Anti-Glutamine Synthetase (GLUL) Polyclonal Antibody for WB, IHC-P, IF/ICC, ELISA - P15104

Core Product Specifications and Parameters

Biological Background: Glutamine Synthetase (GLUL) Function and Localization

• Glutamine synthetase (GS), also known as glutamate-ammonia ligase or palmitoyltransferase GLUL (aliases: GS, GLNS, PIG43, PIG59), is a key enzyme in nitrogen metabolism that catalyzes the ATP-dependent conversion of glutamate and ammonia into glutamine (PubMed:16267323, PubMed:30158707, PubMed:36289327). Related references: PMID:16267323 PMID:30158707 PMID:36289327
• In the brain, GLUL plays a critical role in detoxifying ammonia and converting neurotoxic glutamate to inert glutamine, while in the liver, it participates in systemic ammonia clearance (By similarity).
• The enzyme is essential for proliferation of fetal skin fibroblasts (PubMed:18662667) and contributes to ribosomal 40S subunit biogenesis (PubMed:26711351). Related references: PMID:18662667 PMID:26711351
• GLUL exhibits non-canonical functions: it acts as a palmitoyltransferase for the GTPase RHOJ, facilitating its membrane localization and activation, which is required for endothelial cell migration and angiogenesis (PubMed:30158707). Related references: PMID:30158707
• Through interaction with BEST2, GLUL modulates BEST2 channel activity: it inhibits channel gating in the absence of intracellular L-glutamate but sensitizes BEST2 to glutamate, which promotes channel opening (PubMed:36289327). Related references: PMID:36289327
• The enzyme localizes to multiple subcellular compartments including the cytosol, microsomes, mitochondria, and cell membrane (UniProt).
• GLUL is expressed in endothelial cells and is regulated by acetylation, phosphorylation, and ubiquitination; it binds ATP, magnesium, and manganese as cofactors (UniProt).
• During erythropoiesis, GLUL detoxifies ammonium generated by porphobilinogen deaminase during heme biosynthesis, preventing oxidative stress (By similarity).

Experimental Guidance and Technical Tips

• Given the recombinant immunogen spanning nearly full-length GLUL, the polyclonal antibody is expected to detect both native and denatured protein across multiple applications.
• For Western blot (WB), anticipate a single band at approximately 42 kDa; consider using a positive control lysate from human, mouse, or rat liver or brain tissue.
• In immunohistochemistry (IHC-P), optimize antigen retrieval conditions and validate with appropriate tissue controls (e.g., human liver sections) due to variable protein abundance across sample types.
• For immunofluorescence (IF/ICC), co-localization studies with markers for cytosol, mitochondria, or cell membrane may be informative given the enzyme's diverse subcellular localization.
• As a polyclonal reagent, lot-to-lot consistency may vary; perform internal validation with known positive and negative cell lines to confirm specificity.

CamelBio: Your One-Stop Sourcing Bridge

CamelBio provides diagnostic manufacturers, labs, and research institutes with one-stop access to IVD raw materials, technical services, and consulting—covering every stage from concept to clinic. Our anti-GLUL polyclonal antibody supports research into glutamine metabolism, ammonia detoxification, and angiogenesis. Complement this with our validated antibody pairs, optimized monoclonal/polyclonal antibodies, and bulk ancillary reagents to streamline your assay development and procurement.