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TRIM10 Protein (AA 1-489) (Strep Tag)

TRIM10 Origin: Mouse Host: Tobacco (Nicotiana tabacum) Recombinant > 80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC). ELISA, WB, SDS
Catalog No. ABIN3120069
  • Target See all TRIM10 Proteins
    TRIM10 (Tripartite Motif Containing 10 (TRIM10))
    Protein Type
    Recombinant
    Protein Characteristics
    AA 1-489
    Origin
    • 4
    • 1
    • 1
    • 1
    Mouse
    Source
    • 3
    • 2
    • 1
    • 1
    Tobacco (Nicotiana tabacum)
    Purification tag / Conjugate
    This TRIM10 protein is labelled with Strep Tag.
    Application
    ELISA, Western Blotting (WB), SDS-PAGE (SDS)
    Sequence
    MASAPSVTSL ADEVNCPICQ GTLREPVTID CGHNFCRGCL TRYCEIPGPE SEESLSCPLC KEPFRPGSFR PNWQLANVVE NIERLQLAST RGLEVEDACP EHGEKIYFFC EEDEAQLCVV CRETGQHGAH TVRFLEDAAG PYREQIQKCL VCLRKEREEI QETQSRENKR IQVLLTQVAT KRQQVISQFA HLSQFLQQQQ TALLAQLEGL DGDILKQQEE FDSLATGEIC RFSTLIEELE EKNKRTARGL LTDIRSTLIR CETRKCRKPE AISPELGQRI RDFPQQAIPL RQEMKTFLEK LCFELDYEPA HISLDPQTSH PKLLLSEDHR RARFSYKWQN SPDTPQRFDR VTCVLAQCGF TGGRHTWMVN VDLAHGGSCT VGVVREDVRR KGELRLRPEE GIWAVRLAWG FVSALGSFPT RLALEEQPRK VQVSLDYEVG WITFVNAVTQ EHIYTFTASF TQKIFPLFGL WGRGSSFSLS CQEGAVSLL
    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 in one-step affinity chromatography
    • 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 try to ensure that you receive soluble 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 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®).
    Purity
    > 80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).
    Top Product
    Discover our top product TRIM10 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
    TRIM10 (Tripartite Motif Containing 10 (TRIM10))
    Alternative Name
    Trim10 (TRIM10 Products)
    Synonyms
    TRIM10 Protein, HERF1 Protein, RFB30 Protein, RNF9 Protein, rfb30 Protein, 3.8-1.2 Protein, AI324236 Protein, BB139825 Protein, Herf1 Protein, Rnf9 Protein, Rfb30 Protein, tripartite motif containing 10 Protein, tripartite motif-containing protein 10 Protein, tripartite motif-containing 10 Protein, TRIM10 Protein, LOC100481044 Protein, Trim10 Protein
    Background
    Tripartite motif-containing protein 10 (Hematopoietic RING finger 1) (RING finger protein 9),FUNCTION: E3 ligase that plays an essential role in the differentiation and survival of terminal erythroid cells (PubMed:18560381). May directly bind to PTEN and promote its ubiquitination, resulting in its proteasomal degradation and activation of hypertrophic signaling (PubMed:32343488). In addition, plays a role in immune response regulation by repressing the phosphorylation of STAT1 and STAT2 in the interferon/JAK/STAT signaling pathway independent of its E3 ligase activity. Mechanistically, interacts with the intracellular domain of IFNAR1 and thereby inhibits the association between TYK2 and IFNAR1 (By similarity). {ECO:0000250|UniProtKB:Q9UDY6, ECO:0000269|PubMed:18560381, ECO:0000269|PubMed:32343488}.
    Molecular Weight
    55.6 kDa
    UniProt
    Q9WUH5
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