JMJD7 Human

Jumonji Domain Containing 7 Human Recombinant

Cat. No.

BT17353

Source

Escherichia Coli.

Synonyms

Jumonji Domain Containing 7, Jumonji Domain-Containing Protein 7, JmjC Domain-Containing Protein 7.

Appearance

Sterile Filtered clear solution.

Purity

Greater than 90.0% as determined by SDS-PAGE.

Usage

THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.

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Description

JMJD7 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 339 amino acids (1-316 a.a) and having a molecular mass of 38.3kDa.

JMJD7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction

JmjC domain-containing protein 7, also known as JMJD7, belongs to the JMJD family. This family comprises proteins containing a conserved JmjC domain, a structural motif found within the cupin metalloenzyme superfamily. Initially thought to be an alternatively spliced variant of PLA2G4B, JMJD7 is actually a distinct gene located upstream of PLA2G4B. Interestingly, most tissues express transcripts that extend from the JMJD7 gene into the downstream PLA2G4B gene. This transcriptional read-through can lead to the production of fusion proteins containing the N-terminal portion of JMJD7 linked to the PLA2G4B protein.

Description

Recombinant human JMJD7, expressed in E. coli, is a non-glycosylated polypeptide chain. This single chain protein consists of 339 amino acids, with a truncated sequence spanning residues 1 to 316. It has a molecular weight of 38.3 kDa. The recombinant protein is further engineered to include a 23 amino acid His-tag at its N-terminus, facilitating purification using proprietary chromatographic techniques.

Physical Appearance

The product is a clear solution that has been sterilized by filtration.

Formulation

The provided JMJD7 protein solution has a concentration of 1 mg/ml. It is formulated in a buffer consisting of 20mM Tris-HCl (pH 8.0), 10% glycerol, and 0.1M NaCl.

Stability

For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the product at -20°C. To ensure optimal stability during long-term storage, the addition of a carrier protein like HSA or BSA (0.1%) is advisable. Repeated freezing and thawing of the product should be avoided.

Purity

Analysis by SDS-PAGE indicates a purity greater than 90%.

Synonyms

Jumonji Domain Containing 7, Jumonji Domain-Containing Protein 7, JmjC Domain-Containing Protein 7.

Source

Escherichia Coli.

Amino Acid Sequence

MGSSHHHHHH SSGLVPRGSH MGSMAEAALE AVRSELREFP AAARELCVPL AVPYLDKPPT PLHFYRDWVC PNRPCIIRNA LQHWPALQKW SLPYFRATVG STEVSVAVTP DGYADAVRGD RFMMPAERRL PLSFVLDVLE GRAQHPGVLY VQKQCSNLPS ELPQLLPDLE SHVPWASEAL GKMPDAVNFW LGEAAAVTSL HKDHYENLYC VVSGEKHFLF HPPSDRPFIP YELYTPATYQ LTEEGTFKVV DEEAMEKVPW IPLDPLAPDL ARYPSYSQAQ ALRCTVRAGE MLYLPALWFH HVQQSQGCIA VNFWYDMEYD LKYSYFQLLD SLTKASGLD

Product Science Overview

Introduction

Jumonji Domain Containing 7 (JMJD7) is a protein-coding gene that belongs to the Jumonji family of proteins. These proteins are characterized by the presence of a Jumonji C (JmjC) domain, which is part of the cupin metalloenzyme superfamily. The JmjC domain is known for its role in catalyzing various biochemical reactions, including histone demethylation and hydroxylation. JMJD7 is highly conserved across species, indicating its crucial role in cellular processes.

Structure and Function

JMJD7 is a bifunctional enzyme that acts both as an endopeptidase and a 2-oxoglutarate-dependent monooxygenase. As an endopeptidase, it cleaves histone N-terminal tails at the carboxyl side of methylated arginine or lysine residues, generating ‘tailless nucleosomes’ which may trigger transcription elongation. It preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3, and H4. Additionally, JMJD7 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, promoting their interaction with ribonucleic acids (RNA).

Biological Significance

The biological significance of JMJD7 extends beyond its enzymatic activities. It plays a role in protein biosynthesis by modifying the translation machinery. The deregulation of JMJD7 has been associated with various diseases, including myasthenic syndrome, congenital, 4B, fast-channel. Moreover, the Jumonji family of proteins, including JMJD7, has been implicated in the regulation of gene expression through histone post-translational modifications (PTMs). These modifications are crucial for the regulation of chromatin structure and function, influencing processes such as transcription, DNA repair, and replication.

Research and Clinical Implications

Research on JMJD7 and other Jumonji family proteins has gained significant attention due to their roles in epigenetic regulation and disease. The deregulation of Jumonji proteins has been linked to various cancers, including colon, prostate, hematological, and breast cancers. Understanding the mechanisms underlying JMJD7’s function and its role in disease can provide insights into potential therapeutic targets for cancer and other diseases associated with epigenetic deregulation.

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JMJD7 Human

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