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ATP7A Protein (AA 1-1491) (Strep Tag)

This Recombinant ATP7A protein is expressed in Cell-free protein synthesis (CFPS).
Catalog No. ABIN3135596

Quick Overview for ATP7A Protein (AA 1-1491) (Strep Tag) (ABIN3135596)

Target

See all ATP7A Proteins
ATP7A (ATPase, Cu++ Transporting, alpha Polypeptide (ATP7A))

Protein Type

Recombinant

Origin

  • 4
  • 2
Mouse

Source

  • 2
  • 2
  • 1
  • 1
Cell-free protein synthesis (CFPS)

Application

Western Blotting (WB), SDS-PAGE (SDS), ELISA

Purity

approximately 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).

Grade

custom-made
  • Protein Characteristics

    AA 1-1491

    Purification tag / Conjugate

    This ATP7A protein is labelled with Strep Tag.

    Sequence

    MEPSVDANSI TITVEGMTCI SCVRTIEQQI GKVNGVHHIK VSLEEKSATI IYDPKLQTPK TLQEAIDDMG FDALLHNANP LPVLTNTVFL TVTAPLTLPW DHIQSTLLKT KGVTGVKISP QQRSAVVTII PSVVSASQIV ELVPDLSLDM GTQEKKSGAC EEHSTPQAGE VMLKMKVEGM TCHSCTSTIE GKVGKLQGVQ RIKVSLDNQE ATIVFQPHLI TAEEIKKQIE AVGFPAFIKK QPKYLKLGAI DVERLKNTPV KSSEGSQQKS PSYPSDSTTM FTIEGMHCKS CVSNIESALS TLQYVSSIVV SLENRSAIVK YNASLVTPEM LRKAIEAISP GQYRVSIASE VESTASSPSS SSLQKMPLNI VSQPLTQEAV ININGMTCNS CVQSIEGVIS KKPGVKSIHV SLANSTGTIE FDPLLTSPET LREAIEDMGF DAALPDMKEP LVVIAQPSLE TPLLPSSNEL ENVMTSVQNK CYIQVSGMTC ASCVANIERN LRREEGIYSV LVALMAGKAE VRYNPAVIQP RVIAEFIREL GFGAMVMENA GEGNGILELV VRGMTCASCV HKIESTLTKH KGIFYCSVAL ATNKAHIKYD PEIIGPRDII HTIGSLGFEA SLVKKDRSAN HLDHKREIKQ WRGSFLVSLF FCIPVMGLMV YMMVMDHHLA TLHHNQNMSN EEMINMHSAM FLERQILPGL SIMNLLSLLL CLPVQFCGGW YFYIQAYKAL KHKTANMDVL IVLATTIAFA YSLVILLVAM FERAKVNPIT FFDTPPMLFV FIALGRWLEH IAKGKTSEAL AKLISLQATE ATIVTLNSEN LLLSEEQVDV ELVQRGDIIK VVPGGKFPVD GRVIEGHSMV DESLITGEAM PVAKKPGSTV IAGSINQNGS LLIRATHVGA DTTLSQIVKL VEEAQTSKAP IQQFADKLSG YFVPFIVLVS IVTLLVWIII GFQNFEIVET YFPGYNRSIS RTETIIRFAF QASITVLCIA CPCSLGLATP TAVMVGTGVG AQNGILIKGG EPLEMAHKVK VVVFDKTGTI THGTPVVNQV KVLVESNKIS RNKILAIVGT AESNSEHPLG AAVTKYCKKE LDTETLGTCT DFQVVPGCGI SCKVTNIEGL LHKSNLKIEE NNIKNASLVQ IDAINEQSST SSSMIIDAHL SNAVNTQQYK VLIGNREWMI RNGLVISNDV DESMIEHERR GRTAVLVTID DELCGLIAIA DTVKPEAELA VHILKSMGLE VVLMTGDNSK TARSIASQVG ITKVFAEVLP SHKVAKVKQL QEEGKRVAMV GDGINDSPAL AMANVGIAIG TGTDVAIEAA DVVLIRNDLL DVVASIDLSR KTVKRIRINF VFALIYNLVG IPIAAGVFLP IGLVLQPWMG SAAMAASSVS VVLSSLFLKL YRKPTYDNYE LHPRSHTGQR SPSEISVHVG IDDTSRNSPR LGLLDRIVNY SRASINSLLS DKRSLNSVVT SEPDKHSLLV GDFREDDDTT L
    Sequence without tag. The proposed Strep-Tag is based on experience with the expression system. Our team may suggest an additional tag depending on the complexity of the protein. If 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 in one-step affinity chromatography
    • State-of-the-art algorithm used for plasmid design (Gene synthesis).

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

    The big advantage of ordering our predefined custom 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 against its specific reference buffer.
    • We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.

    Purification

    One-step Strep-tag purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®).
  • Want other Options for this Protein ?

    !
    Discover Our Catalog and Custom Protein Service Options!
    Product
    Expression System
    Conjugate
    Origin
    Price
    Expression System Escherichia coli (E. coli)
    Conjugate His tag
    Origin Mouse
    Price $673.68

    Your project requires further customization? Contact us and discover our custom protein solutions

  • 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.
    Standard Storage Buffer: PBS pH 7.4, 10 % Glycerol Might differ depending on protein.

    Handling Advice

    Avoid repeated freeze-thaw cycles.

    Storage

    -80 °C

    Storage Comment

    Store at -80°C.

    Expiry Date

    12 months
  • Target

    ATP7A (ATPase, Cu++ Transporting, alpha Polypeptide (ATP7A))

    Alternative Name

    Atp7a

    Background

    Copper-transporting ATPase 1 (EC 7.2.2.8) (Copper pump 1) (Menkes disease-associated protein homolog),FUNCTION: ATP-driven copper (Cu(+)) ion pump that plays an important role in intracellular copper ion homeostasis (PubMed:25639447, PubMed:27337370, PubMed:18650808). 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 (By similarity). 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:27337370, PubMed:18650808, PubMed:16371425, PubMed:12488345). Upon elevated cytosolic copper concentrations, it relocalizes to the plasma membrane where it is responsible for the export of excess Cu(+) ions (By similarity). 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:25639447, PubMed:15634787, PubMed:16371425, PubMed:12488345). In the melanosomes of pigmented cells, provides copper cofactor to TYR to form an active TYR holoenzyme for melanin biosynthesis (PubMed:18650808). {ECO:0000250|UniProtKB:Q04656}.

    Molecular Weight

    162.0 kDa

    UniProt

    Q64430

    Pathways

    Transition Metal Ion Homeostasis, Ribonucleoside Biosynthetic Process
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