Name: Recombinant Human ATP synthase subunit alpha, mitochondrial (ATP5F1A)
Brand: CUSABIO
SKU: CSB-EP002344HU

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

59.2kDa

Protein Length

Full Length of Mature Protein

Tag Info

N-terminal 6xHis-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/-80°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

3-7 business days

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.

Description

This Recombinant Human ATP5F1A protein was made through genetic engineering. By putting the ATP5F1A gene into the genetic material of E.coli cell, the E.coli could be used as factories or producers to make the desired ATP5F1A protein for research uses. The expression region of this protein is at 44-553aa. N-terminal 6xHis tag was used in the expression process. The purity is 90%+ determined by SDS-PAGE.

ATP synthase F1 subunit alpha (ATP5F1A), a complex V protein, was the most frequently affected subunit, in 10% of tumors and 11% of benign prostate tissues (but not both tissues in any single patient). A possible role of complex V in prostate cancer development is suggested by the significant positive correlation of ATP5F1A levels with earlier-onset prostate cancer. Besides, researchers found that a novel correlation between ATP5A1 gene expression and progression of human clear cell renal cell carcinoma by co‑expression analysis. Additionally, ATP5A1 participates in transcriptional and posttranscriptional regulation of cancer-associated genes by modulating their expression and alternative splicing profiles in hela cells.

Customer Reviews and Q&A

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■ Q&A

I want to know if the protein, Catalog # CSB-EP002344HU is also available without tag? Or is it possible to reliably remove the tag?
If available without tag, can you please provide pricing information?

Thanks for your inquiry. Generally we provide two kinds of tags for this protein. The details are as follows.
Code: CSB-EP002344HU
Name: Recombinant Human ATP synthase subunit alpha, mitochondrial(ATP5A1)
Expression Region: 44-553aa, Full Length of Mature Protein
Tag Info: N-terminal 6xHis-tag
Code: CSB-EP002344HUa2
Name: Recombinant Human ATP synthase subunit alpha, mitochondrial(ATP5A1)
Expression Region: 44-553aa, Full Length of Mature Protein
Tag Info: N-terminal 6xHis-SUMO-tag
We could try to remove the tag but can't guarantee 100% success. However, based on our annual analysis data of tag removal, the success rate reaches 75%-86%.
If we succed in removing the tag, we will charge you for protein production cost + tag removal cost.
If we fail in removing the tag, we will send you the tagged protein and will only charge you for protein production cost.

Target Background

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.

Gene References into Functions

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
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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Involvement in disease

Combined oxidative phosphorylation deficiency 22 (COXPD22); Mitochondrial complex V deficiency, nuclear 4 (MC5DN4)

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

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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