JMJD7 Protein (AA 1-316) (Strep Tag)

Catalog No. ABIN3132750

Product Details

Target: JMJD7 (Jumonji Domain Containing 7 (JMJD7))

Protein Type: Recombinant

Protein Characteristics: AA 1-316

Origin: Mouse

Source: Tobacco (Nicotiana tabacum)

Purification tag / Conjugate: This JMJD7 protein is labelled with Strep Tag.

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

Sequence: MAEAALEAVR RALQEFPAAA RDLNVPRVVP YLDEPPSPLC FYRDWVCPNR PCIIRNALQH WPALQKWSLS YLRATVGSTE VSVAVTPDGY ADAVRGDRFV MPAERRLPIS HVLDVLEGRA QHPGVLYVQK QCSNLPTELP QLLSDIESHV PWASESLGKM PDAVNFWLGD ASAVTSLHKD HYENLYCVVS GEKHFLLHPP SDRPFIPYNL YTPATYQLTE EGTFRVVDEE AMEKVPWIPL DPLAPDLTQY PSYSQAQALH CTVRAGEMLY LPALWFHHVQ QSHGCIAVNF WYDMEYDLKY SYFQLMDTLT RATGLD
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: JMJD7 (Jumonji Domain Containing 7 (JMJD7))

Alternative Name: Jmjd7 (JMJD7 Products)

Synonyms: jumonji domain containing 7 Protein, JMJD7 Protein, Jmjd7 Protein

Background: Bifunctional peptidase and (3S)-lysyl hydroxylase Jmjd7 (EC 1.14.11.63) (EC 3.4.-.-) (JmjC domain-containing protein 7) (Jumonji domain-containing protein 7) (L-lysine (3S)-hydroxylase Jmjd7),FUNCTION: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase (PubMed:28847961) (By similarity). 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 (PubMed:28847961). 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 (PubMed:28847961). Additionally, may play a role in protein biosynthesis by modifying the translation machinery. Acts as a Fe(2+) and 2-oxoglutarate-dependent monooxygenase, catalyzing (S)-stereospecific hydroxylation at C-3 of 'Lys-22' of DRG1 and 'Lys-21' of DRG2 translation factors (TRAFAC), promoting their interaction with ribonucleic acids (RNA) (By similarity). {ECO:0000250|UniProtKB:P0C870, ECO:0000269|PubMed:28847961}.

Molecular Weight: 35.9 kDa

UniProt: P0C872