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

Catalog No. ABIN3128612

Product Details

Target: JMJD5 (Jumonji Domain Containing 5 (JMJD5))

Protein Type: Recombinant

Protein Characteristics: AA 1-414

Origin: Mouse

Source: Tobacco (Nicotiana tabacum)

Purification tag / Conjugate: This JMJD5 protein is labelled with Strep Tag.

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

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 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 by multi-step, protein-specific process to ensure correct folding and modification.
• 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 will ensure that you receive a correctly folded 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 in several dilutions and is measured against its specific reference buffer.
• We use the Expasy's protparam tool to determine the absorption coefficient of each protein.

Purification: Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):

1. In a first purification step, the protein is purified from the cleared cell lysate using StrepTag capture material. Eluate fractions are analyzed by SDS-PAGE.
2. Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatography. Eluate fractions are analyzed by SDS-PAGE and Western blot.

Purity: ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.

Endotoxin Level: Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)

Grade: Crystallography grade

Application Details

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

Handling

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 Details

Target: JMJD5 (Jumonji Domain Containing 5 (JMJD5))

Alternative Name: Kdm8 (JMJD5 Products)

Synonyms: jmjd5 Protein, JMJD5 Protein, 3110005O21Rik Protein, Jmjd5 Protein, zgc:173863 Protein, zgc:91962 Protein, RGD1304823 Protein, lysine demethylase 8 Protein, jumonji domain containing 5 Protein, hypothetical protein Protein, lysine (K)-specific demethylase 8 Protein, KDM8 Protein, PTRG_02386 Protein, MCYG_00400 Protein, CC1G_13927 Protein, PGTG_16928 Protein, kdm8 Protein, Kdm8 Protein

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