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Anti-Glutamic Acid Decarboxylase 65/67 antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Anti-GAD 65/67
MDL number:

biological source


Quality Level



antibody form

IgG fraction of antiserum

antibody product type

primary antibodies




buffered aqueous solution

mol wt

antigen 65-67 kDa

species reactivity

feline, human, rat, mouse, pig


antibody small pack of 25 μL


immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:1,000 using tissue sections of rat pancreas
microarray: suitable
western blot: 1:10,000 using rat brain extract

UniProt accession no.

shipped in

dry ice

storage temp.


Gene Information

human ... GAD2(2572)
mouse ... Gad2(14417)
rat ... Gad2(24380)

Related Categories

General description

GAD 65 has been identified as an autoantigen in insulin dependent diabetes mellitus (IDDM) and stiff-man syndrome (SMS).
GAD is highly expressed in GABAergic neurons and pancreatic β cells. It is transiently expressed in non-GABAergic embryonic and adult neurons, indicating a role in development. It is also present in testis, oviduct, and ovary GAD exists as two isoforms, GAD 65 and GAD 67 (molecular masses of 65 and 67 kDa, respectively) that are encoded by two different genes. GAD65 is an ampiphilic, membrane anchored protein, (585 amino acid residues) and is encoded on human chromosome 10. GAD 67 is a cytoplasmic protein (594 amino acid residues) and is encoded on chromosome 2. There is 64% amino acid idENTITY_TYPE_CODE. The two isoforms appear to have distinct intraneuronal distribution in the brain. The protein is initially localized to cytosol and then gets anchored to the membrane upon post translational modification. The GAD2 gene is mapped to human chromosome 10p12.1.


Reacts specifically with GAD 65 and GAD 67 isoforms in extracts of rat brain and rat pancreas.
Reacts specifically with GAD 65 and GAD 67 isoforms from brain.


synthetic peptide corresponding to the C-terminal region of human GAD 67 (amino acids 579-594). The sequence is identical in human GAD 65 (amino acids 570-585), in rat, mouse, and pig GAD 65, in rat, pig, and cat GAD 67, and is highly conserved in GAD 67 of mouse origin (single amino acid substitution).


Anti-Glutamic Acid Decarboxylase 65/67 antibody produced in rabbit has also been used in Immunohistochemistry and Immunocytochemistry.
Anti-GAD 65/67 may be used for the detection and localization of GAD 65/67 isoforms by immunofluorescence and immunohistochemistry in rat retinal cells, human subthalamus neurons, and pancreatic β-cells of rat. The minimum working dilution that may be used is 1:10000. Detection by immunoblotting may be possible in brain cells of monkey, human, rat and gecko. at a minimum working dilution of 1:1000.

Biochem/physiol Actions

Glutamic acid decarboxylase (GAD) is the key enzyme that catalyses the conversion of L-glutamate to γ-aminobutyric acid (GABA). GABA is a principal inhibitory neurotransmitter and a paracrine signal molecule in pancreatic islet cells. GAD 65 has been identified as an autoantigen in insulin dependent diabetes mellitus (IDDM) and stiff-man syndrome (SMS).

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.


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.

Storage Class Code

12 - Non Combustible Liquids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

Synaptic currents and transmitter responses in human NT2 neurons differentiated in aggregate culture.
Podrygajlo G, et al.
Neuroscience Letters, 468(3), 207-210 (2010)
Aberrant accumulation of the diabetes autoantigen GAD65 in Golgi membranes in conditions of ER stress and autoimmunity.
Phelps E A, et al.
Diabetes, db160180 (2016)
Tomohiro Hamada et al.
Brain research. Molecular brain research, 139(1), 42-51 (2005-06-15)
Transgenic rats expressing enhanced green fluorescent protein (EGFP) under the control of an estrogen receptor (ER) alpha promoter were generated to tag ERalpha-positive neurons in the brain. Two transgenes, one containing sequences for promoter A and DsRed and the other
John A Gebe et al.
Journal of autoimmunity, 30(4), 197-206 (2007-10-24)
A human T-cell receptor (TcR) derived from an autoreactive T-cell specific for GAD65, from a subject at high risk for autoimmune diabetes, was introduced into HLA-DR4 transgenic mice. The source of TcR was a CD4(+) T(H)1(+) T-cell clone which responded
Yoko Inoue et al.
Bioscience, biotechnology, and biochemistry, 72(9), 2269-2276 (2008-09-09)
Glutamate decarboxylase (GAD) is an enzyme that synthesizes gamma-aminobutyrate (GABA), a major inhibitory neurotransmitter in the central nervous system. Post-translational modification of GAD, such as N-terminal blockage, phosphorylation-dephosphorylation, and palmitoylation, is an important factor in the biological activity of GAD.

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