GLSA1 E.Coli
Glutaminase 1 E.Coli Recombinant
Cat. No.
BT24457
Source
Escherichia Coli.
Synonyms
Glutaminase 1, ybaS.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% 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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In Stock 
Description
GLSA1 E.Coli Recombinant fused with a 20 amino acid His tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 330 amino acids (1-310a.a.) and having a molecular mass of 35.0kDa.
The GLSA1 is purified by proprietary chromatographic techniques.
The GLSA1 is purified by proprietary chromatographic techniques.
Product Specs
Introduction
GlsA1, a member of the serine-dependent beta-lactamases and penicillin-binding proteins superfamily found in nearly all bacteria and eukaryotes, catalyzes the hydrolytic deamidation of l-glutamine to l-glutamate and free ammonia (NH₄⁺).
Description
Recombinant E. coli GLSA1, expressed in E. coli and fused with a 20 amino acid His tag at the N-terminus, is a single, non-glycosylated polypeptide chain. It consists of 330 amino acids (1-310 a.a.) and has a molecular weight of 35.0 kDa. GLSA1 is purified using proprietary chromatographic techniques.
Physical Appearance
Sterile, colorless, and filtered solution.
Formulation
The GLSA1 solution (1 mg/ml) is supplied in a buffer containing 20 mM Tris-HCl (pH 8.0), 0.1 M NaCl, 1 mM DTT, and 10% glycerol.
Stability
For short-term storage (2-4 weeks), store at 4°C. For long-term storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for extended storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is greater than 95.0% as determined by SDS-PAGE analysis.
Synonyms
Glutaminase 1, ybaS.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MLDANKLQQA VDQAYTQFHS LNGGQNADYI PFLANVPGQL AAVAIVTCDG NVYSAGDSDY RFALESISKV CTLALALEDV GPQAVQDKIG ADPTGLPFNS VIALELHGGK PLSPLVNAGA IATTSLINAE NVEQRWQRIL HIQQQLAGEQ VALSDEVNQS EQTTNFHNRA IAWLLYSAGY LYCDAMEACD VYTRQCSTLL NTIELATLGA TLAAGGVNPL THKRVLQADN VPYILAEMMM EGLYGRSGDW AYRVGLPGKS GVGGGILAVV PGVMGIAAFS PPLDEDGNSV RGQKMVASVA KQLGYNVFKG
Product Science Overview
Structure and Function
Glutaminase 1 is a member of the glutaminase family of enzymes, which are characterized by their ability to hydrolyze the amide bond in glutamine. The enzyme is typically found in the mitochondria of cells, where it participates in the conversion of glutamine to glutamate, a key step in the production of energy and the synthesis of other important biomolecules.
The recombinant form of Glutaminase 1 from Escherichia coli (E. coli) is produced using genetic engineering techniques. This involves inserting the gene encoding Glutaminase 1 into a plasmid vector, which is then introduced into E. coli cells. The bacteria are cultured under conditions that promote the expression of the enzyme, which is subsequently purified for use in various applications.
Applications
Recombinant Glutaminase 1 has several important applications in research and industry:
- Biochemical Research: The enzyme is used to study the metabolic pathways involving glutamine and glutamate. It is also used to investigate the role of glutaminase in various diseases, including cancer and neurological disorders.
- Industrial Production: Glutaminase 1 is used in the production of flavor enhancers, such as monosodium glutamate (MSG), which is widely used in the food industry.
- Medical Applications: The enzyme is being explored as a potential therapeutic target for the treatment of cancer, as many tumor cells rely on glutamine metabolism for growth and survival.
Production and Purification
The production of recombinant Glutaminase 1 involves several steps:
- Gene Cloning: The gene encoding Glutaminase 1 is cloned into a plasmid vector, which is then introduced into E. coli cells.
- Expression: The bacteria are cultured under conditions that induce the expression of the enzyme. This typically involves the use of an inducible promoter, such as the lac promoter, which can be activated by the addition of a specific inducer, such as isopropyl β-D-1-thiogalactopyranoside (IPTG).
- Purification: The enzyme is purified from the bacterial cells using techniques such as affinity chromatography, which allows for the isolation of the enzyme based on its specific binding properties.
Challenges and Future Directions
While the production of recombinant Glutaminase 1 has been successful, there are still several challenges that need to be addressed:
- Yield and Activity: Optimizing the yield and activity of the enzyme is crucial for its use in various applications. This involves fine-tuning the expression conditions and purification methods to maximize the production of active enzyme.
- Stability: Ensuring the stability of the enzyme during storage and use is important for its practical applications. This may involve the use of stabilizing agents or modifications to the enzyme to enhance its stability.
- Therapeutic Potential: Further research is needed to fully understand the therapeutic potential of Glutaminase 1 in the treatment of diseases such as cancer. This includes investigating the enzyme’s role in tumor metabolism and developing strategies to target it effectively.
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