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CTR9 Protein (AA 1-1173) (Strep Tag)

This Recombinant CTR9 protein is produced in Cell-free protein synthesis (CFPS).
Catalog No. ABIN3135488

Quick Overview for CTR9 Protein (AA 1-1173) (Strep Tag) (ABIN3135488)

Target

CTR9 (RNA Polymerase-Associated Protein CTR9 Homolog (CTR9))

Protein Type

Recombinant

Origin

  • 2
  • 1
Mouse

Source

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

Application

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

Purity

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

Grade

custom-made
  • Protein Characteristics

    AA 1-1173

    Purification tag / Conjugate

    This CTR9 protein is labelled with Strep Tag.

    Sequence

    MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALALE YYKQGKTEEF VKLLEAARID GNLDYRDHEK DQMTCLDTLA AYYVQQARKE KNKDNKKDLI TQATLLYTMA DKIIMYDQNH LLGRACFCLL EGDKMDQADA QFHFVLNQSP NNIPALLGKA CISFNKKDYR GALAYYKKAL RTNPGCPAEV RLGMGHCFVK LNKLEKARLA FSRALELNSK CVGALVGLAV LELNNKEADS IKNGVQLLSR AYTIDPSNPM VLNHLANHFF FKKDYSKVQH LALHAFHNTE VEAMQAESCY QLARSFHVQE DYDQAFQYYY QATQFASSSF VLPFFGLGQM YIYRGDKENA SQCFEKVLKA YPNNYETMKI LGSLYAASED QEKRDIAKGH LKKVTEQYPD DVEAWIELAQ ILEQTDIQGA LSAYGTATRI LQEKVQADVP PEILNNVGAL HFRLGNLGEA KKYFLASLDR AKAEAEHDEH YYNAISVTTS YNLARLYEAM CEFHEAEKLY KNILREHPNY VDCYLRLGAM ARDKGNFYEA SDWFKEALQI NQDHPDAWSL IGNLHLAKQE WGPGQKKFER ILKQPATQSD TYSMLALGNV WLQTLHQPTR DREKEKRHQD RALAIYKQVL RNDAKNLYAA NGIGAVLAHK GYFREARDVF AQVREATADI SDVWLNLAHI YVEQKQYISA VQMYENCLRK FYKHQNTEVV LYLARALFKC GKLQECKQTL LKARHVAPSD TVLMFNVALV LQRLATSVLK DEKSNLKEVL NAVKELELAH RYFSYLSKVG DKMRFDLALA ASEARQCSDL LSQAQYHVAR ARKQDEEERE LRAKQEQEKE LLRQKLLKEQ EEKRLREKEE QKKLLEQRAQ YVEKTKNILM FTGETEATKE KKRGGGGGRR SKKGGEFDEF VNDDTDDDLP VSKKKKRRKG SGSEQEGEEE EGGERKKKRR RRPPKGEEGS EEEETENGPK PKKRRPPRAE KKKAPKPERL PPSMKGKIKS KAIISSSDDS SDEDKLKIAD EGHPRNSNSD SDDDERPNRR ASSESDSDDN QNKSGSEAGS PRRSGRQESD EDSDSDQPSR KRRRSGSEQS DNESVQSGRS PSGASENEND SRPASPSAES DHESEQGSDN EGSGQGSGNE SEPEGSNNEA SDRGSEHGSD DSD
    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

    CTR9 (RNA Polymerase-Associated Protein CTR9 Homolog (CTR9))

    Alternative Name

    Ctr9

    Background

    RNA polymerase-associated protein CTR9 homolog (SH2 domain-binding protein 1) (Tetratricopeptide repeat-containing, SH2-binding phosphoprotein of 150 kDa) (TPR-containing, SH2-binding phosphoprotein of 150 kDa) (p150TSP),FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'Ser-2'- and 'Ser-5'-phosphorylated forms and is involved in transcriptional elongation, acting both independently and synergistically with TCEA1 and in cooperation with the DSIF complex and HTATSF1. PAF1C is required for transcription of Hox and Wnt target genes. PAF1C is involved in hematopoiesis and stimulates transcriptional activity of KMT2A/MLL1. PAF1C is involved in histone modifications such as ubiquitination of histone H2B and methylation on histone H3 'Lys-4' (H3K4me3). PAF1C recruits the RNF20/40 E3 ubiquitin-protein ligase complex and the E2 enzyme UBE2A or UBE2B to chromatin which mediate monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1), UB2A/B-mediated H2B ubiquitination is proposed to be coupled to transcription. PAF1C is involved in mRNA 3' end formation probably through association with cleavage and poly(A) factors. Required for mono- and trimethylation on histone H3 'Lys-4' (H3K4me3) and dimethylation on histone H3 'Lys-79' (H3K4me3). Required for Hox gene transcription (By similarity). Required for the trimethylation of histone H3 'Lys-4' (H3K4me3) on genes involved in stem cell pluripotency, this function is synergistic with CXXC1 indicative for an involvement of the SET1 complex. Involved in transcriptional regulation of IL6-responsive genes and in JAK-STAT pathway, may regulate DNA-association of STAT3. {ECO:0000250|UniProtKB:Q6PD62, ECO:0000269|PubMed:17911113, ECO:0000269|PubMed:19345177}.

    Molecular Weight

    133.4 kDa

    UniProt

    Q62018

    Pathways

    Cellular Response to Molecule of Bacterial Origin, Stem Cell Maintenance
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