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CHRM3 recombinant protein :: Muscarinic acetylcholine receptor M3 Recombinant Protein

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Catalog # MBS955742
Unit / Price
Scan QR to view Datasheet
  0.01 mg (E-Coli)  /  $160 +1 FREE 8GB USB
  0.01 mg (Yeast)  /  $175 +1 FREE 8GB USB
  0.05 mg (E-Coli)  /  $200 +1 FREE 8GB USB
  0.05 mg (Yeast)  /  $225 +1 FREE 8GB USB
  0.1 mg (E-Coli)  /  $295 +1 FREE 8GB USB
  0.1 mg (Yeast)  /  $355 +1 FREE 8GB USB
  0.2 mg (E-Coli)  /  $480 +1 FREE 8GB USB
  0.2 mg (Yeast)  /  $565 +1 FREE 8GB USB
  0.5 mg (E-Coli)  /  $790 +1 FREE 8GB USB
  0.5 mg (Yeast)  /  $925 +1 FREE 8GB USB
  1 mg (E-Coli)  /  $1,215 +1 FREE 8GB USB
  1 mg (Yeast)  /  $1,410 +1 FREE 8GB USB
Product Name

Muscarinic acetylcholine receptor M3 (CHRM3), Recombinant Protein

Popular Item
Full Product Name

Recombinant Human Muscarinic acetylcholine receptor M3

Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
253-492. Partial.
3D Structure
ModBase 3D Structure for P20309
E Coli or Yeast or Baculovirus or Mammalian Cell
Greater than 90% as determined by SDS-PAGE. (lot specific)
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterile filter available upon request.
Low endotoxin available upon request.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of CHRM3 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
CHRM3 recombinant protein
The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover.
Product Categories/Family for CHRM3 recombinant protein

CHRM3 recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for CHRM3. It may not necessarily be applicable to this product.
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
NCBI Official Full Name
muscarinic acetylcholine receptor M3
NCBI Official Synonym Full Names
cholinergic receptor, muscarinic 3
NCBI Official Symbol
CHRM3  [Similar Products]
NCBI Official Synonym Symbols
  [Similar Products]
NCBI Protein Information
muscarinic acetylcholine receptor M3
UniProt Protein Name
Muscarinic acetylcholine receptor M3
UniProt Gene Name
CHRM3  [Similar Products]
UniProt Entry Name
NCBI Summary for CHRM3
The muscarinic cholinergic receptors belong to a larger family of G protein-coupled receptors. The functional diversity of these receptors is defined by the binding of acetylcholine and includes cellular responses such as adenylate cyclase inhibition, phosphoinositide degeneration, and potassium channel mediation. Muscarinic receptors influence many effects of acetylcholine in the central and peripheral nervous system. The muscarinic cholinergic receptor 3 controls smooth muscle contraction and its stimulation causes secretion of glandular tissue. [provided by RefSeq, Jul 2008]
UniProt Comments for CHRM3
mAChR M3: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is Pi turnover. Defects in CHRM3 are the cause of Eagle-Barrett syndrome (EGBRS). EGBRS is a syndrome characterized by thin abdominal musculature with overlying lax skin, cryptorchism, megacystis with disorganized detrusor muscle, and urinary tract abnormalities. Belongs to the G-protein coupled receptor 1 family. Muscarinic acetylcholine receptor subfamily. CHRM3 sub-subfamily.

Protein type: Receptor, GPCR; Membrane protein, integral; Membrane protein, multi-pass; GPCR, family 1

Chromosomal Location of Human Ortholog: 1q43

Cellular Component: asymmetric synapse; basolateral plasma membrane; cell junction; dendrite; integral to plasma membrane; nerve terminal; plasma membrane; postsynaptic membrane; synapse

Molecular Function: acetylcholine binding; drug binding; G-protein coupled acetylcholine receptor activity; phosphoinositide phospholipase C activity; protein binding; receptor activity

Biological Process: acetylcholine receptor signaling, muscarinic pathway; cell proliferation; energy reserve metabolic process; G-protein coupled receptor protein signaling pathway; muscarinic acetylcholine receptor, adenylate cyclase inhibiting pathway; muscarinic acetylcholine receptor, phospholipase C activating pathway; nervous system development; positive regulation of smooth muscle contraction; protein modification process; regulation of insulin secretion; regulation of vascular smooth muscle contraction; saliva secretion; signal transduction; smooth muscle contraction; synaptic transmission, cholinergic

Disease: Abdominal Muscles, Absence Of, With Urinary Tract Abnormality And Cryptorchidism
Product References and Citations for CHRM3 recombinant protein
Distinct primary structures, ligand-binding properties and tissue-specific expression of four human muscarinic acetylcholine receptors.Peralta E.G., Ashkenazi A., Winslow J.W., Smith D.H., Ramachandran J., Capon D.J.EMBO J. 6:3923-3929(1987) Cloning and expression of the human and rat m5 muscarinic acetylcholine receptor genes.Bonner T.I., Young A.C., Brann M.R., Buckley N.J.Neuron 1:403-410(1988) Human-specific amino acid changes found in 103 protein-coding genes.Kitano T., Liu Y.-H., Ueda S., Saitou N.Mol. Biol. Evol. 21:936-944(2004) cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org) .Puhl H.L. III, Ikeda S.R., Aronstam R.S. The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006) Antisense promoter of human L1 retrotransposon drives transcription of adjacent cellular genes.Speek M.Mol. Cell. Biol. 21:1973-1985(2001) Mutation of carboxyl-terminal threonine residues in human M3 muscarinic acetylcholine receptor modulates the extent of sequestration and desensitization.Yang J., Williams J.A., Yule D.I., Logsdon C.D.Mol. Pharmacol. 48:477-485(1995) Muscarinic acetylcholine receptor M3 mutation causes urinary bladder disease and a prune-belly-like syndrome.Weber S., Thiele H., Mir S., Toliat M.R., Sozeri B., Reutter H., Draaken M., Ludwig M., Altmuller J., Frommolt P., Stuart H.M., Ranjzad P., Hanley N.A., Jennings R., Newman W.G., Wilcox D.T., Thiel U., Schlingmann K.P., Beetz R., Hoyer P.F., Konrad M., Schaefer F., Nurnberg P., Woolf A.S.Am. J. Hum. Genet. 89:668-674(2011) The muscarinic M3 acetylcholine receptor exists as two differently sized complexes at the plasma membrane.Patowary S., Alvarez-Curto E., Xu T.R., Holz J.D., Oliver J.A., Milligan G., Raicu V.Biochem. J. 452:303-312(2013) Identification and structural determination of the M(3) muscarinic acetylcholine receptor basolateral sorting signal.Iverson H.A., Fox D. III, Nadler L.S., Klevit R.E., Nathanson N.M.J. Biol. Chem. 280:24568-24575(2005)

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