protein

DENR Protein, Human (His-SUMO)

HY-P72172

5 μg;10 μg;50 μg

158;269;753 USD

DENR Protein, Human (His-SUMO)

proteins

E. coli

5 μg;10 μg;50 μg

158;269;753 USD

DENR proteins play a key role in the translation process, participating in mRNA scanning and start codon recognition. It crucially promotes the recruitment of aminoacylated initiator tRNA to the 40S ribosomal P site during translation initiation. DENR Protein, Human (His-SUMO) is the recombinant human-derived DENR protein, expressed by E. coli , with N-6*His, N-SUMO labeled tag. The total length of DENR Protein, Human (His-SUMO) is 197 a.a., with molecular weight (affected by relative charge) of ~46 KDa.

Human

The DENR protein emerges as a key player in translation processes, potentially involved in the translation of target mRNAs through scanning and recognition of the initiation codon. It plays a pivotal role in translation initiation by promoting the recruitment of aminoacylated initiator tRNA to the P site of 40S ribosomes. Additionally, DENR is implicated in facilitating the release of deacylated tRNA and mRNA from recycled 40S subunits following ABCE1-mediated dissociation of post-termination ribosomal complexes into subunits. Notably, DENR contributes to the modulation of the translational profile of a subset of cancer-related mRNAs when recruited to the translational initiation complex by the oncogene MCTS1, highlighting its potential involvement in cancer-associated translational regulation. Its interaction with MCTS1 further underscores its significance in intricate cellular processes related to translation initiation and control.

denr; DENR_HUMAN; Density regulated protein; Density-regulated protein; DRP; DRP1; DRP1 protein; Protein DRP1; SMAP-3; SMAP3; Smooth muscle cell associated protein 3; Smooth muscle cell-associated protein 3

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm sterile filtered 20 mM Tris-HCl, 0.5 M NaC, 6% Trehalose, pH 8.0.

Room temperature in continental US;may vary elsewhere.