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GW21023

Sigma-Aldrich

Anti-ATP7A antibody produced in chicken

affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-ATPase, Cu++ transporting, α polypeptide, Anti-Copper-transporting ATPase 1, Anti-Menkes disease-associated protein

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About This Item

Numéro MDL:
MFCD03455449
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

chicken

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Espèces réactives

human, mouse, rat

Fabricant/nom de marque

Genway 15-288-21023

Technique(s)

western blot: suitable

Numéro d'accès NCBI

NP_000043.1

Numéro d'accès UniProt

Q04656

Conditions d'expédition

wet ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... ATP7A(538)

Immunogène

Immunogen Sequence: GI # 4502321, sequence 1407-1500
Recombinant ATPase

Application

Anti-ATP7A antibody produced in chicken is suitable for western blotting analysis at a dilution of 1:500, for tissue or cell staining at a dilution of 1:200.

Actions biochimiques/physiologiques

Copper-transporting ATPase 1 is a protein encoded by the ATP7A gene in humans. It mediates systemic copper absorption and provides cupro-enzymes in the trans-Golgi network (TGN) with copper. It constitutively cycles between the TGN and plasma membrane (PM) for regulating the metal homeostasis. Mutation in this gene causes Menkes disease, a rare X-linked recessive disorder characterized by multi-systemic disorder of copper deficiency. This disease is caused due to a novel "silent" substitution in the ATP7A gene.

Forme physique

Solution in phosphate buffered saline containing 0.02% sodium azide.

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Consulter la Bibliothèque de documents

Lisbeth Birk Møller et al.
Molecular genetics and metabolism, 110(4), 490-492 (2013-10-09)
We present a case of classical Menkes disease (MD) due to a novel "silent" substitution in the ATP7A gene; c.2781G>A (p.K927K). The affected nucleotide is the last nucleotide in exon 13, and affects mRNA splicing. Transcripts missing exon 13; and
Qiao Wang et al.
Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics, 16(6), 624-628 (2014-06-14)
Menkes disease is a rare X-linked recessive disorder characterized by multi-systemic disorder of copper deficiency caused by ATP7A gene mutation. In this study, the clinical and laboratory features of three patients with Menkes disease were analyzed. Prenatal diagnosis had been
Zoe G Holloway et al.
Molecular biology of the cell, 24(11), 1735-1748 (2013-04-19)
The transporter ATP7A mediates systemic copper absorption and provides cuproenzymes in the trans-Golgi network (TGN) with copper. To regulate metal homeostasis, ATP7A constitutively cycles between the TGN and plasma membrane (PM). ATP7A trafficking to the PM is elevated in response
Varadarajan Sudhahar et al.
American journal of physiology. Cell physiology, 319(5), C933-C944 (2020-09-17)
Caveolin-1 (Cav-1) is a scaffolding protein and a major component of caveolae/lipid rafts. Previous reports have shown that endothelial dysfunction in Cav-1-deficient (Cav-1-/-) mice is mediated by elevated oxidative stress through endothelial nitric oxide synthase (eNOS) uncoupling and increased NADPH

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