Recombinant Human Acetylcholine Receptor Subunit Epsilon (CHRNE) Protein (His&Myc)

Name: Recombinant Human Acetylcholine Receptor Subunit Epsilon (CHRNE) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00552P
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 Epsilon (CHRNE) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q04844
Target Symbol	CHRNE
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	KNEELRLYHHLFNNYDPGSRPVREPEDTVTISLKVTLTNLISLNEKEETLTTSVWIGIDWQDYRLNYSKDDFGGIETLRVPSELVWLPEIVLENNIDGQFGVAYDANVLVYEGGSVTWLPPAIYRSVCAVEVTYFPFDWQNCSLIFRSQTYNAEEVEFTFAVDNDGKTINKIDIDTEAYTENGEWAIDFCPGVIRRHHGGATDGPGETDVIYSLIIRRK
Expression Range	21-239aa
Protein Length	Partial
Mol. Weight	32.5 kDa
Research Area	Others
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, Epsilon/CHRNE sub-subfamily
Database References	HGNC: 1966 OMIM: 100725 KEGG: hsa:1145 STRING: 9606.ENSP00000293780 UniGene: PMID: 29383513 Specific mutations in COLQ, RAPSN, and CHRNE occur in specific ethnic populations in Israel and should be taken into account when the diagnosis of congenital myasthenic syndrome is suspected.. PMID: 28024842 mutational analysis of CHRNE revealed a homozygous 1293insG, which is a well-known low-expressor receptor mutation in patients with epidermolysis bullosa simplex and congenital myasthenic syndrome. PMID: 21175599 This study provied that new mouse model for the slow-channel congenital myasthenic syndrome induced by the AChR epsilonL221F mutation. PMID: 22178625 Three siblings have a clinical history and examination findings typical of homozygous CHRNE mutations; clinical presentation of congenital myasthenia subtypes is variable, and accurate genotyping is essential in choosing appropriate treatment. PMID: 21150643 Targeting nAChR could offer a strategy for reducing neurodegeneration secondary to hyperphosphorylation of protein tau. PMID: 21715663 The mutations in the varepsilon subunit altered Ca(2+) permeability of AChR-channels, with varepsilon(L269F) increasing P(f) and varepsilon(I257F) decreasing it. PMID: 21470676 analysis of symmetry at the extracellular domain-transmembrane domain interface in acetylcholine receptor channel gating PMID: 20864527 two binding sites differ by roughly 10-fold in the affinity of the shut receptor for ACh in the wild type, and that in the epsilonL221F mutation the lower affinity is increased so the sites become more similar. PMID: 12562900 There was deletion in exon 7 of CHRNE. We cloned the entire CHRNE spanning 12 exons and 11 introns and expressed it in COS cells PMID: 14532324 It was found that mutations within muscle AChRs are the most common cause of CMS. The majority are located within the epsilon-subunit gene and result in AChR deficiency. PMID: 14592868 AChR epsilon-chain peptides are tested for their in vitro ability to activate peripheral blood mononuclear leukocytes of myasthenia gravis (MG) patients; MG patient cells are stimulated, whereas cells from nonmyasthenic subjects do not respond. PMID: 15652413 Reported is a patient with a congenital myasthenic syndrome due to two compound heterozygous mutations of the CHRNE gene. T PMID: 16087917 a patient with a slow-channel congenital myasthenic syndrome who carries a novel slow-channel mutation(novel valine to phenylalanine mutation ) in the epsilon subunit of the acetylcholine receptor. PMID: 16198106 the intrinsically high Ca2+ permeability of human AChRs probably predisposes to development of the endplate myopathy when opening events of the AChR channel are prolonged by altered AChR-channel kinetics PMID: 16527851 enhanced Ca2+ permeability of the mutant receptors overrides the protective effect of desensitization and, together with the prolonged opening events of the AChR channel, is important in slow channel syndromes PMID: 17272341 Upon activation of AChR, GABP recruits the histone acetyl transferase (HAT) p300 on the AChR epsilon subunit promoter, whereas it rather recruits the histone deacetylase HDAC1 when the promoter is not activated. PMID: 17304221 This is the first synonymous mutation in CHRNE known to generate a cryptic splice site, and mRNA quantification strongly suggests that it is the disease-causing mutation. PMID: 17363247 The greater abundance of mRNA for AChR epsilon-subunit than for other subunits suggests that the AChR epsilon-subunit may play a distinctive role in autosensitization in MG-associated thymomas, particularly those of type A or AB. PMID: 18657869 These results strongly support the hypothesis that epsilon1293insG mutations in a myasthenic syndrome derives from an ancient single founder event in the North African population. PMID: 19064877 We have identified mutations within the acetylcholine receptor (AChR) epsilon-subunit gene underlying congenital myasthenic syndromes in nine patients (seven kinships) of Dutch origin. PMID: 19544078

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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.