Glutamate Dehydrogenase (GDHB) antibody

Details for Product No. ABIN99811
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Synonyms C2H1orf130
Cow (Bovine)
(7), (3), (2), (1)
(7), (3), (2)
Western Blotting (WB), ELISA
(12), (8), (4), (3), (1), (1)
Pubmed 8 references available
Quantity 2 mL
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Catalog No. ABIN99811
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Immunogen This antibody was prepared from whole rabbit serum produced by repeated immunizations with a full length Glutamate Dehydrogenase protein isolated from Bovine Liver.
Characteristics Concentration Definition: by Refractometry
Alternative Name Glutamate Dehydrogenase
Background Glutamate is a major excitatory neurotransmitter. One enzyme central to the metabolism of glutamate is glutamate dehydrogenase (GDH1; EC, that catalyzes the reversible deamination of L-glutamate to 2-oxoglutarate using NAD+ or NADP+. Mammalian GDH is composed of six identical subunits, and the regulation of GDH is very complex.  It has been a major goal to identify the substrate and regulatory binding sites of GDH. It is only in recent years that the three-dimensional structure of GDH from microorganisms is available. Very recently, crystallization of bovine liver GDH was reported for the first time from the mammalian sources. However, remarkably little is known about the detailed structure of mammalian GDH, especially the brain enzymes.
Synonyms: Glutamate dehydrogenase 1, mitochondrial GDH 1 EC=
Gene ID 281785, 32880221
UniProt P00366
Research Area Metabolism, Amino Acids, Enzymes
Application Notes This antibody has been tested for use in ELISA and by western blot.  Specific conditions for reactivity should be optimized by the end user. Bovine glutamate dehydrogenase exists as a homohexamer located within the mitochondrial matrix.  Expect a band approximately 56 kDa in size corresponding to glutamate dehydrogenase monomer subunit by western blotting in the appropriate cell or tissue extract.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Restore with deionized water (or equivalent)
Concentration 85 mg/mL
Buffer 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C
Supplier Images
anti-Glutamate Dehydrogenase (GDHB) antibody Western blot analysis is shown using anti-bovine glutamate dehydrogenase antibody to detect the enzyme from bovine liver preparations.  Comparison to a molecular weight marker indicates a predominant band of ~62 kDa.  The higher molecular weight band may represent a subunit dimer.  A 4-20% gradient gel was used to separate proteins prior to transfer to 0.2 µm nitrocellulose.  The blot was incubated with a 1:1,000 dilution of the antibody for 2 h at room temperature followed by detection using IRDye™800 labeled Goat-a-Rabbit IgG [H&L] (611-132-122) diluted 1:5,000 for 45 min at room temperature. IRDye™800 fluorescence image was captured using the Odyssey® Infrared Imaging System developed by LI-COR. IRDye is a trademark of LI-COR, Inc.  Other detection systems will yield similar results.
Product cited in: Frigerio, Karaca, De Roo et al.: "Deletion of Glud1 (Glutamate Dehydrogenase 1) in the Central Nervous System affects glutamate handling without altering synaptic transmission." in: Journal of neurochemistry, 2012 (PubMed).

General Anthonio, Brees, Baumgart-Vogt et al.: "Small G proteins in peroxisome biogenesis: the potential involvement of ADP-ribosylation factor 6." in: BMC cell biology, Vol. 10, pp. 58, 2009 (PubMed).

Huybrechts, Van Veldhoven, Hoffman et al.: "Identification of a novel PEX14 mutation in Zellweger syndrome." in: Journal of medical genetics, Vol. 45, Issue 6, pp. 376-83, 2008 (PubMed).

Korolainen, Goldsteins, Nyman et al.: "Oxidative modification of proteins in the frontal cortex of Alzheimer's disease brain." in: Neurobiology of aging, Vol. 27, Issue 1, pp. 42-53, 2005 (PubMed).

Fransen, Vastiau, Brees et al.: "Potential role for Pex19p in assembly of PTS-receptor docking complexes." in: The Journal of biological chemistry, Vol. 279, Issue 13, pp. 12615-24, 2004 (PubMed).

Carobbio, Ishihara, Fernandez-Pascual et al.: "Insulin secretion profiles are modified by overexpression of glutamate dehydrogenase in pancreatic islets." in: Diabetologia, Vol. 47, Issue 2, pp. 266-76, 2004 (PubMed).

Akutsu, Miyazaki: "Biochemical and immunohistochemical studies on tropomyosin and glutamate dehydrogenase in the chicken liver." in: Zoological science, Vol. 19, Issue 3, pp. 275-86, 2002 (PubMed).

Maechler, Gjinovci, Wollheim: "Implication of glutamate in the kinetics of insulin secretion in rat and mouse perfused pancreas." in: Diabetes, Vol. 51 Suppl 1, pp. S99-102, 2002 (PubMed).

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