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COX2 Protein (AA 1-227) (Strep Tag)

This Recombinant COX2 protein is produced in Cell-free protein synthesis (CFPS).
Catalog No. ABIN3132339

Quick Overview for COX2 Protein (AA 1-227) (Strep Tag) (ABIN3132339)

Target

See all COX2 Proteins
COX2 (Cytochrome C Oxidase Subunit II (COX2))

Protein Type

Recombinant

Origin

  • 4
  • 2
  • 1
  • 1
Mouse

Source

  • 3
  • 2
  • 2
  • 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 1-227

    Purification tag / Conjugate

    This COX2 protein is labelled with Strep Tag.

    Sequence

    MAYPFQLGLQ DATSPIMEEL MNFHDHTLMI VFLISSLVLY IISLMLTTKL THTSTMDAQE VETIWTILPA VILIMIALPS LRILYMMDEI NNPVLTVKTM GHQWYWSYEY TDYEDLCFDS YMIPTNDLKP GELRLLEVDN RVVLPMELPI RMLISSEDVL HSWAVPSLGL KTDAIPGRLN QATVTSNRPG LFYGQCSEIC GSNHSFMPIV LEMVPLKYFE NWSASMI
    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®).
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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.

    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

    COX2 (Cytochrome C Oxidase Subunit II (COX2))

    Alternative Name

    Mtco2

    Background

    Cytochrome c oxidase subunit 2 (EC 7.1.1.9) (Cytochrome c oxidase polypeptide II),FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00410}.

    Molecular Weight

    26.0 kDa

    UniProt

    P00405

    Pathways

    Brown Fat Cell Differentiation, Positive Regulation of fat Cell Differentiation
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