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AB181625

Anti-Glutamine Synthetase antibody

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(1 Publication)

Goat Polyclonal Glutamine Synthetase antibody. Suitable for WB and reacts with Brevibacterium samples. Cited in 1 publication. Immunogen corresponding to Native Full Length Protein corresponding to Human GLUL.

View Alternative Names

GLNS, GLUL, Glutamine synthetase, GS, Glutamate--ammonia ligase, Palmitoyltransferase GLUL

2 Images
Western blot - Anti-Glutamine Synthetase antibody (AB181625)
  • WB

Supplier Data

Western blot - Anti-Glutamine Synthetase antibody (AB181625)

All lanes:

Western blot - Anti-Glutamine Synthetase antibody (ab181625) at 1/1000 dilution

All lanes:

Glutamine Synthetase at 0.05 µg

Secondary

All lanes:

Peroxidase anti-Goat at 1/40000 dilution

Predicted band size: 42 kDa

false

Western blot - Anti-Glutamine Synthetase antibody (AB181625)
  • WB

Supplier Data

Western blot - Anti-Glutamine Synthetase antibody (AB181625)

Other band(s) : Glutamine Synthetase splice variants and isoforms.

All lanes:

Western blot - Anti-Glutamine Synthetase antibody (ab181625) at 1/3000 dilution

Lane 1:

Glutamine Synthetase Reduced at 1 µg

Lane 2:

Glutamine Synthetase Non-reduced at 1 µg

Secondary

All lanes:

Dylight 649 conjugated Donkey anti goat at 1/10000 dilution

Predicted band size: 42 kDa

false

Key facts

Host species

Goat

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Brevibacterium

Applications

WB

applications

Immunogen

Native Full Length Protein corresponding to Human GLUL.

P15104

Reactivity data

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Properties and storage information

Form
Liquid
Purity
IgG fraction
Purification technique
Ion exchange chromatography
Purification notes
Anti-Glutamine Synthetase antibody is an IgG fraction antibody purified from monospecific antiserum by a multi-step process which includes delipidation, salt fractionation and ion exchange chromatography followed by extensive dialysis against the buffer.
Storage buffer
Preservative: 0.01% Sodium azide Constituents: 0.88% Sodium chloride, 0.424% Potassium phosphate solution
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Glutamine synthetase also known as glutamine s synthetase or glnA is an enzyme that catalyzes the ATP-dependent conversion of glutamate and ammonia into glutamine. This reaction plays an important role in nitrogen metabolism. Glutamine synthetase has a molecular weight of approximately 620 kDa and forms a multimeric structure commonly seen in bacteria plants and animal tissues with significant expression in the brain liver and kidneys.
Biological function summary

This enzyme supports the detoxification of ammonia by incorporating it into glutamine an essential amino acid and nitrogen donor. Glutamine synthetase operates independently rather than as part of a larger protein complex. It assists in maintaining cellular nitrogen balance and facilitates the synthesis of proteins and other nitrogen-containing molecules. Glutamine peptides serve vital roles in cellular processes underlining the significance of their synthesis.

Pathways

Glutamine synthetase integrates into the glutamate and glutamine cycle between neurons and glial cells highlighting its part in neurotransmitter metabolism. It also features prominently in the urea cycle influencing nitrogen disposal in organisms. Glutamine synthetase interacts with glutaminase which assists in transforming glutamine back to glutamate maintaining a balance of nitrogenous compounds within these pathways.

Glutamine synthetase abnormalities link to hepatic encephalopathy and neurodegenerative disorders such as Alzheimer's disease. Altered enzyme expression contributes to increased ammonia levels adversely affecting brain function. In Alzheimer's disease connections with tau and amyloid-beta proteins suggest a link between glutamine synthetase activity and neurotoxic events. Understanding these interactions may offer insights into therapeutic approaches for these conditions.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Glutamine synthetase that catalyzes the ATP-dependent conversion of glutamate and ammonia to glutamine (PubMed : 16267323, PubMed : 30158707, PubMed : 36289327). 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 (By similarity). Essential for proliferation of fetal skin fibroblasts (PubMed : 18662667). 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 (PubMed : 30158707). May act as a palmitoyltransferase for RHOJ : able to autopalmitoylate and then transfer the palmitoyl group to RHOJ (PubMed : 30158707). Plays a role in ribosomal 40S subunit biogenesis (PubMed : 26711351). Through the interaction with BEST2, inhibits BEST2 channel activity by affecting the gating at the aperture in the absence of intracellular L-glutamate, but sensitizes BEST2 to intracellular L-glutamate, which promotes the opening of BEST2 and thus relieves its inhibitory effect on BEST2 (PubMed : 36289327).
See full target information GLUL

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Molecular psychiatry 26:2514-2532 PubMed33303946

2020

ZFP804A mutant mice display sex-dependent schizophrenia-like behaviors.

Applications

Unspecified application

Species

Unspecified reactive species

Ying Huang,Jing Huang,Qi-Xin Zhou,Chun-Xian Yang,Cui-Ping Yang,Wan-Ying Mei,Lei Zhang,Qiong Zhang,Ling Hu,Yun-Qing Hu,Ning-Ning Song,Sheng-Xi Wu,Lin Xu,Yu-Qiang Ding
View all publications

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