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ATP5B Protein (AA 48-529) (His tag)

Crystallography grade ATP5B Origin: Human Host: Escherichia coli (E. coli) Recombinant >95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. WB, SDS, ELISA, Crys
Catalog No. ABIN3089631
  • Target See all ATP5B Proteins
    ATP5B (ATP Synthase, H+ Transporting, Mitochondrial F1 Complex, beta Polypeptide (ATP5B))
    Protein Type
    Recombinant
    Protein Characteristics
    AA 48-529
    Origin
    • 2
    • 1
    • 1
    • 1
    • 1
    Human
    Source
    • 3
    • 2
    • 1
    Escherichia coli (E. coli)
    Purification tag / Conjugate
    This ATP5B protein is labelled with His tag.
    Application
    Western Blotting (WB), SDS-PAGE (SDS), ELISA, Crystallization (Crys)
    Sequence
    AQTSPSPKAG AATGRIVAVI GAVVDVQFDE GLPPILNALE VQGRETRLVL EVAQHLGEST VRTIAMDGTE GLVRGQKVLD SGAPIKIPVG PETLGRIMNV IGEPIDERGP IKTKQFAPIH AEAPEFMEMS VEQEILVTGI KVVDLLAPYA KGGKIGLFGG AGVGKTVLIM ELINNVAKAH GGYSVFAGVG ERTREGNDLY HEMIESGVIN LKDATSKVAL VYGQMNEPPG ARARVALTGL TVAEYFRDQE GQDVLLFIDN IFRFTQAGSE VSALLGRIPS AVGYQPTLAT DMGTMQERIT TTKKGSITSV QAIYVPADDL TDPAPATTFA HLDATTVLSR AIAELGIYPA VDPLDSTSRI MDPNIVGSEH YDVARGVQKI LQDYKSLQDI IAILGMDELS EEDKLTVSRA RKIQRFLSQP FQVAEVFTGH MGKLVPLKET IKGFQQILAG EYDHLPEQAF YMVGPIEEAV AKADKLAEEH SS
    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 ATP5B 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 ATP5B 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
    ATP5B (ATP Synthase, H+ Transporting, Mitochondrial F1 Complex, beta Polypeptide (ATP5B))
    Alternative Name
    ATP5B (ATP5B Products)
    Synonyms
    atpmb Protein, atpsb Protein, Atpsyn-beta Protein, hm:zehn0534 Protein, im:6793121 Protein, wu:fj38d01 Protein, zgc:111961 Protein, ATPMB Protein, ATPSB Protein, ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide Protein, ATP synthase subunit beta, mitochondrial Protein, ATP synthase, H+ transporting mitochondrial F1 complex, beta subunit Protein, ATP synthase, H+ transporting, mitochondrial F1 complex, beta polypeptide S homeolog Protein, ATP5B Protein, atp5b Protein, Atp5b Protein, LOC100401662 Protein, LOC100635763 Protein, atp5b.S 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.
    Molecular Weight
    52.7 kDa Including tag.
    UniProt
    P06576
    Pathways
    Proton Transport, Ribonucleoside Biosynthetic Process
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