Glutamate Decarboxylase 2 (Pancreatic Islets and Brain, 65kDa) (GAD2) antibody

Details for Product No. ABIN967657
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Antigen
Synonyms GAD65, gad65, F12P19.12, F12P19_12, GLUTAMATE DECARBOXYLASE 2, glutamate decarboxylase 2, zgc:112198, 6330404F12Rik, GAD(65), Gad-2
Reactivity
Rat (Rattus)
(101), (57), (42), (24), (24), (15), (12), (3), (1), (1)
Host
Mouse
(96), (13), (8)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(4), (4), (3), (2), (2), (2), (2), (2), (2), (2), (2), (1), (1), (1)
Application
Western Blotting (WB), Immunohistochemistry (Frozen Sections) (IHC (fro)), Immunoprecipitation (IP)
(79), (37), (27), (23), (20), (14), (10), (6), (3), (3), (2), (1)
Pubmed 7 references available
Quantity 0.1 mg
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Catalog No. ABIN967657
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Immunogen Purified Rat GAD65
Clone GAD-6
Isotype IgG2a, kappa
Cross-Reactivity Human, Mouse (Murine), Pig (Porcine)
Characteristics 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Please refer to us for technical protocols.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
Purification Purified from tissue culture supernatant or ascites by affinity chromatography.
Alternative Name GAD65
Background Gamma-aminobutyric acid (GABA) is an amino acid neurotransmitter that is considered to be the major inhibitory neurotransmitter in the mammalian central nervous system. The highest concentrations of GABA are found in the brain, where it is synthesized from glutamic acid to GABA by an enzyme called glutamic acid decarboxylase (GAD). GAD is also expressed in the insulin-producing beta cells of the islets of Langerhans. Two isoforms of GAD are present in rat brain, GAD65 and GAD67, based on their relative molecular weight in kDa. Both isoforms have significant levels of homology in the catalytic portion of the molecule, but differ greatly in the first 95 amino acids in the N-terminal region. GAD65 migrates at ~65 kDa in SDS/PAGE. The antibody is reported to recognize rat, human, mouse, and pig GAD65. Purified GAD65 from rat brain was used as the immunogen. The specific epitope recognized by this clone is a linear epitope localized in the last 41 amino acids of GAD65.
Molecular Weight 65 kDa
Research Area Neurology, Amino Acids
Application Notes Rat brain cortex is recommended as a positive control for western blot
Restrictions For Research Use only
Format Liquid
Concentration 0.5 mg/ml
Buffer Aqueous buffered solution.
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 Decarboxylase 2 (Pancreatic Islets and Brain, 65kDa) (GAD2) antibody Western blot analysis of GAD65. Lysates from rat brain cortex were probed with purified anti-GAD65 (clone GAD-6) at a concentration of 5.0 (lane 1), 2.0 (lane 2) or 0.5 µg/ml (lane 3). GAD65 is identified as a protein of ~65 kDa.
anti-Glutamate Decarboxylase 2 (Pancreatic Islets and Brain, 65kDa) (GAD2) antibody (2) anti-Glutamate Decarboxylase 2 (Pancreatic Islets and Brain, 65kDa) (GAD2) antibody (Image 2)
Product cited in: Bu, Erlander, Hitz et al.: "Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 89, Issue 6, pp. 2115-9, 1992 (PubMed).

Chang, Gottlieb: "Characterization of the proteins purified with monoclonal antibodies to glutamic acid decarboxylase." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 8, Issue 6, pp. 2123-30, 1988 (PubMed).

Kaufman, McGinnis, Krieger et al.: "Brain glutamate decarboxylase cloned in lambda gt-11: fusion protein produces gamma-aminobutyric acid." in: Science (New York, N.Y.), Vol. 232, Issue 4754, pp. 1138-40, 1986 (PubMed).

Esclapez, Tillakaratne, Kaufman et al.: "Comparative localization of two forms of glutamic acid decarboxylase and their mRNAs in rat brain supports the concept of functional differences between the forms." in: The Journal of neuroscience : the official journal of the Society for Neuroscience, Vol. 14, Issue 3 Pt 2, pp. 1834-55, 1994 (PubMed).

Kim, Richter, Aanstoot et al.: "Differential expression of GAD65 and GAD67 in human, rat, and mouse pancreatic islets." in: Diabetes, Vol. 42, Issue 12, pp. 1799-808, 1993 (PubMed).

Hsu, Thomas, Chen et al.: "Role of synaptic vesicle proton gradient and protein phosphorylation on ATP-mediated activation of membrane-associated brain glutamate decarboxylase." in: The Journal of biological chemistry, Vol. 274, Issue 34, pp. 24366-71, 1999 (PubMed).

Kanaani, Lissin, Kash et al.: "The hydrophilic isoform of glutamate decarboxylase, GAD67, is targeted to membranes and nerve terminals independent of dimerization with the hydrophobic membrane-anchored isoform, GAD65." in: The Journal of biological chemistry, Vol. 274, Issue 52, pp. 37200-9, 2000 (PubMed).

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