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

Catalog No. ABIN3114338

This Recombinant ATP7A protein is produced in Cell-free protein synthesis (CFPS).

Quick Overview for ATP7A Protein (AA 1-1500) (Strep Tag) (ABIN3114338)

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

Protein Type: Recombinant

Origin: Human

Source: 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

Product Details

Protein Characteristics: AA 1-1500

Purification tag / Conjugate: This ATP7A protein is labelled with Strep Tag.

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 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®).

Application Details

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

Handling

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 Details

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),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