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ATP5A1 Protein (AA 44-553) (His tag)

Crystallography grade ATP5A1 Origin: Human Host: Escherichia coli (E. coli) Recombinant >95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. ELISA, SDS, WB, Crys
Catalog No. ABIN3089681
  • Target See all ATP5A1 Proteins
    ATP5A1 (ATP Synthase, H+ Transporting, Mitochondrial F1 Complex, alpha Subunit 1, Cardiac Muscle (ATP5A1))
    Protein Type
    Recombinant
    Protein Characteristics
    AA 44-553
    Origin
    • 2
    • 1
    • 1
    Human
    Source
    • 2
    • 1
    • 1
    Escherichia coli (E. coli)
    Purification tag / Conjugate
    This ATP5A1 protein is labelled with His tag.
    Application
    ELISA, SDS-PAGE (SDS), Western Blotting (WB), Crystallization (Crys)
    Sequence
    QKTGTAEMSS ILEERILGAD TSVDLEETGR VLSIGDGIAR VHGLRNVQAE EMVEFSSGLK GMSLNLEPDN VGVVVFGNDK LIKEGDIVKR TGAIVDVPVG EELLGRVVDA LGNAIDGKGP IGSKTRRRVG LKAPGIIPRI SVREPMQTGI KAVDSLVPIG RGQRELIIGD RQTGKTSIAI DTIINQKRFN DGSDEKKKLY CIYVAIGQKR STVAQLVKRL TDADAMKYTI VVSATASDAA PLQYLAPYSG CSMGEYFRDN GKHALIIYDD LSKQAVAYRQ MSLLLRRPPG REAYPGDVFY LHSRLLERAA KMNDAFGGGS LTALPVIETQ AGDVSAYIPT NVISITDGQI FLETELFYKG IRPAINVGLS VSRVGSAAQT RAMKQVAGTM KLELAQYREV AAFAQFGSDL DAATQQLLSR GVRLTELLKQ GQYSPMAIEE QVAVIYAGVR GYLDKLEPSK ITKFENAFLS HVVSQHQALL GTIRADGKIS EQSDAKLKEI VTNFLAGFEA
    Sequence without tag. Tag location is at the discretion of the manufacturer. If you have a special request, please contact us.
    Characteristics
    • Made in Germany - from design to production - by highly experienced protein experts.
    • Human ATP5A1 Protein (raised in E. Coli) purified by multi-step, protein-specific process to ensure crystallization grade.
    • State-of-the-art algorithm used for plasmid design (Gene synthesis).

    This protein is a made to order protein and will be made for the first time for your order. Our experts in the lab will ensure that you receive a correctly folded protein.

    The big advantage of ordering our made-to-order proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.

    In the unlikely event that the protein cannot be expressed or purified we do not charge anything (other companies might charge you for any performed steps in the expression process for custom-made proteins, e.g. fees might apply for the expression plasmid, the first expression experiments or purification optimization).

    When you order this made-to-order protein you will only pay upon receival of the correctly folded protein. With no financial risk on your end you can rest assured that our experienced protein experts will do everything to make sure that you receive the protein you ordered.

    The concentration of our recombinant proteins is measured using the absorbance at 280nm. The protein's absorbance will be measured in several dilutions and is measured against its specific reference buffer.

    The concentration of the protein is calculated using its specific absorption coefficient. We use the Expasy's protparam tool to determine the absorption coefficient of each protein.

    Purification
    Two step purification of proteins expressed in bacterial culture:
    1. In a first purification step, the protein is purified from the cleared cell lysate using three different His-tag capture materials: high yield, EDTA resistant, or DTT resistant. Eluate fractions are analyzed by SDS-PAGE.
    2. Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatography. Eluate fractions are analyzed by SDS-PAGE and Western blot.
    Purity
    >95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
    Sterility
    0.22 μm filtered
    Endotoxin Level
    Endotoxin has not been removed. Please contact us if you require endotoxin removal.
    Grade
    Crystallography grade
    Top Product
    Discover our top product ATP5A1 Protein
  • Application Notes
    In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a guarantee though.
    Comment

    In cases in which it is highly likely that the recombinant protein with the default tag will be insoluble our protein lab may suggest a higher molecular weight tag (e.g. GST-tag) instead to increase solubility. We will discuss all possible options with you in detail to assure that you receive your protein of interest.

    Restrictions
    For Research Use only
  • Format
    Liquid
    Buffer
    100 mM NaCL, 20 mM Hepes, 10% glycerol. pH value is at the discretion of the manufacturer.
    Handling Advice
    Avoid repeated freeze-thaw cycles.
    Storage
    -80 °C
    Storage Comment
    Store at -80°C.
    Expiry Date
    Unlimited (if stored properly)
  • Target
    ATP5A1 (ATP Synthase, H+ Transporting, Mitochondrial F1 Complex, alpha Subunit 1, Cardiac Muscle (ATP5A1))
    Alternative Name
    ATP5A1 (ATP5A1 Products)
    Synonyms
    atp5a Protein, MGC108350 Protein, AI035633 Protein, AL022851 Protein, AL023067 Protein, Atpm Protein, D18Ertd206e Protein, Mom2 Protein, ATP5A Protein, ATP5AL2 Protein, ATPM Protein, MC5DN4 Protein, MOM2 Protein, OMR Protein, ORM Protein, hATP1 Protein, zgc:154103 Protein, ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle L homeolog Protein, ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1, cardiac muscle Protein, ATP synthase subunit alpha, mitochondrial Protein, ATP synthase, H+ transporting, mitochondrial F1 complex, alpha subunit 1 Protein, atp5a1.L Protein, ATP5A1 Protein, atp5a1 Protein, LOC100395383 Protein, Atp5a1 Protein
    Background
    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). {ECO:0000250, ECO:0000269|PubMed:10077593, ECO:0000269|PubMed:19285951}.
    Molecular Weight
    56.2 kDa Including tag.
    UniProt
    P25705
    Pathways
    Proton Transport, Ribonucleoside Biosynthetic Process
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