such as BSA (1-3%)
Immunohistochemistry: rat frozen sections. 1:50-1:200, internal epitope; use triton X-100 in blocking buffer only; dilute primary antibody in PBS or TBS with 0.5%-1% BSA or NGS only.
Optimal working dilutions must be determined by the end user.
Physical form
Affinity purified immunoglobulin. Lyophilized from phosphate buffered saline, pH 7.4, containing 1% BSA and 0.05% sodium azide as a preservative. Reconstitute with 200 μL of sterile deionized water. Centrifuge antibody preparation before use (10,000 x g for 5 min).
Storage and Stability
Maintain lyophilized material at -20°C for up to 12 months after date of receipt. After reconstitution maintain at -20°C in undiluted aliquots for up to 6 months. Avoid repeated freeze/thaw cycles.
Analysis Note
Control
Included free of charge with the antibody is 60 μg of control fusion protein (lyophilized powder). The stock solution of the fusion protein can be made up using 100 μL of PBS. For positive control, in Western blot using 10 ng of protein per minigel lane. For negative control, preincubate 3 μg of fusion protein with 1 μg of antibody for one hour at room temperature. Optimal concentrations must be determined by the end user.
Included free of charge with the antibody is 60 μg of control fusion protein (lyophilized powder). The stock solution of the fusion protein can be made up using 100 μL of PBS. For positive control, in Western blot using 10 ng of protein per minigel lane. For negative control, preincubate 3 μg of fusion protein with 1 μg of antibody for one hour at room temperature. Optimal concentrations must be determined by the end user.
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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hcodes
pcodes
Hazard Classifications
Aquatic Chronic 3
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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M Takamori et al.
European journal of neurology, 14(11), 1230-1235 (2007-09-04)
The Lambert-Eaton myasthenic syndrome (LEMS), often associated with small-cell lung carcinoma (SCLC), is a disorder of acetylcholine (ACh) release from motor nerve terminals. In most patients, it is caused by autoantibodies against the P/Q-type voltage-gated calcium channels (VGCC) that trigger
Marci L Smith et al.
Molecular vision, 20, 1328-1356 (2014-10-30)
The α7 nicotinic acetylcholine receptor (nAChR) is widely expressed in the nervous system, including in the inner retinal neurons in all species studied to date. Although reductions in the expression of α7 nAChRs are thought to contribute to the memory
Gitte Jositsch et al.
Naunyn-Schmiedeberg's archives of pharmacology, 379(4), 389-395 (2008-11-01)
Acetylcholine (ACh) is a major regulator of visceral function exerting pharmacologically relevant effects upon smooth muscle tone and epithelial function via five types of muscarinic receptors (M1R-M5R). In this paper, we assessed the specificity of muscarinic receptor (MR) antibodies in
Chase M Carver et al.
Frontiers in neuroscience, 15, 681144-681144 (2021-09-08)
We investigated the contribution of excitatory transient receptor potential canonical (TRPC) cation channels to posttraumatic hyperexcitability in the brain 7 days following controlled cortical impact model of traumatic brain injury (TBI) to the parietal cortex in male adult mice. We
Eleanor D Muise et al.
Data in brief, 10, 482-486 (2017-01-06)
The data presented in this article are related to the research article entitled "Distribution of muscarinic acetylcholine receptor subtypes in the murine small intestine" (E.D. Muise, N. Gandotra, J.J. Tackett, M.C. Bamdad, R.A. Cowles, 2016) [1]. We recently demonstrated that
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