HPA022124
Anti-ALAD antibody produced in rabbit
affinity isolated antibody, buffered aqueous glycerol solution, Ab2
Sinónimos:
Anti-ALADH, Anti-Delta-aminolevulinic acid dehydratase, Anti-Porphobilinogen synthase
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About This Item
Productos recomendados
origen biológico
rabbit
conjugado
unconjugated
forma del anticuerpo
affinity isolated antibody
tipo de anticuerpo
primary antibodies
clon
polyclonal
formulario
buffered aqueous glycerol solution
reactividad de especies
human
técnicas
immunoblotting: 0.04-0.4 μg/mL
immunohistochemistry: 1:200-1:500
secuencia del inmunógeno
VLIFGVPSRVPKDERGSAADSEESPAIEAIHLLRKTFPNLLVACDVCLCPYTSHGHCGLLSENGAFRAEESRQRLAEVALAYA
Nº de acceso UniProt
Condiciones de envío
wet ice
temp. de almacenamiento
−20°C
modificación del objetivo postraduccional
unmodified
Información sobre el gen
human ... ALAD(210)
Descripción general
ALAD (δ-aminolevulinic acid dehydratase) is a cytoplasm localized gene mapped to human chromosome 9q33.1. It exists in both octameric and hexameric form.
Inmunógeno
Delta-aminolevulinic acid dehydratase recombinant protein epitope signature tag (PrEST)
Aplicación
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.
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.
Acciones bioquímicas o 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 y beneficios
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:
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.
Ligadura / enlace
Corresponding Antigen APREST75306
Forma física
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
Información legal
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
Cláusula de descargo de responsabilidad
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 clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 1
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°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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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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