AV41656
Anti-ALAD (AB1) antibody produced in rabbit
affinity isolated antibody
Synonym(s):
Anti-δ-Aminolevulinate dehydratase, Anti-ALADH, Anti-MGC5057
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About This Item
NACRES:
NA.41
UNSPSC Code:
12352203
biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
39 kDa
species reactivity
dog, horse, human, guinea pig, bovine
concentration
0.5 mg - 1 mg/mL
technique(s)
western blot: suitable
NCBI accession no.
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... ALAD(210)
General description
ALAD (δ-aminolevulinic acid dehydratase) is a cytoplasm localized gene mapped to human chromosome 9q33.1. It exists in both octameric and hexameric form. ALAD localizes in the cytoplasm.
Immunogen
Synthetic peptide directed towards the N terminal region of human ALAD
Application
Anti-ALAD (AB1) antibody produced in rabbit is suitable for western blot.
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).
Physical form
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
Other Notes
Synthetic peptide located within the following region: EEMLRPLVEEGLRCVLIFGVPSRVPKDERGSAADSEESPAIEAIHLLRKT
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
12 - Non Combustible Liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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The reproductive hormone cycle of adult female American alligators from a barrier island population.
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
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
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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