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JMJD5 Protein (AA 1-414) (Strep Tag)

Recombinant JMJD5 protein expressed in Cell-free protein synthesis (CFPS).
Catalog No. ABIN3128612
starts at
$20,480.57
Plus shipping costs $50.00, if applicable $20.00 dry ice
250 μg
Shipping to: United States
Delivery in 55 to 67 Business Days

Quick Overview for JMJD5 Protein (AA 1-414) (Strep Tag) (ABIN3128612)

Target

See all JMJD5 Proteins
JMJD5 (Jumonji Domain Containing 5 (JMJD5))

Protein Type

Recombinant

Origin

  • 5
  • 1
  • 1
  • 1
  • 1
  • 1
  • 1
Mouse

Source

  • 5
  • 4
  • 1
  • 1
Cell-free protein synthesis (CFPS)

Application

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

Purity

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

Grade

custom-made
  • Protein Characteristics

    AA 1-414

    Purification tag / Conjugate

    This JMJD5 protein is labelled with Strep Tag.

    Sequence

    MSEDTTEPLV GSSTLWKELR TLLPDKEEEL KLDLGEKVDR SVAALLRQAV GLFYAGHWQG CLQASEAVLD YSWEKLNTGP WRDVDKEWRR VYSFGCLLKA LCLCQAPQKA TTVVEALRVC DMGLLMGAAI LEDILLKVVA VLQTHQLPGK QPARGPHQDQ PATKKAKCDA SPAPDVMLER MVPRLRCPPL QYFKQHFLVP GRPVILEGVA DHWPCMKKWS LQYIQEIAGC RTVPVEVGSR YTDEDWSQTL MTVDEFIQKF ILSEAKDVGY LAQHQLFDQI PELKRDISIP DYCCLGNGEE EEITINAWFG PQGTISPLHQ DPQQNFLVQV LGRKYIRLYS PQESEAVYPH ETHILHNTSQ VDVENPDLEK FPKFTEAPFL SCILSPGDTL FIPAKYWHYV RSLDLSFSVS FWWS
    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

    JMJD5 (Jumonji Domain Containing 5 (JMJD5))

    Alternative Name

    Kdm8

    Background

    Bifunctional peptidase and arginyl-hydroxylase JMJD5 (EC 1.14.11.73) (EC 3.4.-.-) (JmjC domain-containing protein 5) (Jumonji C domain-containing protein 5) (L-arginine (3R)-hydroxylase KDM8) (Lysine-specific demethylase 8),FUNCTION: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Upon DNA damage, cleaves the N-terminal tail of histone H3 at monomethylated lysine residues, preferably at monomethylated 'Lys-9' (H3K9me1). The histone variant H3F3A is the major target for cleavage. Additionally, acts as a Fe(2+) and 2-oxoglutarate-dependent monooxygenase, catalyzing (R)-stereospecific hydroxylation at C-3 of 'Arg-137' of RPS6 and 'Arg-141' of RCCD1, but the biological significance of this activity remains to be established. Regulates mitosis through different mechanisms: Plays a role in transcriptional repression of satellite repeats, possibly by regulating H3K36 methylation levels in centromeric regions together with RCCD1. Possibly together with RCCD1, is involved in proper mitotic spindle organization and chromosome segregation. Negatively regulates cell cycle repressor CDKN1A/p21, which controls G1/S phase transition. Required for G2/M phase cell cycle progression. Regulates expression of CCNA1/cyclin-A1, leading to cancer cell proliferation. Also, plays a role in regulating alpha-tubulin acetylation and cytoskeletal microtubule stability involved in epithelial to mesenchymal transition (By similarity). Regulates the circadian gene expression in the liver (PubMed:30500822). Represses the transcriptional activator activity of the CLOCK-BMAL1 heterodimer in a catalytically-independent manner (By similarity). Negatively regulates the protein stability and function of CRY1, required for AMPK-FBXL3-induced CRY1 degradation (PubMed:30500822). {ECO:0000250|UniProtKB:Q8N371, ECO:0000269|PubMed:30500822}.

    Molecular Weight

    47.1 kDa

    UniProt

    Q9CXT6

    Pathways

    Chromatin Binding
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