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ATP7A Protein (AA 1-1500) (Strep Tag)

Crystallography grade ATP7A Origin: Human Host: Tobacco (Nicotiana tabacum) Recombinant >80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. WB, SDS, ELISA
Catalog No. ABIN3089623
  • Target See all ATP7A Proteins
    ATP7A (ATPase, Cu++ Transporting, alpha Polypeptide (ATP7A))
    Protein Type
    Recombinant
    Protein Characteristics
    AA 1-1500
    Origin
    • 6
    • 5
    Human
    Source
    • 4
    • 4
    • 2
    • 1
    Tobacco (Nicotiana tabacum)
    Purification tag / Conjugate
    This ATP7A protein is labelled with Strep Tag.
    Application
    Western Blotting (WB), SDS-PAGE (SDS), ELISA
    Sequence
    MDPSMGVNSV TISVEGMTCN SCVWTIEQQI GKVNGVHHIK VSLEEKNATI IYDPKLQTPK TLQEAIDDMG FDAVIHNPDP LPVLTDTLFL TVTASLTLPW DHIQSTLLKT KGVTDIKIYP QKRTVAVTII PSIVNANQIK ELVPELSLDT GTLEKKSGAC EDHSMAQAGE VVLKMKVEGM TCHSCTSTIE GKIGKLQGVQ RIKVSLDNQE ATIVYQPHLI SVEEMKKQIE AMGFPAFVKK QPKYLKLGAI DVERLKNTPV KSSEGSQQRS PSYTNDSTAT FIIDGMHCKS CVSNIESTLS ALQYVSSIVV SLENRSAIVK YNASSVTPES LRKAIEAVSP GLYRVSITSE VESTSNSPSS SSLQKIPLNV VSQPLTQETV INIDGMTCNS CVQSIEGVIS KKPGVKSIRV SLANSNGTVE YDPLLTSPET LRGAIEDMGF DATLSDTNEP LVVIAQPSSE MPLLTSTNEF YTKGMTPVQD KEEGKNSSKC YIQVTGMTCA SCVANIERNL RREEGIYSIL VALMAGKAEV RYNPAVIQPP MIAEFIRELG FGATVIENAD EGDGVLELVV RGMTCASCVH KIESSLTKHR GILYCSVALA TNKAHIKYDP EIIGPRDIIH TIESLGFEAS LVKKDRSASH LDHKREIRQW RRSFLVSLFF CIPVMGLMIY MMVMDHHFAT LHHNQNMSKE EMINLHSSMF LERQILPGLS VMNLLSFLLC VPVQFFGGWY FYIQAYKALK HKTANMDVLI VLATTIAFAY SLIILLVAMY ERAKVNPITF FDTPPMLFVF IALGRWLEHI AKGKTSEALA KLISLQATEA TIVTLDSDNI LLSEEQVDVE LVQRGDIIKV VPGGKFPVDG RVIEGHSMVD ESLITGEAMP VAKKPGSTVI AGSINQNGSL LICATHVGAD TTLSQIVKLV EEAQTSKAPI QQFADKLSGY FVPFIVFVSI ATLLVWIVIG FLNFEIVETY FPGYNRSISR TETIIRFAFQ ASITVLCIAC PCSLGLATPT AVMVGTGVGA QNGILIKGGE PLEMAHKVKV VVFDKTGTIT HGTPVVNQVK VLTESNRISH HKILAIVGTA ESNSEHPLGT AITKYCKQEL DTETLGTCID FQVVPGCGIS CKVTNIEGLL HKNNWNIEDN NIKNASLVQI DASNEQSSTS SSMIIDAQIS NALNAQQYKV LIGNREWMIR NGLVINNDVN DFMTEHERKG RTAVLVAVDD ELCGLIAIAD TVKPEAELAI HILKSMGLEV VLMTGDNSKT ARSIASQVGI TKVFAEVLPS HKVAKVKQLQ EEGKRVAMVG DGINDSPALA MANVGIAIGT GTDVAIEAAD VVLIRNDLLD VVASIDLSRK TVKRIRINFV FALIYNLVGI PIAAGVFMPI GLVLQPWMGS AAMAASSVSV VLSSLFLKLY RKPTYESYEL PARSQIGQKS PSEISVHVGI DDTSRNSPKL GLLDRIVNYS RASINSLLSD KRSLNSVVTS EPDKHSLLVG DFREDDDTAL
    Sequence without tag. The proposed Strep-Tag is based on experience s with the expression system, a different complexity of the protein could make another tag necessary. In case you have a special request, please contact us.
    Characteristics
    Key Benefits:
    • Made in Germany - from design to production - by highly experienced protein experts.
    • Protein expressed with ALiCE® and purified by multi-step, protein-specific process to ensure correct folding and modification.
    • These proteins are normally active (enzymatically functional) as our customers have reported (not tested by us and not guaranteed).
    • 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.


