GLUL Antibody, FITC conjugated

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Description

Structure and Conjugation Chemistry

GLUL Antibody, FITC conjugated, combines a monoclonal or polyclonal antibody with FITC, a fluorophore excited at 488 nm (emission ~519 nm). FITC binds to primary amines (lysine residues) on the antibody, typically at a ratio of 3–6 FITC molecules per antibody to avoid quenching or solubility issues .

ParameterDetails
Conjugation SiteLysine residues (mainly in Fab region for antigen binding)
FITC:Protein Ratio40–80 µg FITC/mg antibody (optimized for brightness and low background)
Reaction BufferPBS or reaction buffer (sodium azide-free to prevent FITC inactivation)
PurificationGel filtration or dialysis to remove unreacted FITC

Applications

GLUL Antibody, FITC conjugated, is used in:

  • Immunohistochemistry (IHC): Detecting cytoplasmic/membranous GLUL in paraffin-embedded tissues .

  • Flow Cytometry (FCM): Quantifying intracellular GLUL expression .

  • Immunofluorescence (IF): Localizing GLUL in subcellular compartments (e.g., mitochondria) .

Example Applications Table

ApplicationKey Use CasesOptimal Dilution
IHC-ParaffinCancer, neurodegeneration, metabolic disorders Experimentally determined
Flow CytometryIntracellular staining in Jurkat cells, immune cells 0.4 µg/10⁶ cells
ImmunofluorescenceMitochondrial GLUL detection in brain or liver tissues 1:50–1:500

Conjugation Heterogeneity

Mass spectrometry studies reveal that Lys-based conjugation produces a heterogeneous mixture of antibody-FITC complexes. For example:

  • Adalimumab-Lys: 2–6 FITC molecules/antibody .

  • Nivolumab-Lys: 28–42 biotin molecules (analogous to FITC conjugation) .

AntibodyConjugation SitesImpact on Function
Adalimumab-LysFab region dominantSlight reduction in antigen binding (~91%)
Nivolumab-LysFc region dominantReduced Fc binding (~61%), increased assay sensitivity

Functional Impacts

  • Fab Conjugation: Preserves antigen binding but may reduce fluorescence brightness due to quenching .

  • Fc Conjugation: Reduces Fc-mediated interactions (e.g., Fc receptor binding) .

Challenges and Best Practices

  • Optimization: Dilutions and conjugation ratios must be experimentally validated .

  • Stability: FITC is light-sensitive; store at 4°C in the dark .

  • Sodium Azide Removal: Critical to prevent FITC inactivation .

Future Directions

  • Site-Specific Conjugation: Targeting specific residues (e.g., Cys) to reduce heterogeneity .

  • Multicolor Flow Cytometry: Pairing with other fluorophores (e.g., Cy3, Dylight488) .

Product Specs

Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Lead Time
Typically, we can ship products within 1-3 business days of receiving your order. Delivery time may vary depending on the purchasing method and location. For specific delivery timeframes, please consult your local distributor.
Synonyms
cell proliferation-inducing protein 59 antibody; Cgl2214 antibody; GLNA antibody; GLNA_HUMAN antibody; GLNS antibody; GLUL antibody; Glutamate ammonia ligase antibody; Glutamate decarboxylase antibody; Glutamate--ammonia ligase antibody; glutamine synthase antibody; Glutamine synthetase antibody; glutamine synthetase I antibody; GS antibody; PIG 43 antibody; PIG 59 antibody; PIG43 antibody; PIG59 antibody; Proliferation inducing protein 43 antibody
Target Names
Uniprot No.

