HPA014769
Anti-ALDH3A2 antibody produced in rabbit
Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution
别名:
Anti-ALDH10, Anti-FALDH, Anti-SLS, ALDH3A2 Antibody - Anti-ALDH3A2 antibody produced in rabbit, Aldh3A2 Antibody
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所有图片(2)
About This Item
推荐产品
生物来源
rabbit
质量水平
偶联物
unconjugated
抗体形式
affinity isolated antibody
抗体产品类型
primary antibodies
克隆
polyclonal
产品线
Prestige Antibodies® Powered by Atlas Antibodies
表单
buffered aqueous glycerol solution
种属反应性
human
技术
immunohistochemistry: 1:50- 1:200
免疫原序列
SHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFSHQRPCLLKSLKREGANKLRYPPNSQSKVDWGKFFLLKRFNKE
UniProt登记号
运输
wet ice
储存温度
−20°C
靶向翻译后修饰
unmodified
基因信息
human ... ALDH3A2(224)
一般描述
ALDH3A2 (aldehyde dehydrogenase 3 family, member A2) is a fatty aldehyde dehydrogenase, which has two alternatively spliced isoforms, differing at their C-termini. This gene is localized to human chromosome 17p11.2, spans 31kb, and contains 11 exons. The predominant isoform has 485 amino acids, and the other isoform has 508 amino acids. It also has three isoforms differing in their sizes, and the two longer transcripts are predominant in brain, heart, pancreas, and skeletal muscle. The shorter isoform is abundant in liver.
免疫原
Fatty aldehyde dehydrogenase recombinant protein epitope signature tag (PrEST)
应用
Anti-ALDH3A2 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project . Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)
Western Blotting (1 paper)
生化/生理作用
ALDH3A2 (aldehyde dehydrogenase 3 family, member A2) is responsible for the oxidation of medium and long-chain fatty aldehydes, giving rise to carboxylic acids. It is a microsomal enzyme, and catalyzes the above reaction in an NAD (nicotinamide-adenine-dinucleotide)-dependent manner. It is also responsible for catalyzing the oxidation of fatty alcohols, and is a part of the fatty alcohol:NAD+ oxidoreductase (FAO) complex. Inactivation of this gene might lead to the accumulation of highly active lipids and fatty alcohols, eventually affecting the integrity of plasma membrane. Mutations in this gene lead to the autosomal recessive disorder called Sjögren-Larsson syndrome (SLS), which is characterized by mental retardation, ichthyosis, and spastic diplegia or tetraplegia.
特点和优势
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.
联系
Corresponding Antigen APREST71639
外形
Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide
法律信息
Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany
免责声明
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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储存分类代码
10 - Combustible liquids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
法规信息
常规特殊物品
W B Rizzo et al.
American journal of human genetics, 65(6), 1547-1560 (1999-12-01)
Sjögren-Larsson syndrome (SLS) is an autosomal recessive disorder characterized by ichthyosis, mental retardation, spasticity, and deficient activity of fatty aldehyde dehydrogenase (FALDH). To define the molecular defects causing SLS, we performed mutation analysis of the FALDH gene in probands from
M A Willemsen et al.
Brain : a journal of neurology, 124(Pt 7), 1426-1437 (2001-06-16)
Sjögren-Larsson syndrome (SLS) is an autosomal recessively inherited neurocutaneous disorder caused by a deficiency of the microsomal enzyme fatty aldehyde dehydrogenase (FALDH). We report the clinical characteristics and the results of molecular studies in 19 SLS patients. Patients 1-17 show
William B Rizzo et al.
Human mutation, 26(1), 1-10 (2005-06-03)
Sjögren-Larsson syndrome (SLS) is an autosomal recessive disorder characterized by ichthyosis, mental retardation, and spastic diplegia or tetraplegia. The disease is caused by mutations in the ALDH3A2 gene (also known as FALDH and ALDH10) on chromosome 17p11.2 that encodes fatty
Raghavendra Mysore et al.
Biochimica et biophysica acta, 1861(4), 342-351 (2016-01-10)
We investigated the expression of miR-192* (miR-192-3p) in the visceral adipose tissue (VAT) of obese subjects and its function in cultured human adipocytes. This miRNA is a 3' arm derived from the same pre-miRNA as miR-192 (miR-192-5p) implicated in type
Anatole Ghazalpour et al.
PLoS genetics, 7(6), e1001393-e1001393 (2011-06-23)
The relationships between the levels of transcripts and the levels of the proteins they encode have not been examined comprehensively in mammals, although previous work in plants and yeast suggest a surprisingly modest correlation. We have examined this issue using
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