GATC Human
Glutamyl-TRNA Amidotransferase, Subunit C Human Recombinant
Cat. No.
BT4374
Source
Escherichia Coli.
Synonyms
Glutamyl-TRNA(Gln) Amidotransferase Subunit C, Glu-AdT
Subunit C, 15E1.2, Glutamyl-TRNA(Gln) Amidotransferase Subunit C Homolog
(Bacterial), Glutamyl-TRNA(Gln) Amidotransferase Subunit C Mitochondrial, Glutamyl-TRNA(Gln)
Amidotransferase Subunit C Homolog, EC 6.3.5, Protein 15E1.2.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
GATC Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 159 amino acids (1-136 a.a) and having a molecular mass of 17.5kDa (Molecular size on SDS-PAGE will appear higher).
GATC is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Introduction
Glutamyl-tRNA amidotransferase, subunit C, also known as GATC, is an enzyme that facilitates the conversion of misacylated Glu-tRNA(Gln) to properly charged Gln-tRNA(Gln) in the mitochondria. This process is crucial for ensuring the availability of correctly charged glutamine tRNA for protein synthesis. GATC achieves this through a transamidation reaction that requires glutamine and ATP and involves the formation of an activated gamma-phospho-Glu-tRNA(Gln) intermediate. Furthermore, GATC constitutes a subunit of the heterotrimeric GatCAB amidotransferase (AdT) complex, which comprises A (QRSL1), B (PET112), and C (GATC) subunits.
Description
This product is a recombinant human GATC protein produced in E. coli. It is a single, non-glycosylated polypeptide chain that consists of 159 amino acids, with amino acids 1-136 representing the GATC sequence. The protein has a molecular mass of 17.5 kDa. However, its apparent size on SDS-PAGE may be higher due to the presence of a 23 amino acid His-tag at the N-terminus. The protein has been purified using proprietary chromatographic techniques to ensure high purity.
Physical Appearance
The product is a clear solution that has been sterilized by filtration.
Formulation
The GATC protein is supplied at a concentration of 0.25 mg/ml in a buffer consisting of 20 mM Tris-HCl (pH 8.0), 0.15 M NaCl, 30% glycerol, and 1 mM DTT.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For long-term storage, it is recommended to store the product at -20°C. To further enhance stability during long-term storage, adding a carrier protein such as HSA or BSA to a final concentration of 0.1% is advisable. It is crucial to avoid repeated freeze-thaw cycles to prevent protein degradation.
Purity
The purity of the GATC protein is greater than 85.0%, as determined by SDS-PAGE analysis.
Synonyms
Glutamyl-TRNA(Gln) Amidotransferase Subunit C, Glu-AdT
Subunit C, 15E1.2, Glutamyl-TRNA(Gln) Amidotransferase Subunit C Homolog
(Bacterial), Glutamyl-TRNA(Gln) Amidotransferase Subunit C Mitochondrial, Glutamyl-TRNA(Gln)
Amidotransferase Subunit C Homolog, EC 6.3.5, Protein 15E1.2.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMWSRLVW LGLRAPLGGR QGFTSKADPQ GSGRITAAVI EHLERLALVD
FGSREAVARL EKAIAFADRL RAVDTDGVEP MESVLEDRCL YLRSDNVVEG NCADELLQNS HRVVEEYFVA
PPGNISLPKL DEQEPFPHS
Product Science Overview
Gene and Protein Structure
Function
The primary function of the GATC protein is to enable the formation of correctly charged Gln-tRNA (Gln) through the transamidation of misacylated Glu-tRNA (Gln) in the mitochondria . This reaction occurs in the presence of glutamine and ATP, resulting in an activated gamma-phospho-Glu-tRNA (Gln) . The proper functioning of this protein is essential for mitochondrial translation and overall cellular energy production .
Clinical Significance
Mutations in the GATC gene have been associated with combined oxidative phosphorylation deficiency 42 (COXPD42), a mitochondrial disorder . This condition is characterized by impaired mitochondrial protein synthesis and energy production, leading to various clinical manifestations . Patients with COXPD42 often exhibit symptoms such as muscle weakness, developmental delay, and other systemic issues .
Research and Applications
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