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生物源
rabbit
品質等級
共軛
unconjugated
抗體表格
affinity isolated antibody
抗體產品種類
primary antibodies
無性繁殖
polyclonal
形狀
buffered aqueous solution
分子量
39 kDa
物種活性
human
濃度
0.5 mg - 1 mg/mL
技術
immunohistochemistry: suitable
western blot: suitable
NCBI登錄號
UniProt登錄號
運輸包裝
wet ice
儲存溫度
−20°C
目標翻譯後修改
unmodified
基因資訊
human ... ALAD(210)
一般說明
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.
特異性
Anti-ALAD (AB2) antibody detects bovine, human, mouse, and rat porphobilinogen synthase (delta-aminolevulinate dehydratase) enzymes.
免疫原
Synthetic peptide directed towards the middle region of human ALAD
應用
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.
生化／生理作用
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).
序列
Synthetic peptide located within the following region: SVMSYSAKFASCFYGPFRDAAKSSPAFGDRRCYQLPPGARGLALRAVDRD
外觀
Purified antibody supplied in 1x PBS buffer with 0.09% (w/v) sodium azide and 2% sucrose.
免責聲明
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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儲存類別代碼
10 - Combustible liquids
水污染物質分類（WGK）
WGK 3
閃點（°F）
Not applicable
閃點（°C）
Not applicable
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
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
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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