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Merck
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Key Documents

HPA022124

Sigma-Aldrich

Anti-ALAD antibody produced in rabbit

affinity isolated antibody, buffered aqueous glycerol solution, Ab2

Sinônimo(s):

Anti-ALADH, Anti-Delta-aminolevulinic acid dehydratase, Anti-Porphobilinogen synthase

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About This Item

Código UNSPSC:
12352203
Número do Atlas de Proteínas Humanas:
NACRES:
NA.41

fonte biológica

rabbit

conjugado

unconjugated

forma do anticorpo

affinity isolated antibody

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

forma

buffered aqueous glycerol solution

reatividade de espécies

human

técnica(s)

immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:200-1:500

sequência de imunogênio

VLIFGVPSRVPKDERGSAADSEESPAIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFRAEESRQRLAEVALAYA

nº de adesão UniProt

Condições de expedição

wet ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... ALAD(210)

Descrição geral

ALAD (δ-aminolevulinic acid dehydratase) is a cytoplasm localized gene mapped to human chromosome 9q33.1. It exists in both octameric and hexameric form.

Imunogênio

Delta-aminolevulinic acid dehydratase recombinant protein epitope signature tag (PrEST)

Aplicação

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.

Ações bioquímicas/fisiológicas

The cytosolic ALAD (δ-aminolevulinic acid dehydratase) plays a vital role in the heme biosynthetic pathway. It facilitates the second step, which is basically the condensation reaction of 5-aminolevulinic acid, leading to the formation of a monopyrrole termed as porphobilinogen. It is one of the main targets of lead toxicity. Lead replaces zinc present in ALAD, leading to inactivation of the enzyme. Deficiency in ALAD causes ALAD deficiency porphyria (ADP).

Características e benefícios

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Ligação

Corresponding Antigen APREST75306

forma física

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Informações legais

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

Exoneração de responsabilidade

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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Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

Busque Certificados de análise (COA) digitando o Número do Lote do produto. Os números de lote e remessa podem ser encontrados no rótulo de um produto após a palavra “Lot” ou “Batch”.

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Fangjing Wang et al.
International journal of oncology, 30(1), 33-44 (2006-12-05)
The lack of good molecular markers for diagnosis as well as treatment assessment has rendered the hepatocellular carcinoma (HCC) a major challenge in health care. In this study, woodchucks were used as an animal model for hepatitis virus-induced HCC, and
Heather J Hamlin et al.
Reproduction (Cambridge, England), 147(6), 855-863 (2014-03-13)
Comparatively, little data are available detailing the geographic variation that exists in the reproductive endocrinology of adult alligators, especially those living in barrier islands. The Merritt Island National Wildlife Refuge (MI) is a unique barrier island environment and home to
Sarah H Lawrence et al.
The Journal of biological chemistry, 284(51), 35807-35817 (2009-10-09)
Porphobilinogen synthase (PBGS) catalyzes the first common step in tetrapyrrole (e.g. heme, chlorophyll) biosynthesis. Human PBGS exists as an equilibrium of high activity octamers, low activity hexamers, and alternate dimer configurations that dictate the stoichiometry and architecture of further assembly.
E K Jaffe et al.
The Journal of biological chemistry, 276(2), 1531-1537 (2000-10-18)
Human porphobilinogen synthase (PBGS) is a main target in lead poisoning. Human PBGS purifies with eight Zn(II) per homo-octamer; four ZnA have predominantly nonsulfur ligands, and four ZnB have predominantly sulfur ligands. Only four Zn(II) are required for activity. To
N Ishida et al.
The Journal of clinical investigation, 89(5), 1431-1437 (1992-05-01)
Cloning and expression of the defective genes for delta-aminolevulinate dehydratase (ALAD) from a patient with inherited ALAD deficiency porphyria (ADP) were carried out. Cloning of cDNAs for the defective ALAD were performed from EBV-transformed lymphoblastoid cells of the proband, and

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