Antibody data
- Antibody Data
- Antigen structure
- References [7]
- Comments [0]
- Validations [0]
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- Product number
- ABIN967657 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Glutamate Decarboxylase 2 (Pancreatic Islets and Brain, 65kDa) (GAD2) antibody
- Antibody type
- Monoclonal
- Antigen
- Purified Rat GAD65
- Description
- Purified from tissue culture supernatant or ascites by affinity chromatography.
- Reactivity
- Rat
- Host
- Mouse
- Isotype
- IgG
- Antibody clone number
- GAD-6
- Vial size
- 0.1 mg
- Concentration
- 0.5 mg/ml
- Storage
- 4°C
Submitted references The hydrophilic isoform of glutamate decarboxylase, GAD67, is targeted to membranes and nerve terminals independent of dimerization with the hydrophobic membrane-anchored isoform, GAD65.
Role of synaptic vesicle proton gradient and protein phosphorylation on ATP-mediated activation of membrane-associated brain glutamate decarboxylase.
Comparative localization of two forms of glutamic acid decarboxylase and their mRNAs in rat brain supports the concept of functional differences between the forms.
Differential expression of GAD65 and GAD67 in human, rat, and mouse pancreatic islets.
Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene.
Characterization of the proteins purified with monoclonal antibodies to glutamic acid decarboxylase.
Brain glutamate decarboxylase cloned in lambda gt-11: fusion protein produces gamma-aminobutyric acid.
Kanaani J, Lissin D, Kash SF, Baekkeskov S
The Journal of biological chemistry 1999 Dec 24;274(52):37200-9
The Journal of biological chemistry 1999 Dec 24;274(52):37200-9
Role of synaptic vesicle proton gradient and protein phosphorylation on ATP-mediated activation of membrane-associated brain glutamate decarboxylase.
Hsu CC, Thomas C, Chen W, Davis KM, Foos T, Chen JL, Wu E, Floor E, Schloss JV, Wu JY
The Journal of biological chemistry 1999 Aug 20;274(34):24366-71
The Journal of biological chemistry 1999 Aug 20;274(34):24366-71
Comparative localization of two forms of glutamic acid decarboxylase and their mRNAs in rat brain supports the concept of functional differences between the forms.
Esclapez M, Tillakaratne NJ, Kaufman DL, Tobin AJ, Houser CR
The Journal of neuroscience : the official journal of the Society for Neuroscience 1994 Mar;14(3 Pt 2):1834-55
The Journal of neuroscience : the official journal of the Society for Neuroscience 1994 Mar;14(3 Pt 2):1834-55
Differential expression of GAD65 and GAD67 in human, rat, and mouse pancreatic islets.
Kim J, Richter W, Aanstoot HJ, Shi Y, Fu Q, Rajotte R, Warnock G, Baekkeskov S
Diabetes 1993 Dec;42(12):1799-808
Diabetes 1993 Dec;42(12):1799-808
Two human glutamate decarboxylases, 65-kDa GAD and 67-kDa GAD, are each encoded by a single gene.
Bu DF, Erlander MG, Hitz BC, Tillakaratne NJ, Kaufman DL, Wagner-McPherson CB, Evans GA, Tobin AJ
Proceedings of the National Academy of Sciences of the United States of America 1992 Mar 15;89(6):2115-9
Proceedings of the National Academy of Sciences of the United States of America 1992 Mar 15;89(6):2115-9
Characterization of the proteins purified with monoclonal antibodies to glutamic acid decarboxylase.
Chang YC, Gottlieb DI
The Journal of neuroscience : the official journal of the Society for Neuroscience 1988 Jun;8(6):2123-30
The Journal of neuroscience : the official journal of the Society for Neuroscience 1988 Jun;8(6):2123-30
Brain glutamate decarboxylase cloned in lambda gt-11: fusion protein produces gamma-aminobutyric acid.
Kaufman DL, McGinnis JF, Krieger NR, Tobin AJ
Science (New York, N.Y.) 1986 May 30;232(4754):1138-40
Science (New York, N.Y.) 1986 May 30;232(4754):1138-40
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