GLUL Recombinant Monoclonal Antibody

Code: CSB-RA260993A0HU

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Size:

50μl100μl

US$210

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Species Reactivity: Human

Application: ELISA, FC

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Target Background

Product Details

Uniprot NO.

P15104

Target Names

GLUL

Alternative Names

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

Species Reactivity

Human

Immunogen

A synthesized peptide derived from human GLUL

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

Rabbit IgG

Clone No.

5E8

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Rabbit IgG in 10mM phosphate buffered saline , pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.

Form

Liquid
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Scope Application

ELISA Protocol Flow Cytometry (FC) Protocol

Recommended Dilution

Application	Recommended Dilution
FC	1:50-1:200

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

Datasheet & COA

Antibody FAQs

Images

Overlay Peak curve showing jurkat cells stained with CSB-RA260993A0HU (red line) at 1:100. The cells were fixed in 4% formaldehyde and permeated by 0.2% TritonX-100 for 10min. Then 10% normal goat serum to block non-specific protein-protein interactions followed by the antibody (1ug/1*10⁶cells) for 45min at 4℃. The secondary antibody used was FITC-conjugated goat anti-rabbit IgG (H+L) at 1/200 dilution for 35min at 4℃.Control antibody (green line) was Rabbit IgG (1ug/1*10⁶cells) used under the same conditions. Acquisition of >10,000 events was performed.

Description

Glutamine synthetase, encoded by the GLUL gene, catalyzes the ATP-dependent condensation of glutamate and ammonia to form glutamine, positioning it at a critical metabolic junction in nitrogen metabolism, amino acid homeostasis, and ammonia detoxification. This enzyme plays essential roles in multiple tissues, with particular significance in the liver where it serves as the final barrier against systemic ammonia toxicity, and in the brain where it maintains glutamate-glutamine cycling between neurons and astrocytes. Beyond its metabolic functions, GLUL has been identified as a proliferation-inducing protein, making it relevant to cancer metabolism research where altered glutamine utilization is a recognized hallmark of tumor biology.

This recombinant monoclonal antibody, clone 5E8, offers researchers the reproducibility advantages inherent to recombinant technology. Because the antibody sequence is defined and expressed consistently, you can expect uniform performance across experiments and over time, eliminating the lot-to-lot variability that can complicate long-term studies or multi-site collaborations. Raised in rabbit against a synthetic peptide derived from human GLUL, this antibody has been validated for human samples and purified by affinity chromatography to ensure high specificity.

Flow cytometry validation using Jurkat cells demonstrates clear detection of intracellular GLUL, with the antibody producing a distinct positive shift compared to isotype control when used at 1:100 dilution following fixation and permeabilization. This validation in a human T-cell leukemia line confirms utility for intracellular flow cytometry applications, with recommended working dilutions ranging from 1:50 to 1:200. The antibody is also validated for ELISA applications, providing flexibility for researchers studying glutamine metabolism, hepatic function, neurological disorders, or cancer metabolic reprogramming.

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Target Background

Function(From Uniprot)

Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine. Its role depends on tissue localization: in the brain, it regulates the levels of toxic ammonia and converts neurotoxic glutamate to harmless glutamine, whereas in the liver, it is one of the enzymes responsible for the removal of ammonia. Essential for proliferation of fetal skin fibroblasts. Independently of its glutamine synthetase activity, required for endothelial cell migration during vascular development: acts by regulating membrane localization and activation of the GTPase RHOJ, possibly by promoting RHOJ palmitoylation. May act as a palmitoyltransferase for RHOJ: able to autopalmitoylate and then transfer the palmitoyl group to RHOJ. Plays a role in ribosomal 40S subunit biogenesis.

