Recombinant Mouse Nicotinic Acetylcholine Receptor alpha 1/CHRNA1 Protein (His tag)

Beta LifeScience SKU/CAT #: BLA-9980P

Recombinant Mouse Nicotinic Acetylcholine Receptor alpha 1/CHRNA1 Protein (His tag)

Beta LifeScience SKU/CAT #: BLA-9980P
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Product Overview

Host Species Mouse
Accession P04756
Synonym Acetylcholine receptor subunit alpha ACHA_HUMAN AChR ACHRA ACHRD CHNRA Cholinergic receptor nicotinic alpha 1 subunit Cholinergic receptor nicotinic alpha polypeptide 1 Cholinergic receptor, nicotinic, alpha polypeptide 1 (muscle) Chrna1 CMS1A CMS1B CMS2A FCCMS Nicotinic cholinergic receptor alpha 1 SCCMS Schizophrenia neurophysiologic defect candidate
Description Recombinant Mouse Nicotinic Acetylcholine Receptor alpha 1/CHRNA1 Protein (His tag) was expressed in E.coli. It is a Protein fragment
Source E.coli
Molecular Weight 29 kDa including tags
Purity >90% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular Location Cell junction, synapse, postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Protein Families Ligand-gated ion channel (TC 1.A.9) family, Acetylcholine receptor (TC 1.A.9.1) subfamily, Alpha-1/CHRNA1 sub-subfamily
Database References

Gene Functions References

  1. A triad of residues aligning to Thr-152, Glu-209, and Lys-211 in Htr3, appear to be involved in side-chain interactions near binding sites in Htr3a (subunit alpha) and muscle-type Chrna1. Data suggest that mutating Htr3a triad to that of Chrna1 increases binding affinity of nicotine to Htr3a. (Htr3 = 5-hydroxytryptamine/serotonin receptor; Chrna1 = cholinergic receptor nicotinic alpha polypeptide 1) PMID: 29298898
  2. The results indicate that in the absence of the alpha1-nAChR subunit, clusters of nAChRs coupled to SK2 potassium channels as well as functional efferent synapses did form, showing that alpha1 is not necessary for these processes to take place. PMID: 27098031
  3. Findings suggest the possible role of controlling localised inflammatory response by parasympathetic cholinergic nerves through a1nAChRs of inflammation sites. PMID: 26778394
  4. This study demonstrates that genes coding for CHRNA1 subunits may contain variants associated with statin-induced ADRs. PMID: 22688219
  5. Chrna1 was co-purified with nicotinic acetylcholine receptor (AChR) in C2C12 myotubes. In addition, Stau1 was found to interact with Chrna1 mRNA, and knocking down of Stau1 by RNAi resulted in defective AChR clustering. PMID: 22884571
  6. These results suggest that in skeletal muscle cells, neural activity reduces the molar ratio of YB-1 relative to its binding AChR alpha mRNA, leading to an increase of ribosome binding to the mRNA, and thus activating translation. PMID: 21964286
  7. Chrna1 could be the first transcriptional target of atonal homolog 1 in the inner ear PMID: 17961150
  8. The nAChRalpha1 gene plays a significant role at the artery wall, and reducing its expression decreases aortic plaque development. PMID: 20810113
  9. These data identify caveolin-3 as a critical component of the signaling machinery that drives nicotinic acetylcholine receptor clustering and controls neuromuscular junction function. PMID: 19940021
  10. These two residues (and homologous sites in epsilon; subunit) are not involved in specific interactions with nicotinic agonist, and they affect activation of nicotinic receptor by shaping overall structure of agonist binding site. PMID: 12411516
  11. In murine muscle-type AChR alpha transmembrane 3 domain, tryptophan substitution at positions Phe-284, Ala-287, and Ile-290 produces a significant increase in normalized macroscopic response in channel gating, primarily the channel closing rate. PMID: 14705933
  12. the interaction between alpha AChR M1 and M2 domains plays a key role in channel gating PMID: 17028140
  13. Receptors with neutral side chains at position 89 function well, if side chain is less perturbing than amide of asparagine (nitro or keto groups allow function) or if a compensating backbone mutation is introduced to relieve unfavorable electrostatics. PMID: 17223685
  14. HDAC4 is a neural activity-regulated deacetylase and a key signaling component that relays neural activity to the muscle transcriptional machinery through Dach2, myogenin, and nAChR PMID: 17873280
  15. Data suggest that the alpha1 nicotinic acetylcholine receptor might play an important role in mechanotransduction of tensile stress loading on maxillofacial skeletal myocytes. PMID: 18163199
  16. In S269I, mutant the peak-current amplitude decreases along trains of nearly saturating ACh pulses delivered at physiologically relevant frequencies, consistent with enhanced entry into desensitization in congenital myasthenic syndrome. PMID: 19171769
  17. The local anaesthetics proadifen and adiphenine inhibit nicotinic receptors by different molecular mechanisms. PMID: 19422391
  18. In this mouse experiemntal myasthenia gravis study demonstrated that Acetylcholine receptor-alpha1 subunit expression was increase with varying disease severity. PMID: 19609914
  19. fibroblast nicotinic receptor alpha1 binds urokinase and promotes renal fibrosis PMID: 19690163


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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