437695
Anti-Lipoic Acid Rabbit pAb
liquid, Calbiochem®
Synonym(s):
Anti-LA
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.43
Recommended Products
biological source
rabbit
Quality Level
antibody form
diluted serum
antibody product type
primary antibodies
clone
polyclonal
form
liquid
does not contain
preservative
species reactivity (predicted by homology)
all
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
avoid repeated freeze/thaw cycles
isotype
IgG
shipped in
wet ice
storage temp.
−70°C
target post-translational modification
unmodified
General description
Rabbit polyclonal antibody supplied as diluted serum. Recognizes native lipoic acid and lipoic acid covalently attached to proteins.
Recognizes native lipoic acid. Does not recognize lipoic acid modified by 4-HNE (4-hydroxy-2-noneal) and other lipid peroxidation products.
This Anti-Lipoic Acid Rabbit pAb is validated for use in ELISA, Frozen Sections, Immunoblotting, Paraffin Sections for the detection of Lipoic Acid.
Immunogen
lipoic acid conjugated to KLH
Application
ELISA (1:500-1:1000)
Frozen Sections (1:50-1:500)
Immunoblotting (1:1000-1:10,000)
Paraffin Sections (1:50-1:500)
Frozen Sections (1:50-1:500)
Immunoblotting (1:1000-1:10,000)
Paraffin Sections (1:50-1:500)
Warning
Toxicity: Standard Handling (A)
Physical form
serum diluted in buffer, 50% glycerol, pH 7.5.
Other Notes
Does not bind lipoic acid modified by 4-HNE (4-hydroxy-2-noneal) and other lipid peroxidation products. Useful for assessing whether protein-bound lipoic acids have undergone certain forms of oxidative modification. The presence of protein-bound lipoic acid can be used as a marker for mitochondria. Variables associated with assay conditions will dictate the optimal working dilution.
Sasaki, M., et al. 2000. J. Autoimmun.15, 51.
Heitzer, T., et al. 2001. Free Radic. Biol. Med.31, 53.
Patrick. L. 2000. Altern. Med. Rev.5, 290.
Shi, S.S., et al. 1999. Antioxid. Redox Signal1, 123.
Humphries, K.M. and Szeda, L.I. 1998. Biochemistry37, 15835.
Heitzer, T., et al. 2001. Free Radic. Biol. Med.31, 53.
Patrick. L. 2000. Altern. Med. Rev.5, 290.
Shi, S.S., et al. 1999. Antioxid. Redox Signal1, 123.
Humphries, K.M. and Szeda, L.I. 1998. Biochemistry37, 15835.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Certificates of Analysis (COA)
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Rosa Purroy et al.
Redox biology, 32, 101520-101520 (2020-04-13)
Friedreich ataxia (FA) is a cardioneurodegenerative disease caused by deficient frataxin expression. This mitochondrial protein has been related to iron homeostasis, energy metabolism, and oxidative stress. Previously, we set up a cardiac cellular model of FA based on neonatal rat
Nicolas L Taylor et al.
Methods in molecular biology (Clifton, N.J.), 372, 389-403 (2008-03-05)
Mitochondria not only are a source of reactive oxygen species (ROS) but also are sites of oxidative damage. In plants, mitochondria must normally operate when there are high levels of ROS produced during photosynthesis and photorespiration. These levels are further
Hirokazu Kinugawa et al.
MicrobiologyOpen, 9(10), e1113-e1113 (2020-08-31)
Pyruvate dehydrogenase (PDH) and 2-oxoglutarate dehydrogenase (ODH) are critical enzymes in central carbon metabolism. In Corynebacterium glutamicum, an unusual hybrid complex consisting of CgE1p (thiamine diphosphate-dependent pyruvate dehydrogenase, AceE), CgE2 (dihydrolipoamide acetyltransferase, AceF), CgE3 (dihydrolipoamide dehydrogenase, Lpd), and CgE1o (thiamine
Yvonne Sun et al.
Infection and immunity, 78(11), 4667-4673 (2010-09-09)
Anteiso-branched-chain fatty acids (BCFA) represent the dominant group of membrane fatty acids and have been established as crucial determinants in resistance against environmental stresses in Listeria monocytogenes, a facultative intracellular pathogen. Here, we investigate the role of anteiso-BCFA in L.
Claudia Huichalaf et al.
Molecular therapy. Methods & clinical development, 24, 367-378 (2022-03-08)
Friedreich's ataxia is a rare disorder resulting from deficiency of frataxin, a mitochondrial protein implicated in the synthesis of iron-sulfur clusters. Preclinical studies in mice have shown that gene therapy is a promising approach to treat individuals with Friedreich's ataxia.
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