    Expression System:
    • ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
    • During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

    Concentration:
    • 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.
    • We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.

    Purification
    Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):
    1. In a first purification step, the protein is purified from the cleared cell lysate using StrepTag capture material. 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
    >80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
    Endotoxin Level
    Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)
    Grade
    Crystallography grade
    Top Product
    Discover our top product ATP7A 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

    ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
    During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

    Restrictions
    For Research Use only
  • Format
    Liquid
    Buffer
    The buffer composition is at the discretion of the manufacturer. If you have a special request, please contact us.
    Handling Advice
    Avoid repeated freeze-thaw cycles.
    Storage
    -80 °C
    Storage Comment
    Store at -80°C.
    Expiry Date
    Unlimited (if stored properly)
  • Target
    ATP7A (ATPase, Cu++ Transporting, alpha Polypeptide (ATP7A))
    Alternative Name
    ATP7A (ATP7A Products)
    Synonyms
    ATP7A Protein, cal Protein, wu:fc43e01 Protein, zgc:153422 Protein, zgc:158633 Protein, DDBDRAFT_0218568 Protein, DDBDRAFT_0235190 Protein, DDB_0218568 Protein, DDB_0235190 Protein, atpase Protein, Atp7a Protein, kal Protein, atp7a Protein, DSMAX Protein, MK Protein, MNK Protein, SMAX3 Protein, Blo Protein, DXHXS1608e Protein, I14 Protein, Mo Protein, blotchy Protein, br Protein, brindled Protein, mottled Protein, Mnk Protein, ATPase copper transporting alpha Protein, ATPase, Cu++ transporting, alpha polypeptide Protein, P-type ATPase Protein, ATP synthase subunit a Protein, copper-transporting ATPase 1 Protein, ATP7A Protein, atp7a Protein, LOC100049514 Protein, Atp7a Protein, LOC412379 Protein
    Background
    Copper-transporting ATPase 1 (EC 7.2.2.8) (Copper pump 1) (Menkes disease-associated protein),FUNCTION: ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:10419525, PubMed:11092760, PubMed:28389643). Within a catalytic cycle, acquires Cu(+) ion from donor protein on the cytoplasmic side of the membrane and delivers it to acceptor protein on the lumenal side. The transfer of Cu(+) ion across the membrane is coupled to ATP hydrolysis and is associated with a transient phosphorylation that shifts the pump conformation from inward-facing to outward-facing state (PubMed:10419525, PubMed:19453293, PubMed:19917612, PubMed:31283225, PubMed:28389643). Under physiological conditions, at low cytosolic copper concentration, it is localized at the trans-Golgi network (TGN) where it transfers Cu(+) ions to cuproenzymes of the secretory pathway (PubMed:28389643, PubMed:11092760). Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions (PubMed:10419525, PubMed:28389643). May play a dual role in neuron function and survival by regulating cooper efflux and neuronal transmission at the synapse as well as by supplying Cu(+) ions to enzymes such as PAM, TYR and SOD3 (PubMed:28389643) (By similarity). In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (By similarity). {ECO:0000250|UniProtKB:Q64430, ECO:0000269|PubMed:10419525, ECO:0000269|PubMed:11092760, ECO:0000269|PubMed:19453293, ECO:0000269|PubMed:19917612, ECO:0000269|PubMed:28389643, ECO:0000269|PubMed:31283225}.
    Molecular Weight
    163.4 kDa
    UniProt
    Q04656
    Pathways
    Transition Metal Ion Homeostasis, Ribonucleoside Biosynthetic Process
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