Recombinant Human ATP synthase subunit alpha, mitochondrial(ATP5F1A)

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Code CSB-EP002344HUa2
Size US$1726Purchase it in Cusabio online store
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP002344HUa2 could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) ATP5A1.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP002344HUa2 could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) ATP5A1.
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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names ATP5F1A
Uniprot No. P25705
Research Area Metabolism
Alternative Names 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)
Source E.coli
Expression Region 44-553aa
Target Protein Sequence QKTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGEELLGRVVDALGNAIDGKGPIGSKTRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGSDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVAYRQMSLLLRRPPGREAYPGDVFYLHSRLLERAAKMNDAFGGGSLTALPVIETQAGDVSAYIPTNVISITDGQIFLETELFYKGIRPAINVGLSVSRVGSAAQTRAMKQVAGTMKLELAQYREVAAFAQFGSDLDAATQQLLSRGVRLTELLKQGQYSPMAIEEQVAVIYAGVRGYLDKLEPSKITKFENAFLSHVVSQHQALLGTIRADGKISEQSDAKLKEIVTNFLAGFEA
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 71.2kDa
Protein Length Full Length of Mature Protein
Tag Info N-terminal 6xHis-SUMO-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Basically, we can dispatch the products out in 3-7 working days after receiving your orders. Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

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 (By similarity).
Gene References into Functions
  1. Using systems biology techniques to study gene coexpression network, ATP5A1 was identified and found highly expressed in normal kidney than clear cell renal cell carcinoma (ccRCC) tissues of each grade. Functional and pathway enrichment analysis demonstrated that ATP5A1 is overrepresented in pathway of oxidative phosphorylation, which associated with tumorigenesis and tumor progression. PMID: 29207195
  2. This cohort study showed that the ATP5A1 gene was down regulation between patients with idiopathic Parkinson disease and controls PMID: 28916538
  3. 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
  4. 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
  5. High mRNA levels of ATP5A1 are associated with glioblastoma. PMID: 26526033
  6. Hemoglobin - a novel ligand of hepatocyte ectopic F1-ATPase PMID: 26769832
  7. 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
  8. Mitochondrial calpain-1 disrupts ATP synthase, leading to mitochondrial reactive oxygen species generation, which promotes proinflammatory response and myocardial dysfunction during endotoxemia. PMID: 26246018
  9. 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
  10. A mutation in ATP5A1 causes a fatal neonatal mitochondrial encephalopathy. PMID: 23599390
  11. 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
  12. Homozygous mutations in this gene are the likely cause of mitochondrial disease in two sisters, with support from a yeast model. PMID: 23596069
  13. F1-ATPase at the cell surface of colonic epithelial cells has a role in mediating cell proliferation PMID: 23055519
  14. 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
  15. Antibodies to the beta- and gamma-subunits of F(1)-ATPase are further antimitochondrial antibodies in primary biliary cirrhosis. PMID: 22098431
  16. 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
  17. Data suggest that F1-ATPase catalytic site show the correlation between the phosphate binding and the tightening of the alphabeta-interface. PMID: 21481781
  18. This protein has been found differentially expressed in the anterior cingulate cortex in men patients with schizophrenia. PMID: 20381070
  19. 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
  20. 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
  21. analysis of vascular endothelial ectoadenylate kinase and plasma membrane ATP synthase PMID: 16714292
  22. Higher levels of ATP5a1 expression are associated with certain Single Nucleotide Polymorphisms and with TP53 mutation. PMID: 19261598
  23. 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
  24. This protein has been found differentially expressed in the Wernicke's Area from patients with schizophrenia. PMID: 19405953
  25. This protein has been found differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia. PMID: 19110265

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Involvement in disease Combined oxidative phosphorylation deficiency 22 (COXPD22); Mitochondrial complex V deficiency, nuclear 4 (MC5DN4)
Subcellular Location Mitochondrion inner membrane, Cell membrane, Peripheral membrane protein, Extracellular side
Protein Families ATPase alpha/beta chains family
Tissue Specificity Fetal lung, heart, liver, gut and kidney. Expressed at higher levels in the fetal brain, retina and spinal cord.
Database Links

HGNC: 823

OMIM: 164360

KEGG: hsa:498

STRING: 9606.ENSP00000282050

UniGene: Hs.298280

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