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AB199198

HRP Anti-Glutamine Synthetase antibody [EPR13022(B)]

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(1 Publication)

Rabbit Recombinant Monoclonal Glutamine Synthetase antibody - conjugated to HRP. Suitable for WB, IHC-P and reacts with Human, Mouse, Rat samples. Cited in 1 publication.

View Alternative Names

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

1 Images
Western blot - HRP Anti-Glutamine Synthetase antibody [EPR13022(B)] (AB199198)
  • WB

Unknown

Western blot - HRP Anti-Glutamine Synthetase antibody [EPR13022(B)] (AB199198)

This blot was produced using a 4-12% Bis-tris gel under the MOPS buffer system. The gel was run at 200V for 50 minutes before being transferred onto a Nitrocellulose membrane at 30V for 70 minutes. The membrane was then blocked for an hour using 3% milk before being incubated with 199198 overnight at 4°C. Antibody binding was visualised using ECL development solution ab133406.

All lanes:

Western blot - HRP Anti-Glutamine Synthetase antibody [EPR13022(B)] (ab199198) at 1/2500 dilution

All lanes:

Liver (Human) Tissue Lysate - fetal normal tissue at 10 µg

Predicted band size: 42 kDa

Observed band size: 45 kDa

true

Exposure time: 20min

  • Carrier free

    Anti-Glutamine Synthetase antibody [EPR13022(B)] - BSA and Azide free

  • Unconjugated

    Anti-Glutamine Synthetase antibody [EPR13022(B)]

  • 519 Alexa Fluor® 488

    Alexa Fluor® 488 Anti-Glutamine Synthetase antibody [EPR13022(B)]

  • 565 Alexa Fluor® 555

    Alexa Fluor® 555 Anti-Glutamine Synthetase antibody [EPR13022(B)]

  • 603 Alexa Fluor® 568

    Alexa Fluor® 568 Anti-Glutamine Synthetase antibody [EPR13022(B)]

  • 617 Alexa Fluor® 594

    Alexa Fluor® 594 Anti-Glutamine Synthetase antibody [EPR13022(B)]

  • 665 Alexa Fluor® 647

    Alexa Fluor® 647 Anti-Glutamine Synthetase antibody [EPR13022(B)]

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

EPR13022(B)

Isotype

IgG

Conjugation

HRP

Excitation/Emission
Carrier free

No

Reacts with

Human, Human, Mouse, Rat

Applications

IHC-P, WB

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/2500", "WB-species-notes": "<p></p>", "IHCP-species-checked": "guaranteed", "IHCP-species-dilution-info": "", "IHCP-species-notes": "<p></p>" }, "Mouse": { "WB-species-checked": "guaranteed", "WB-species-dilution-info": "", "WB-species-notes": "<p></p>", "IHCP-species-checked": "guaranteed", "IHCP-species-dilution-info": "", "IHCP-species-notes": "<p></p>" }, "Rat": { "WB-species-checked": "guaranteed", "WB-species-dilution-info": "", "WB-species-notes": "<p></p>", "IHCP-species-checked": "guaranteed", "IHCP-species-dilution-info": "", "IHCP-species-notes": "<p></p>" } } }

Product details

Patented technology
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
pH: 7.4 Preservative: 0.1% Proclin 300 Solution Constituents: PBS, 30% Glycerol (glycerin, glycerine), 1% BSA
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|Store in the dark

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). 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

Publications (1)

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

Pediatrics international : official journal of the Japan Pediatric Society 64:e15159 PubMed35727889

2022

The histone deacetylase inhibitor OBP-801 has in vitro/in vivo anti-neuroblastoma activity.

Applications

Unspecified application

Species

Unspecified reactive species

Daisuke Kaneda,Tomoko Iehara,Ken Kikuchi,Yohei Sugimoto,Norio Nakagawa,Shigeki Yagyu,Mitsuru Miyachi,Eiichi Konishi,Toshiyuki Sakai,Hajime Hosoi
View all publications

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