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Documenti fondamentali

G5038

Sigma-Aldrich

Anti-GAD2(GAD67) Antibody

enhanced validation

rabbit polyclonal

Sinonimo/i:

Anti-GAD 65

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About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.41

Nome del prodotto

Anti-Glutamic Acid Decarboxylase 65 (5-22) antibody produced in rabbit, IgG fraction of antiserum, buffered aqueous solution

Origine biologica

rabbit

Livello qualitativo

Coniugato

unconjugated

Forma dell’anticorpo

IgG fraction of antiserum

Tipo di anticorpo

primary antibodies

Clone

polyclonal

Stato

buffered aqueous solution

Reattività contro le specie

human, mouse, rat, pig, monkey

Convalida avanzata

independent
Learn more about Antibody Enhanced Validation

tecniche

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

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

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

Descrizione generale

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.

Specificità

Reacts specifically with GAD 65 (65 kDa).

Immunogeno

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.

Applicazioni

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

Azioni biochim/fisiol

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.

Stato fisico

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

Esclusione di responsabilità

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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Codice della classe di stoccaggio

10 - Combustible liquids

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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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)
Yelena Glinka et al.
Journal of molecular medicine (Berlin, Germany), 81(3), 175-184 (2003-04-12)
Nonobese diabetic (NOD) mice develop a T-cell dependent autoimmune form of diabetes, in which glutamic acid decarboxylase 65 (GAD65) is an important islet target antigen. Intramuscular DNA vaccination with a plasmid encoding native GAD65 (a cytosolic antigen) did not significantly
mu Neurocircuitry: Establishing in vitro models of neurocircuits with human neurons
Fantuzzo JA, et al.
Technology, 5(02), 87-97 (2017)
N J Tillakaratne et al.
Journal of neurochemistry, 58(2), 618-627 (1992-02-01)
gamma-Aminobutyric acid (GABA) and its synthetic enzyme, glutamate decarboxylase (GAD), are not limited to the nervous system but are also found in nonneural tissues. The mammalian brain contains at least two forms of GAD (GAD67 and GAD65), which differ from
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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