Gene References into Functions

findings reveal that, in addition to the known formation of glutamine, the enzyme glutamine synthetase shows unknown activity in endothelial cell migration during pathological angiogenesis through RHOJ palmitoylation PMID:30158707
In silico analysis potentially links GLUL SNPs with major depression disorder. PMID:29441491
The SNP rs10911021 near glutamate-ammonia ligase is associated with oxidative stress in coronary heart disease patients from Pakistan. PMID:29304826
ASCT2 was significantly overexpressed in the gastric cancer (GC) samples compared with adjacent non-cancerous gastric mucosa, in contrast, a significantly higher level of glutamine synthetase (GS) expression was observed in normal tissues than in GC samples compared with adjacent non-cancerous gastric mucosa. PMID:29435734
The data identify GS activity as mediator of the proangiogenic, immunosuppressive, and pro-metastatic function of M2-like macrophages and highlight the possibility of targeting this enzyme in the treatment of cancer metastasis. PMID:28813676
Data show that 1,25-dihydroxyvitamin D (1,25D) downregulation of glutamine synthetase (GLUL; GS)) was sufficient to reduce abundance and enzyme activity of GS. PMID:29029014
genome-wide association study to identify genetic factors for familial hepatitis B virus-related hepatocellular carcinoma; results identified 2 large effect susceptible haplotypes located at GLUL and SLC13A2/FOXN1 PMID:28662289
GLUL knockdown markedly inhibited the p38 MAPK and ERK1/ERK2 signaling pathways in cultured breast cancer cells and reduces their proliferation. PMID:27791265
co-targeting glutamine synthetase in stroma and glutaminase in cancer cells reduces tumor weight, nodules, and metastasis. PMID:27829138
This study demonstrated that Influence of glutamine synthetase gene polymorphisms on the development of hyperammonemia during valproic acid-based therapy. PMID:26599579
GS is acetylated at lysines 11 and 14, yielding a degron that is necessary and sufficient for binding and ubiquitylation by CRL4(CRBN) and degradation by the proteasome. PMID:26990986
Studied molecular mechanisms of glutamine synthetase mutations that lead to clinically relevant pathologies. PMID:26836257
GLUL rs10911021 is associated prospectively with adjudicated cardiovascular composite end points among overweight/obese individuals with type 2 diabetes. PMID:26395743
Data show that glutamine synthetase (GS) produces glutamine (Gln) from tricarboxylic acid (TCA)-cycle-derived carbons. PMID:26595383
findings point to SNP rs10911021 of GLULas an independent modulator of mortality in patients with type 2 diabetes PMID:25677913
Results highlight the diagnostic errors that can be caused by variant patterns of staining with glutamine synthetase and serum amyloid-associated protein in inflammatory hepatocellular adenoma and focal nodular hyperplasia. PMID:23807780
High Glutamine synthetase expression is associated with epilepsy in newly diagnosed glioblastoma multiforme. PMID:23410662
Glutamine synthetase expression is increased in regenerating hepatocytes and in early hepatocyte progenitor cells prior to morphological evidence of hepatocellular differentiation. PMID:23362937
through a 3-stage genome-wide association study in 4188 type 2 diabetic patients, identified a novel susceptibility locus for coronary heart disease in the region of the GLUL gene PMID:23982368
these results suggest that GLUL contributes to pancreatic regeneration. PMID:22930410
The presence of GS in the post-acrosomal region of the perinuclear theca suggests that human sperm can carry out in glutamine synthesis. PMID:22777743
Data show that the acidification followed by neutralisation (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
This study suggests that serum glutamine synthetase levels have no diagnostic value for Alzheimer's disease. PMID:21597934
glutamine synthetase expression can be used to distinguish astrocytic from oligodendroglial tumors and may play a role in the pathogenesis of astrocytomas. PMID:21682567
The Glul can serve as novel target in diabetes mellitus genetic therapy. PMID:20536387
Glutamine synthetase was up-regulated in hepatocellular carcinoma and may be a novel marker for early diagnosis. PMID:20525558
Standard histology and glutamine synthase status identify a hepatocellular carcinoma subset with distinct clinical and pathologic features. PMID:20233882
2D fingerprinting & mass spectrometry reveal specific targets of protein oxidation in Alzheimer's disease brain, including glutamine synthase, suggesting involvement of oxidatively modified proteins in neurodegeneration. PMID:12160938
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
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
In myocytes and hepatomas, but not in adipocytes, glutamine acts to moderate glutamine synthetase induction by glucocorticoids. PMID:17197094
We confirmed the induction of GS expression by dexamethasone published previously. Components of the glutamatergic system may play a role in bone pathophysiology PMID:17627080
Crystal structure of GLUL illustrates substrate-induced conformational change and provides opportunities for drug and herbicide design. PMID:18005987
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
glutamine synthetase has a role in control of glutamate signalling through Wnt3A and steroid pathways in osteoblastic cells PMID:18555765
Glutamine synthetase can be found during early human fetal stages when it displays a significant effect on cell proliferation PMID:18662667
This study suggests that seizures in GBM are coupled with a highly localized glutamine synthetase deficiency. PMID:19183851
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
GS mRNA and protein expression was not different between normal and fetal growth restriction pregnancy PMID:19500843