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Purified Mouse Anti-ALDH
Purified Mouse Anti-ALDH
Western blot analysis of ALDH on A431 cell lysate. Lane 1: 1:500, lane 2: 1:1000, lane 3: 1:2000 dilution of anti-ALDH antibody.
Purified Mouse Anti-ALDH
Immunofluorescent staining of HepG2 cells with anti-ALDH.
Western blot analysis of ALDH on A431 cell lysate. Lane 1: 1:500, lane 2: 1:1000, lane 3: 1:2000 dilution of anti-ALDH antibody.
Immunofluorescent staining of HepG2 cells with anti-ALDH.
製品詳細
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BD Transduction Laboratories™
Human (QC Testing)
Mouse IgG1
Human ALDH1 aa. 7-128
Western blot (Routinely Tested), Immunofluorescence (Tested During Development), Immunohistochemistry (Reported)
55 kDa
250 µg/ml
AB_398729
Aqueous buffered solution containing BSA, glycerol, and ≤0.09% sodium azide.
RUO


Product Notices

  1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
  2. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
  3. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
  4. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
611194 Rev. 3
抗体の詳細
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44/ALDH

Aldehyde dehydrogenase (ALDH) is a ubiquitous enzyme located in nearly all mammalian tissues. It catalyzes the irreversible oxidation of a range of aliphatic and aromatic aldehydes to their corresponding carboxylic acids. There are multiple isoforms of ALDH which are subdivided into three classes. Class I includes the cytosolic isoforms. Class II includes the mitochondrial isoforms. Class III includes the microsomal, cytosolic tumor specific, and cytosolic dioxin-inducible forms. At least twelve human ALDH isoforms have been identified. Mutations of many of these proteins such as ALDH1, ALDH2, ALDH4, and ALDH10 have been implicated in multiple human metabolic disorders and clinical abnormalities. At the amino acid level, human ALDH isoforms exhibit a wide range of diversity (15% to about 80%). However, multiple protein regions have been highly conserved and are important for functional activities. A well-characterized member of the human ALDH family is ALDH1. It plays a major role in the biosynthesis of retinoic acid from retinol (vitamin A). Retinoic acid, the biologically active form of retinol, is a regulator of cellular proliferation, differentiation, and survival.

611194 Rev. 3
フォーマットの詳細
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Purified
Tissue culture supernatant is purified by either protein A/G or affinity purification methods. Both methods yield antibody in solution that is free of most other soluble proteins, lipids, etc. This format provides pure antibody that is suitable for a number of downstream applications including: secondary labeling for flow cytometry or microscopy, ELISA, Western blot, etc.
Purified
611194 Rev.3
引用&参考文献
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Development References (4)

  1. Greene WK, Bahn S, Masson N, Rabbitts TH. The T-cell oncogenic protein HOX11 activates Aldh1 expression in NIH 3T3 cells but represses its expression in mouse spleen development. Mol Cell Biol. 1998; 18(12):7030-7037. (Biology). View Reference
  2. Kathmann EC, Lipsky JJ. Cloning of a cDNA encoding a constitutively expressed rat liver cytosolic aldehyde dehydrogenase. Biochim Biophys Acta. 1997; 236(2):527-531. (Biology). View Reference
  3. Yoshida A, Rzhetsky A, Hsu LC, Chang C. Human aldehyde dehydrogenase gene family. J Biol Chem. 1998; 251(3):549-557. (Biology). View Reference
  4. Zhou JH, Hanna EY, Roberts D, Weber RS, Bell D. ALDH1 immunohistochemical expression and its significance in salivary adenoid cystic carcinoma. Head & Neck. 2012; 35(4):575-578. (Clone-specific: Immunohistochemistry). View Reference
すべて表示する (4) 表示項目を減らす
611194 Rev. 3

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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

For Research Use Only. Not for use in diagnostic or therapeutic procedures.