COPG Protein (AA 1-874) (Strep Tag)
Quick Overview for COPG Protein (AA 1-874) (Strep Tag) (ABIN3091937)
Target
See all COPG ProteinsProtein Type
Origin
Source
Application
Purity
Grade
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Protein Characteristics
- AA 1-874
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Purification tag / Conjugate
- This COPG protein is labelled with Strep Tag.
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Sequence
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MLKKFDKKDE ESGGGSNPFQ HLEKSAVLQE ARVFNETPIN PRKCAHILTK ILYLINQGEH LGTTEATEAF FAMTKLFQSN DPTLRRMCYL TIKEMSCIAE DVIIVTSSLT KDMTGKEDNY RGPAVRALCQ ITDSTMLQAI ERYMKQAIVD KVPSVSSSAL VSSLHLLKCS FDVVKRWVNE AQEAASSDNI MVQYHALGLL YHVRKNDRLA VNKMISKVTR HGLKSPFAYC MMIRVASKQL EEEDGSRDSP LFDFIESCLR NKHEMVVYEA ASAIVNLPGC SAKELAPAVS VLQLFCSSPK AALRYAAVRT LNKVAMKHPS AVTACNLDLE NLVTDSNRSI ATLAITTLLK TGSESSIDRL MKQISSFMSE ISDEFKVVVV QAISALCQKY PRKHAVLMNF LFTMLREEGG FEYKRAIVDC IISIIEENSE SKETGLSHLC EFIEDCEFTV LATRILHLLG QEGPKTTNPS KYIRFIYNRV VLEHEEVRAG AVSALAKFGA QNEEMLPSIL VLLKRCVMDD DNEVRDRATF YLNVLEQKQK ALNAGYILNG LTVSIPGLER ALQQYTLEPS EKPFDLKSVP LATAPMAEQR TESTPITAVK QPEKVAATRQ EIFQEQLAAV PEFRGLGPLF KSSPEPVALT ESETEYVIRC TKHTFTNHMV FQFDCTNTLN DQTLENVTVQ MEPTEAYEVL CYVPARSLPY NQPGTCYTLV ALPKEDPTAV ACTFSCMMKF TVKDCDPTTG ETDDEGYEDE YVLEDLEVTV ADHIQKVMKL NFEAAWDEVG DEFEKEETFT LSTIKTLEEA VGNIVKFLGM HPCERSDKVP DNKNTHTLLL AGVFRGGHDI LVRSRLLLLD TVTMQVTARS LEELPVDIIL ASVG
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
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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.
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Purification
- One-step Strep-tag purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®).
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Want other Options for this Protein ?
!Discover Our Catalog and Custom Protein Service Options!ProductExpression SystemConjugateOriginPriceExpression System HEK-293 CellsConjugate Myc-DYKDDDDK TagOrigin HumanPrice $956.40Your project requires further customization? Contact us and discover our custom protein solutions
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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.
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Comment
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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
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Format
- Liquid
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Buffer
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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.
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Storage
- -80 °C
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Storage Comment
- Store at -80°C.
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Expiry Date
- 12 months
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- COPG (Coatomer Protein Complex, Subunit gamma (COPG))
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Alternative Name
- COPG1
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Background
- Coatomer subunit gamma-1 (Gamma-1-coat protein) (Gamma-1-COP),FUNCTION: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins, the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis (By similarity). {ECO:0000250, ECO:0000269|PubMed:20674546}.
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Molecular Weight
- 97.7 kDa
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UniProt
- Q9Y678
Target
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