Recombinant Human Acetylcholine Receptor Subunit Alpha (CHRNA1) Protein (His-Trx)

Name: Recombinant Human Acetylcholine Receptor Subunit Alpha (CHRNA1) Protein (His-Trx)
Brand: Beta LifeScience
SKU: BLC-02223P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Acetylcholine Receptor Subunit Alpha (CHRNA1) Protein (His-Trx) is produced by our E.coli expression system. This is a extracellular protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P02708
Target Symbol	CHRNA1
Synonyms	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
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-Trx
Target Protein Sequence	SEHETRLVAKLFKDYSSVVRPVEDHRQVVEVTVGLQLIQLINVDEVNQIVTTNVRLKQGDMVDLPRPSCVTLGVPLFSHLQNEQWVDYNLKWNPDDYGGVKKIHIPSEKIWRPDLVLYNNADGDFAIVKFTKVLLQYTGHITWTPPAIFKSYCEIIVTHFPFDEQNCSMKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKESRGWKHSVTYSCCPDTPYLDITYHFVMQRL
Expression Range	21-255aa
Protein Length	Extracellular Domain
Mol. Weight	44.1kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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	HGNC: 1955 OMIM: 100690 KEGG: hsa:1134 STRING: 9606.ENSP00000261007 UniGene: PMID: 29688589 This study shown that the genetic analysis revealed that the very early onset JMG had a more prominent genetic predisposition in an autoantigen gene (CHRNA1). PMID: 28364296 Data suggest that the mutations made the cholinergic receptor nicotinic alpha 1 subunit channel (CHRNA1) resistant to the antagonists, not by impairing antagonist binding, but rather by producing a gain-of-function phenotype, e.g. increased agonist sensitivity. PMID: 27649498 Study indicated that nicotinic acetylcholine receptor alpha 1-subunit peptides may act as receptor decoy molecules and inhibit the binding of virus to the native host cell receptors and hence may reduce viral infection. PMID: 26656837 ChRnA1 gene variants did not affect the pharmacodynamics of rocuronium. PMID: 25279974 nicotine contributes to the progression and erlotinib-resistance of the NSCLC xenograft model via the cooperation between nAChR and EGFR. PMID: 25670150 show that AON complementary to the 5' splice site of the exon was the most effective at exon skipping of the minigene with causative mutations, as well as endogenous wild-type CHRNA1 PMID: 25888793 The CHRNA1 extracellular domain is an improved protein for use in antigen-specific Myasthenia Gravis therapeutic strategies. PMID: 24376846 HnRNP L and hnRNP LL antagonistically modulate PTB-mediated splicing suppression of CHRNA1 pre-mRNA. PMID: 24121633 High expression of CHRNA1 is associated with lung adenocarcinoma after complete resection. PMID: 23775407 No mutations were found in CHRNG, CHRND and CHRNA1 genes of Indian families with Escobar syndrome. PMID: 23448903 Findings identify a novel lung cancer risk locus on 2q31.1 which correlates with CHRNA1 expression and replicate previous associations on 15q25.1 in African-Americans. PMID: 23232035 V188 is functionally linked to Y190 in the C-loop and to D200 in beta-strand 10 of the acetylcholine receptor alpha subunit, which connects to the M1 transmembrane domain PMID: 22728938 Studies suggest that the receptor nAChRalpha1 is an important regulator of calpain-1 activation and inflammation in the chronic hypercholesterolemic nephropathy. PMID: 20661225 expression of extracellular domain of human muscle acetylcholine receptor alpha subunit in yeast Pichia pastoris PMID: 12015305 DNA analysis of a father and son with dominant fast channel congenital myasthenic syndrome revealed an AChR alpha-subunit F256L missense mutation affecting channel gating PMID: 15079006 A good correlation was found between the expression of PAX3/7-FKHR and AChR, while MyoD1 was more sensitive but less specific. PMID: 16435141 the interaction between alpha AChR M1 and M2 domains plays a key role in channel gating PMID: 17028140 growth factor-induced HMVEC migration, a key angiogenesis event, requires nAChR activation--an effect mediated in part by nAChR-dependent regulation of thioredoxin activity. PMID: 17082486 Here we describe a mechanism controlling thymic transcription of a prototypic tissue-restricted human auto-antigen gene, CHRNA1 PMID: 17687331 No CHRNA1, CHRNB1, or CHRND mutations were detected, but a homozygous RAPSN frameshift mutation, c.1177-1178delAA, was identified in a family with three children affected with lethal fetal akinesia sequence. PMID: 18179903 study reports homozygous nonsense mutations in CHRNA1 and CHRND and shows that they were lethal PMID: 18252226 Presence of heterogeneous nuclear ribonucleoprotein H-binding motif in CHRNA1 close to the 3' end of an intron is an essential but underestimated splicing regulator of the downstream exon. PMID: 18806275

FAQs

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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.