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G5038

Sigma-Aldrich

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

enhanced validation

IgG fraction of antiserum, buffered aqueous solution

Synonym(e):

Anti-GAD 65

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About This Item

MDL-Nummer:
UNSPSC-Code:
12352203
NACRES:
NA.41

Biologische Quelle

rabbit

Qualitätsniveau

Konjugat

unconjugated

Antikörperform

IgG fraction of antiserum

Antikörper-Produkttyp

primary antibodies

Klon

polyclonal

Form

buffered aqueous solution

Speziesreaktivität

human, mouse, rat, pig, monkey

Erweiterte Validierung

independent
Learn more about Antibody Enhanced Validation

Methode(n)

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-Hinterlegungsnummer

Versandbedingung

dry ice

Lagertemp.

−20°C

Posttranslationale Modifikation Target

unmodified

Angaben zum Gen

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

Allgemeine Beschreibung

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.

Spezifität

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.

Anwendung

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

Biochem./physiol. Wirkung

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.

Physikalische Form

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

Haftungsausschluss

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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Lagerklassenschlüssel

10 - Combustible liquids

Flammpunkt (°F)

Not applicable

Flammpunkt (°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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