Recombinant Human Atp Synthase Subunit Alpha, Mitochondrial (ATP5F1A) Protein (His-SUMO)

Name: Recombinant Human Atp Synthase Subunit Alpha, Mitochondrial (ATP5F1A) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-02283P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) ATP5A1.

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Product Overview

Description	Recombinant Human Atp Synthase Subunit Alpha, Mitochondrial (ATP5F1A) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P25705
Target Symbol	ATP5F1A
Synonyms	ATP synthase alpha chain; ATP synthase alpha chain; mitochondrial; ATP synthase subunit alpha; ATP synthase subunit alpha mitochondrial; ATP synthase; H+ transporting; mitochondrial F1 complex; alpha subunit 1; cardiac muscle; ATP synthase; H+ transporting; mitochondrial F1 complex; alpha subunit; 1; ATP synthase; H+ transporting; mitochondrial F1 complex; alpha subunit; isoform 1; cardiac muscle; ATP synthase; H+ transporting; mitochondrial F1 complex; alpha subunit; isoform 2; non-cardiac muscle-like 2; ATP sythase (F1 ATPase) alpha subunit; ATP5A; Atp5a1; ATP5AL2; ATPA_HUMAN; ATPM; Epididymis secretory sperm binding protein Li 123m; hATP1; HEL-S-123m; MC5DN4; mitochondrial; Mitochondrial ATP synthetase; Mitochondrial ATP synthetase oligomycin resistant; Modifier of Min 2; Modifier of Min 2 mouse homolog; Modifier of Min 2; mouse; homolog of; MOM2; OMR; ORM; OTTHUMP00000163475
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	QKTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGSDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRADGKISEQSDAKLKEIVTNFLAGFEA
Expression Range	44-553aa
Protein Length	Full Length of Mature Protein
Mol. Weight	71.2kDa
Research Area	Metabolism
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	Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites. Binds the bacterial siderophore enterobactin and can promote mitochondrial accumulation of enterobactin-derived iron ions.
Subcellular Location	Mitochondrion. Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. Cell membrane; Peripheral membrane protein; Extracellular side.
Protein Families	ATPase alpha/beta chains family
Database References	HGNC: 823 OMIM: 164360 KEGG: hsa:498 STRING: 9606.ENSP00000282050 UniGene: PMID: 29207195 This cohort study showed that the ATP5A1 gene was down regulation between patients with idiopathic Parkinson disease and controls PMID: 28916538 these data highlight a key role of the P2Y1/PI3Kbeta axis in endothelial cell proliferation downstream of ecto-F1-ATPase activation by apoA-I. Pharmacological targeting of this pathway could represent a promising approach to enhance vascular endothelial protection. PMID: 28578353 These findings, together with the previously reported inhibition of respiratory complex I, show that depression of the activity of oxidative phosphorylation enzymes is involved in the cell growth inhibitory action of ATRA. PMID: 27856255 High mRNA levels of ATP5A1 are associated with glioblastoma. PMID: 26526033 Hemoglobin - a novel ligand of hepatocyte ectopic F1-ATPase PMID: 26769832 Here, we found that ATP synthase subunit alpha (ATP5A) was O-GlcNAcylated at Thr432 and ATP5A O-GlcNAcylation was decreased in the brains of AD patients and transgenic mouse model PMID: 26358770 Mitochondrial calpain-1 disrupts ATP synthase, leading to mitochondrial reactive oxygen species generation, which promotes proinflammatory response and myocardial dysfunction during endotoxemia. PMID: 26246018 Studies indicate that the F-ATP synthase can reversibly undergo a Ca(2+)-dependent transition to form a channel that mediates the permeability transition. PMID: 25999424 A mutation in ATP5A1 causes a fatal neonatal mitochondrial encephalopathy. PMID: 23599390 Studies indicate that F1-ATPase (F1) is a rotary motor protein driven by ATP hydrolysis and the minimum complex of F1 for function as a rotary motor is the alpha3beta3gamma subcomplex. PMID: 23395605 Homozygous mutations in this gene are the likely cause of mitochondrial disease in two sisters, with support from a yeast model. PMID: 23596069 F1-ATPase at the cell surface of colonic epithelial cells has a role in mediating cell proliferation PMID: 23055519 An interactive proteomics study was done to examine proteins that bind heterocomplexes with ABCC1 using coimmunoprecipitation and MS/MS analyses. We found that ATP synthase alpha binds to ABCC1 in plasma membranes with a ratio of 2:1. PMID: 22188235 Antibodies to the beta- and gamma-subunits of F(1)-ATPase are further antimitochondrial antibodies in primary biliary cirrhosis. PMID: 22098431 A selective Cys in ATP synthase alpha subunit is targeted by multiple oxidative posttranslational modifications suggesting that this Cys residue may act as a redox sensor modulating ATP synthase function. PMID: 21817160 Data suggest that F1-ATPase catalytic site show the correlation between the phosphate binding and the tightening of the alphabeta-interface. PMID: 21481781 This protein has been found differentially expressed in the anterior cingulate cortex in men patients with schizophrenia. PMID: 20381070 The alpha-chain of ATP synthase is implicated in neurofibrillary degeneration of Alzheimer's disease that is illustrated by the cytosolic accumulation of this mitochondrial protein, which belongs to the mitochondrial respiratory system. PMID: 12614671 Within the structurally-confined internal aqueous cavity of the F1-motor of ATP synthase, function results from free energy changes that shift the balance between interfacial charge hydration and interfacial hydrophobic hydration. PMID: 16378738 analysis of vascular endothelial ectoadenylate kinase and plasma membrane ATP synthase PMID: 16714292 Higher levels of ATP5a1 expression are associated with certain Single Nucleotide Polymorphisms and with TP53 mutation. PMID: 19261598 These data show that an linoleic acid-phospholipid induced stimulation in hepatic HDL secretion is related to the expression and function of membrane ATP metabolizing proteins. PMID: 19717637 This protein has been found differentially expressed in the Wernicke's Area from patients with schizophrenia. PMID: 19405953 This protein has been found differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia. PMID: 19110265

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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.