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AB181625

Anti-Glutamine Synthetase antibody

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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.

대체 명칭 보기

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

1 이미지
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

주요 정보

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 정보

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Brevibacterium": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "", "WB-species-notes": "<p></p>" } } }

특성 및 보관 정보

제형
Liquid
Purity
IgG fraction
Purification 테크닉
Ion exchange chromatography
Purification 관련 사항
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.
보관 버퍼
Preservative: 0.01% Sodium azide Constituents: 0.88% Sodium chloride, 0.424% Potassium phosphate solution
배송 시 보관 조건
Blue Ice
적절한 단기 보관 기간
1-2 weeks
적절한 단기 보관 조건
+4°C
적절한 장기 보관 조건
-20°C
분주 정보
Upon delivery aliquot
보관 정보
Avoid freeze / thaw cycle

추가 정보

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.

제품 프로토콜

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타겟 정보

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). Plays a key role in ammonium detoxification during erythropoiesis : the glutamine synthetase activity is required to remove ammonium generated by porphobilinogen deaminase (HMBS) during heme biosynthesis to prevent ammonium accumulation and oxidative stress (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

제품이 사용된 논문 (1)

Recent publications for all applications. Explore the 전체 목록 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
제품이 사용된 논문 모두 보기

Product promise

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