AV41657
Anti-ALAD (AB2) antibody produced in rabbit
affinity isolated antibody
Sinónimos:
Anti-δ-Aminolevulinate dehydratase, Anti-ALADH, Anti-MGC5057
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
Productos recomendados
biological source
rabbit
Quality Level
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
39 kDa
species reactivity
human
concentration
0.5 mg - 1 mg/mL
technique(s)
immunohistochemistry: suitable
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... ALAD(210)
General description
Delta-Aminolevulinate dehydratase (Porphobilinogen synthase, ALA dehydratase), a zinc metalloenzyme, catalyzes the second step of porphyrin biosynthesis and the first common step in the biosynthesis of all biological tetrapyrroles including hemes, chlorophylls and vitamin B12. Hereditary insufficiency of porphobilinogen synthase causes porphobilinogen synthase (or ALA dehydratase) deficiency poprhyria. In addition to heme biosynthesis ALAD may be an important proteosome interacting protein.
Specificity
Anti-ALAD (AB2) antibody detects bovine, human, mouse, and rat porphobilinogen synthase (delta-aminolevulinate dehydratase) enzymes.
Immunogen
Synthetic peptide directed towards the middle region of human ALAD
Application
Anti-ALAD (AB2) antibody is used to tag porphobilinogen synthase (delta-Aminolevulinate dehydratase) proteins for detection and quantitation by Western blotting and in cells and tissues by immunohistochemical (IHC) techniques. It is used as a probe to study the role of this tetrapyrrole synthesizing enzyme in lead poisoning sensitivity, poprhyria and possibly some cancers.
Biochem/physiol Actions
The cytosolic ALAD (δ-aminolevulinic acid dehydratase) plays a vital role in the heme biosynthetic pathway. It facilitates the second step, which is a condensation reaction of 5-aminolevulinic acid and forms 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).
Sequence
Synthetic peptide located within the following region: SVMSYSAKFASCFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDRD
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Disclaimer
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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Storage Class
10 - Combustible liquids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_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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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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