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Merck

G5038

Sigma-Aldrich

Anti-Glutamic Acid Decarboxylase 65 (5-22) antibody produced in rabbit

enhanced validation

IgG fraction of antiserum, buffered aqueous solution

Sinónimos:

Anti-GAD 65

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human, mouse, rat, pig, monkey

enhanced validation

independent
Learn more about Antibody Enhanced Validation

technique(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:1,000 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)

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 targeted to membranes and nerve endings.

Specificity

Reacts specifically with GAD 65 (65 kDa).

Immunogen

synthetic peptide corresponding to the N-terminal region of human GAD 65 (amino acids 5-22). The sequence is highly conserved in rat and pig GAD 65 (single amino acid substitution) and mouse and monkey GAD 65, but is not found in GAD 67.

Application

Anti-Glutamic Acid Decarboxylase 65 (5-22) antibody produced in rabbit has been used in immunohistochemistry and immunocytochemistry.

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. GAD65 is an ampiphilic, membrane-anchored protein, (585 amino acid residues) and is encoded on human chromosome 10. 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.

Disclaimer

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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Storage Class

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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mu Neurocircuitry: Establishing in vitro models of neurocircuits with human neurons
Fantuzzo JA, et al.
Technology, 5(02), 87-97 (2017)
Regulatory cytokine production stimulated by DNA vaccination against an altered form of glutamic acid decarboxylase 65 in nonobese diabetic mice
Glinka Y, et al.
Journal of Molecular Medicine, 81(3), 175-184 (2003)
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
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
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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