Recombinant Human Electron Transfer Flavoprotein Subunit Alpha, Mitochondrial (ETFA) Protein (GST)

Name: Recombinant Human Electron Transfer Flavoprotein Subunit Alpha, Mitochondrial (ETFA) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09301P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Electron Transfer Flavoprotein Subunit Alpha, Mitochondrial (ETFA) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P13804
Target Symbol	ETFA
Synonyms	Alpha ETF; Alpha-ETF; Electron transfer flavoprotein alpha polypeptide; Electron transfer flavoprotein alpha subunit; Electron transfer flavoprotein subunit alpha mitochondrial; Electron transfer flavoprotein subunit alpha; mitochondrial; Electron transferring flavoprotein alpha polypeptide; EMA; ETFA; ETFA_HUMAN; GA2; Glutaric aciduria II
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MFRAAAPGQLRRAASLLRFQSTLVIAEHANDSLAPITLNTITAATRLGGEVSCLVAGTKCDKVAQDLCKVAGIAKVLVAQHDVYKGLLPEELTPLILATQKQFNYTHICAGASAFGKNLLPRVAAKLEVAPISDIIAIKSPDTFVRTIYAGNALCTVKCDEKVKVFSVRGTSFDAAATSGGSASSEKASSTSPVEISEWLDQKLTKSDRPELTGAKVVVSGGRGLKSGENFKLLYDLADQLHAAVGASRAAVDAGFVPNDMQVGQTGKIVAPELYIAVGISGAIQHLAGMKDSKTIVAINKDPEAPIFQVADYGIVADLFKVVPEMTEILKKK
Expression Range	1-333aa
Protein Length	Full Length
Mol. Weight	62.1kDa
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	Heterodimeric electron transfer flavoprotein that accepts electrons from several mitochondrial dehydrogenases, including acyl-CoA dehydrogenases, glutaryl-CoA and sarcosine dehydrogenase. It transfers the electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). Required for normal mitochondrial fatty acid oxidation and normal amino acid metabolism.
Subcellular Location	Mitochondrion matrix.
Protein Families	ETF alpha-subunit/FixB family
Database References	HGNC: 3481 OMIM: 231680 KEGG: hsa:2108 STRING: 9606.ENSP00000452762 UniGene: Hs.39925
Associated Diseases	Glutaric aciduria 2A (GA2A)

Gene Functions References

Data suggest that ETF (heterodimer of ETFA and ETFB) catalyzes irreversible and pH-dependent oxidation of 8alpha-methyl group of FAD to form to 8-formyl-FAD (8f-FAD). PMID: 29301933
our results indicate that genetic variants in ETFA may modify individual susceptibility to non-GBM of glioma in the Han Chinese population and support the role of the ETFA genes in the occurrence of glioma. PMID: 28320150
the mechanism of tert-butyl hydroperoxide-induced an apoptosis cascade and endoplasmic reticulum stress in hepatocyte cells by up-regulation of ETFA, providing a new mechanism for liver injury. PMID: 24394546
These results are consistent with the electron transfer flavoprotein alpha II domain adopting orientations in solution that deviate from the crystal structure of free ETF towards the active, substrate-bound orientation. PMID: 21308847
investigations are compatible with the notion that the ETFalpha-T171 variant displays an altered conformational landscape that results in reduced protein function under thermal stress PMID: 21219902
Data established structural hotspots within the ETF fold, and provided a rationale for the prediction of effects of mutations in ETF. PMID: 20674745
These studies indicate that a series of conformational changes occur during the assembly of the TMADH.ETF electron transfer complex and that the kinetics of assembly observed with mutant TMADH or ETF complexes are much slower PMID: 11756429
Tissue samples from 16 unrelated patients with ETF deficiency were analysed and the majority of the patients had mutations in the ETFA gene. PMID: 16510302
No mutations in electron-transfer-flavoprotein but maternal riboflavin deficiency led to multiple acyl-CoA dehydrogenation deficiency PMID: 17689999

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.