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Anti-ALDH1A1 (N-terminal region) Antibody

     
  •  - Anti-ALDH1A1 (N-terminal region) Antibody AN1627
    Western blot image of human A431 (lane 1), HepG2 (lane 2), PC3 (lane 3), Jurkat (lane 4), bovine tubulin (lane 5), and recombinant human ALDH1A1 (lane 6). The blot was probed with mouse monoclonal ALDH1A1 M558 (lanes 1-6) at a dilution of 1:1,000.
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Product Information
Primary Accession P00352
Reactivity Bovine
Host Mouse
Clonality Mouse Monoclonal
Isotype IgG1
Clone Names M558
Calculated MW 54862 Da
Additional Information
Gene ID 216
Other Names RALDH, ALDH-E1, ALHDII, Aldehyde dehydrogenase, ALDC, PUMB1, ALDH1A1
Target/Specificity Aldehyde dehydrogenase (ALDH) superfamily is a ubiquitous group of enzymes found in all taxonomic domains. ALDH detoxifies endogenous and exogenous aldehydes, protecting cellular homeostasis and organismal functions. These enzymes are necessary for the synthesis of retinoic acid, betaine, and folate. Recent studies have reported high levels of ALDH found in cancer cells, suggesting that ALDH can act as a marker for cancer cells found in a wide variety of tissues including skin, prostate, lung, and neural tissues. Additionally, certain diseases can be identified when ALDH activity is absent. ALDH1A1 is vital for retinol synthesis and alcohol metabolism. ALDH1A1 active sites include an active cysteine residue, which catalyses the transformation of aldehydes into their respective carboxylic groups. ALDH1A1 amino acid sequence and function is highly conserved in humans and rodents.
Format Protein G Purified
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsAnti-ALDH1A1 (N-terminal region) Antibody is for research use only and not for use in diagnostic or therapeutic procedures.
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Research Areas
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Background

Aldehyde dehydrogenase (ALDH) superfamily is a ubiquitous group of enzymes found in all taxonomic domains. ALDH detoxifies endogenous and exogenous aldehydes, protecting cellular homeostasis and organismal functions. These enzymes are necessary for the synthesis of retinoic acid, betaine, and folate. Recent studies have reported high levels of ALDH found in cancer cells, suggesting that ALDH can act as a marker for cancer cells found in a wide variety of tissues including skin, prostate, lung, and neural tissues. Additionally, certain diseases can be identified when ALDH activity is absent. ALDH1A1 is vital for retinol synthesis and alcohol metabolism. ALDH1A1 active sites include an active cysteine residue, which catalyses the transformation of aldehydes into their respective carboxylic groups. ALDH1A1 amino acid sequence and function is highly conserved in humans and rodents.

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$ 329.00
Cat# AN1627
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