Target Background

Function
Glutamine synthetase catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine. Its role varies depending on tissue localization. In the brain, it regulates toxic ammonia levels and converts neurotoxic glutamate to harmless glutamine. Conversely, in the liver, it participates in ammonia removal. Glutamine synthetase is essential for the proliferation of fetal skin fibroblasts. Independent of its glutamine synthetase activity, it is crucial for endothelial cell migration during vascular development. It regulates membrane localization and activation of the GTPase RHOJ, potentially by promoting RHOJ palmitoylation. Glutamine synthetase may function as a palmitoyltransferase for RHOJ, capable of autopalmitoylating and subsequently transferring the palmitoyl group to RHOJ. It plays a role in ribosomal 40S subunit biogenesis.
Gene References Into Functions
  1. Recent research indicates that, in addition to its known glutamine production, glutamine synthetase exhibits an uncharacterized activity in endothelial cell migration during pathological angiogenesis through RHOJ palmitoylation. PMID: 30158707
  2. In silico analysis suggests a potential link between GLUL SNPs and major depressive disorder. PMID: 29441491
  3. The SNP rs10911021 near glutamate-ammonia ligase has been associated with oxidative stress in coronary heart disease patients from Pakistan. PMID: 29304826
  4. ASCT2 was found to be significantly overexpressed in gastric cancer (GC) samples compared to adjacent non-cancerous gastric mucosa. Conversely, a significantly higher level of glutamine synthetase (GS) expression was observed in normal tissues compared to GC samples. PMID: 29435734
  5. Data identifies GS activity as a mediator of the proangiogenic, immunosuppressive, and pro-metastatic function of M2-like macrophages, highlighting the potential for targeting this enzyme in cancer metastasis treatment. PMID: 28813676
  6. Studies show that 1,25-dihydroxyvitamin D (1,25D) downregulation of glutamine synthetase (GLUL; GS) was sufficient to reduce both GS abundance and enzyme activity. PMID: 29029014
  7. A genome-wide association study to identify genetic factors for familial hepatitis B virus-related hepatocellular carcinoma identified two large-effect susceptible haplotypes located at GLUL and SLC13A2/FOXN1. PMID: 28662289
  8. GLUL knockdown significantly inhibited the p38 MAPK and ERK1/ERK2 signaling pathways in cultured breast cancer cells, leading to a reduction in cell proliferation. PMID: 27791265
  9. Co-targeting glutamine synthetase in the stroma and glutaminase in cancer cells reduces tumor weight, nodules, and metastasis. PMID: 27829138
  10. This study demonstrated the influence of glutamine synthetase gene polymorphisms on the development of hyperammonemia during valproic acid-based therapy. PMID: 26599579
  11. GS is acetylated at lysines 11 and 14, creating a degron essential for binding and ubiquitylation by CRL4(CRBN) and subsequent degradation by the proteasome. PMID: 26990986
  12. The study investigated molecular mechanisms of glutamine synthetase mutations that lead to clinically relevant pathologies. PMID: 26836257
  13. GLUL rs10911021 is prospectively associated with adjudicated cardiovascular composite end points among overweight/obese individuals with type 2 diabetes. PMID: 26395743
  14. Data shows that glutamine synthetase (GS) produces glutamine (Gln) from tricarboxylic acid (TCA)-cycle-derived carbons. PMID: 26595383
  15. Findings point to SNP rs10911021 of GLUL as an independent modulator of mortality in patients with type 2 diabetes. PMID: 25677913
  16. Results highlight the diagnostic errors that can occur due to variant patterns of staining with glutamine synthetase and serum amyloid-associated protein in inflammatory hepatocellular adenoma and focal nodular hyperplasia. PMID: 23807780
  17. High Glutamine synthetase expression is associated with epilepsy in newly diagnosed glioblastoma multiforme. PMID: 23410662
  18. Glutamine synthetase expression is increased in regenerating hepatocytes and in early hepatocyte progenitor cells prior to morphological evidence of hepatocellular differentiation. PMID: 23362937
  19. Through a 3-stage genome-wide association study in 4188 type 2 diabetic patients, a novel susceptibility locus for coronary heart disease was identified in the region of the GLUL gene. PMID: 23982368
  20. These results suggest that GLUL contributes to pancreatic regeneration. PMID: 22930410
  21. The presence of GS in the post-acrosomal region of the perinuclear theca suggests that human sperm can carry out glutamine synthesis. PMID: 22777743
  22. Data indicates that the acidification followed by neutralization (AFBN) pre-treatment protocol for cerebrospinal fluid (CSF) significantly enhances the measurement of glutamine synthetase (GS) and myelin basic protein (MBP) in CSF. PMID: 22542401
  23. This study suggests that serum glutamine synthetase levels lack diagnostic value for Alzheimer's disease. PMID: 21597934
  24. Glutamine synthetase expression can be used to distinguish astrocytic from oligodendroglial tumors and may play a role in the pathogenesis of astrocytomas. PMID: 21682567
  25. The Glul gene could serve as a novel target in genetic therapy for diabetes mellitus. PMID: 20536387
  26. Glutamine synthetase was up-regulated in hepatocellular carcinoma and may serve as a novel marker for early diagnosis. PMID: 20525558
  27. Standard histology and glutamine synthase status identify a hepatocellular carcinoma subset with distinct clinical and pathological features. PMID: 20233882
  28. 2D fingerprinting & mass spectrometry reveal specific targets of protein oxidation in Alzheimer's disease brain, including glutamine synthase, suggesting the involvement of oxidatively modified proteins in neurodegeneration. PMID: 12160938
  29. The detection of a significantly reduced enzymatic activity in the epileptic amygdala supports the assumption that the enzyme defect is localized to the epileptic mesial temporal lobe of corresponding patients. PMID: 16095760
  30. Liver tissue samples from HCV-HCC cancerous tissues and corresponding non-cancerous tissues from patients showed three protein spots of the same molecular mass (42 kDa), whose expression increased in well-differentiated cancerous tissues. PMID: 16609938
  31. In myocytes and hepatomas, but not in adipocytes, glutamine acts to moderate glutamine synthetase induction by glucocorticoids. PMID: 17197094
  32. We confirmed the induction of GS expression by dexamethasone previously published. Components of the glutamatergic system may play a role in bone pathophysiology. PMID: 17627080
  33. The crystal structure of GLUL illustrates substrate-induced conformational change and provides opportunities for drug and herbicide design. PMID: 18005987
  34. In solid pseudopapillary neoplasm of the pancreas, glutamine synthetase expression is highly correlated with Wnt/beta-catenin activation, demonstrating its faithfulness as a Wnt target gene. PMID: 18192886
  35. Glutamine synthetase plays a role in the control of glutamate signaling through Wnt3A and steroid pathways in osteoblastic cells. PMID: 18555765
  36. Glutamine synthetase is found during early human fetal stages, where it exhibits a significant effect on cell proliferation. PMID: 18662667
  37. This study suggests that seizures in GBM are coupled with a highly localized glutamine synthetase deficiency. PMID: 19183851
  38. GS localization was investigated using immunohistochemistry and double-labeling of young and adult human and rat skin sections as well as skin cells in culture. PMID: 19204801
  39. GS mRNA and protein expression did not differ between normal and fetal growth restriction pregnancy. PMID: 19500843

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Database Links

HGNC: 4341

OMIM: 138290

KEGG: hsa:2752

STRING: 9606.ENSP00000307900

UniGene: Hs.132016

Involvement In Disease
Congenital systemic glutamine deficiency (CSGD)
Protein Families
Glutamine synthetase family
Subcellular Location
Cytoplasm, cytosol. Microsome. Mitochondrion. Cell membrane; Lipid-anchor.
Tissue Specificity
Expressed in endothelial cells.

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