GLUL Human, His Active
Glutamine Synthetase Human Recombinant, His Active
Cat. No.
BT26235
Source
Escherichia Coli.
Synonyms
GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.
Appearance
Sterile filtered colorless 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
GLUL Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 393 amino acids (1-373 a.a.) and having a molecular mass of 44.2 kDa. The GLUL is fused to a 20 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Product Specs
Introduction
Glutamine synthetase (GLUL) is an essential enzyme that plays a crucial role in nitrogen metabolism by catalyzing the synthesis of glutamine from glutamate and ammonia. Glutamine, a product of this reaction, serves as a vital energy source and participates in various cellular processes, including cell proliferation, apoptosis inhibition, and signal transduction. GLUL expression is particularly prominent during early fetal development, highlighting its significance in embryogenesis. Moreover, GLUL contributes to maintaining acid-base balance within the body by removing ammonia from circulation, underscoring its role in detoxification. Mutations in the GLUL gene have been implicated in congenital glutamine deficiency, a disorder that underscores the critical importance of this enzyme for human health.
Description
Recombinant human GLUL, expressed in E. coli, is a purified protein with a His-tag. This non-glycosylated polypeptide consists of 393 amino acids, with a molecular weight of 44.2 kDa. The protein sequence spans residues 1-373 of the GLUL protein, with an additional 20 amino acid His-Tag fused at the N-terminus to facilitate purification using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
This solution of human GLUL is supplied in a buffer containing 20mM Tris-HCl (pH 8), 5mM DTT, 0.2M NaCl, and 20% glycerol.
Stability
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. To ensure optimal stability during long-term storage, the addition of a carrier protein such as HSA or BSA (0.1%) is advisable. Repeated freezing and thawing of the product should be avoided.
Purity
The purity of this product is determined to be greater than 90% using SDS-PAGE analysis.
Biological Activity
The specific activity of this enzyme is determined to be greater than 2,800 pmol/min/µg. This value represents the enzyme's ability to convert 1.0 pmole of L-glutamate to L-glutamine per minute at a pH of 7.5 and a temperature of 37°C. This activity is measured using a coupled assay system involving pyruvate kinase (PK) and lactate dehydrogenase (LDH).
Synonyms
GLNS, EC 6.3.1.2, EC 4.1.1.15, GLUL, Glutamine Synthetase, GS, Glutamate decarboxylase, Glutamate--ammonia ligase, PIG43, PIG59.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MTTSASSHLN KGIKQVYMSL PQGEKVQAMY IWIDGTGEGL RCKTRTLDSE PKCVEELPEW NFDGSSTLQS EGSNSDMYLV PAAMFRDPFR KDPNKLVLCE VFKYNRRPAE TNLRHTCKRI MDMVSNQHPW FGMEQEYTLM GTDGHPFGWP SNGFPGPQGP YYCGVGADRA YGRDIVEAHY RACLYAGVKI AGTNAEVMPA QWEFQIGPCE GISMGDHLWV ARFILHRVCE DFGVIATFDP KPIPGNWNGA GCHTNFSTKA MREENGLKYI EEAIEKLSKR HQYHIRAYDP KGGLDNARRL TGFHETSNIN DFSAGVANRS ASIRIPRTVG QEKKGYFEDR
RPSANCDPFS VTEALIRTCL LNETGDEPFQ YKN.
Product Science Overview
Introduction
Glutamine Synthetase (GS), also known as GLUL, is an enzyme that plays a crucial role in nitrogen metabolism by catalyzing the synthesis of glutamine from glutamate and ammonia. This enzyme is essential for various biological processes, including cell proliferation, inhibition of apoptosis, and cell signaling .
Structure and Source
The human recombinant form of Glutamine Synthetase, tagged with a His (histidine) sequence, is produced in Escherichia coli (E. coli). This recombinant protein is a single, non-glycosylated polypeptide chain containing 393 amino acids, including a 20 amino acid His-Tag at the N-terminus . The molecular mass of this recombinant protein is approximately 44.2 kDa .
Biological Function
Glutamine Synthetase is vital for maintaining cellular and systemic homeostasis. It is involved in:
- Energy Production: Glutamine, the product of the GS-catalyzed reaction, serves as a major energy source for cells .
- Cell Proliferation: It supports cell growth and division, particularly during early fetal development .
- Ammonia Detoxification: GS helps in removing excess ammonia from the body, thus maintaining body pH and preventing toxicity .
- Cell Signaling: It plays a role in various signaling pathways that regulate cellular functions .
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