- Tel: 858.663.9055
-
Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
Related Products
|
Glutamine synthetase (GLUL) is a cytoplasmic enzyme that plays a central role in cellular nitrogen metabolism and neurotransmitter homeostasis by catalyzing the ATP-dependent conversion of glutamate and ammonia into glutamine. GLUL (GLUL) is a key component of the glutamate-glutamine cycle, a pathway that is essential for maintaining excitatory neurotransmitter balance and preventing glutamate-mediated excitotoxicity in the central nervous system. This enzyme is highly enriched in astrocytes and other metabolically active support cells, where it functions at the interface of neuronal signaling and metabolic regulation. The Glutamine Synthetase Antibody / Knockdown-Validated Neuro-Metabolic Enzyme Antibody is designed to detect this critical enzyme with high specificity in both tissue-based and biochemical assays. It is part of a collection of knockdown validated antibodies that have been functionally assessed using gene silencing approaches to support target-specific detection.
Glutamine Synthetase antibody, also referred to as GLUL antibody and GS antibody, recognizes a predominantly cytoplasmic protein consistent with its enzymatic role. Immunohistochemistry analysis of formalin-fixed, paraffin-embedded human brain tissue demonstrates diffuse cytoplasmic HRP-DAB brown staining within glial cell populations, with a distribution pattern that highlights astrocytic processes extending throughout the neuropil. This staining pattern reflects the known localization of GLUL in astrocytes, where it supports synaptic function by clearing excess glutamate and converting it into glutamine for neuronal reuse. The contrast between GLUL-positive glial cells and surrounding neural elements provides a clear and biologically meaningful signal for interpreting metabolic activity within brain tissue.
Western blot analysis identifies a distinct band at approximately 40-45 kDa across human cell and tissue lysates, consistent with the expected molecular weight of glutamine synthetase. The band is sharp and reproducible, supporting reliable detection in lysate-based assays. Importantly, knockdown validation using GLUL-targeted shRNA in HeLa cells results in a clear and reproducible reduction in signal compared to wild-type controls, confirming that the detected band corresponds specifically to GLUL protein. This gene silencing-based validation provides direct functional evidence linking antibody signal to endogenous protein expression and establishes a high level of confidence in target specificity.
Functionally, GLUL plays a critical role in ammonia detoxification and amino acid metabolism, particularly in tissues with high metabolic demand such as brain and liver. In the central nervous system, astrocyte-expressed GLUL regulates extracellular glutamate levels, preventing neurotoxicity while sustaining neurotransmitter recycling. This metabolic coupling between astrocytes and neurons is essential for maintaining synaptic stability and supporting sustained neuronal activity. In IHC, this biology is reflected by strong cytoplasmic staining in astrocytes and other metabolically active cells, particularly in regions with high synaptic density.
Beyond its physiological role, GLUL expression is dynamically regulated in response to metabolic stress, hypoxia, and disease states. Altered glutamine synthetase levels have been associated with neurodegenerative conditions, liver dysfunction, and tumor metabolism, where cells adapt to changing nutrient and nitrogen availability. In cancer, GLUL can contribute to metabolic reprogramming by supporting glutamine biosynthesis, enabling cell survival under nutrient-limited conditions. Its expression pattern therefore provides insight into both normal metabolic processes and disease-associated metabolic adaptations.
The combination of characteristic astrocyte-associated cytoplasmic staining in brain tissue, consistent molecular weight detection in western blot, and functional knockdown validation makes clone GLUL/8996R a well-characterized reagent for studying metabolic enzyme function and neurotransmitter regulation. These complementary validation approaches support its use in applications requiring high specificity and reproducibility, particularly in research focused on neurobiology, cellular metabolism, and metabolic stress responses.
This antibody is part of a broader antibody panel offered by NSJ Bioreagents.
Optimal dilution of the Glutamine Synthetase Antibody / Knockdown-Validated Neuro-Metabolic Enzyme Antibody should be determined by the researcher.
A recombinant partial protein sequence (within amino acids 200-373) from the human protein was used as the immunogen for the Glutamine Synthetase antibody rabbit monoclonal GLUL/8996R.
Aliquot the Glutamine Synthetase antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
Glutamine synthetase antibody, GLUL antibody, GS antibody, glutamate ammonia ligase antibody, GLUL knockdown antibody
Your bulk quote request has been submitted successfully!
Please contact us if you have any questions.