G4913
Anti-Glutamic Acid Decarboxylase 65 (514-530) antibody produced in rabbit
IgG fraction of antiserum, buffered aqueous solution
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Synonym(s):
Anti-GAD 65
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biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
IgG fraction of antiserum
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
species reactivity
mouse, pig, human, rat
technique(s)
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:500 using tissue sections of rat pancreas
microarray: suitable
western blot: 1:4,000 using rat brain extract
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... GAD2(2572)
mouse ... Gad2(14417)
rat ... Gad2(24380)
Related Categories
General description
GAD is predominantly expressed in the central nervous system (CNS) and pancreatic islets. It is also expressed in testis, oviduct and ovary. GAD exists in two isofoms, GAD 65 and GAD 67. GAD65 is an ampiphilic, membrane-anchored protein, (585 amino acid residues) and is encoded on human chromosome 10.
Specificity
Reacts specifically with GAD 65 (65 kDa) from brain.
Immunogen
synthetic peptide corresponding to the C-terminal region of human GAD 65 (amino acids 514-530). The sequence is identical in mouse GAD 65 and highly conserved in rat and pig GAD 65 but not found in GAD 67.
Application
Anti-Glutamic Acid Decarboxylase 65 antibody produced in rabbit is suitable as a primary antibody for the determination of expression of GAD 65 isoform in putative P boutons in rat and mouse at a working dilution of 1:5000 and in lysates prepared from rat testis at different developmental ages and rat cerebellum by immunoblotting.
It is also suitable for immunohistochemistry at a working dilution of 1:500 using formalin-fixed, paraffin-embedded sections of rat pancreas and for microarray.
It is also suitable for immunohistochemistry at a working dilution of 1:500 using formalin-fixed, paraffin-embedded sections of rat pancreas and for microarray.
Biochem/physiol Actions
Glutamic Acid Decarboxylase (GAD) catalyzes the conversion of L-glutamate to γ-aminobutyric acid (GABA), the principal inhibitory neurotransmitter in the brain, and a putative paracrine signal molecule in pancreatic islets. It has been identified as an autoantigen in insulin-dependent diabetes mellitus (IDDM) and stiff-man syndrome (SMS) and may serve as a marker in the early stages of IDDM. GAD 65 synthesizes transmitter GABA for vesicular release.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Product No.
Description
Pricing
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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J J Soghomonian et al.
Trends in pharmacological sciences, 19(12), 500-505 (1999-01-01)
Adults express two isoforms of glutamate decarboxylase (GAD), GAD67 and GAD65, which are encoded by different independently regulated genes, a situation that differs from that of other neurotransmitters. In this article, J-J. Soghomonian and David Martin review current knowledge on
A Reetz et al.
The EMBO journal, 10(5), 1275-1284 (1991-05-01)
GABA, a major inhibitory neurotransmitter of the brain, is also present at high concentration in pancreatic islets. Current evidence suggests that within islets GABA is secreted from beta-cells and regulates the function of mantle cells (alpha- and delta-cells). In the
S Baekkeskov et al.
Nature, 347(6289), 151-156 (1990-09-13)
The pancreatic islet beta-cell autoantigen of relative molecular mass 64,000 (64K), which is a major target of autoantibodies associated with the development of insulin-dependent diabetes mellitus (IDDM) has been identified as glutamic acid decarboxylase, the biosynthesizing enzyme of the inhibitory
K Kucharova et al.
Cell transplantation, 20(8), 1163-1178 (2011-06-15)
A major limitation of neural transplantation studies is assessing the degree of host-graft interaction. In the present study, rat hippocampal/cortical embryonic neurons (E18) were infected with a lentivirus encoding enhanced green fluorescent protein (GFP) under control of the neuron-specific
M G Erlander et al.
Neurochemical research, 16(3), 215-226 (1991-03-01)
Studies of the GABA-synthetic enzyme glutamate decarboxylase (glutamic acid decarboxylase; GAD; E.C.4.1.1.15) began in 1951 with the work of Roberts and his colleagues. Since then, many investigators have demonstrated the structural and functional heterogeneity of brain GAD. At least part
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