U7757
Anti-UCP-3 antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
Anti-SLC25A9
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About This Item
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biological source
rabbit
conjugate
unconjugated
antibody form
affinity isolated antibody
antibody product type
primary antibodies
clone
polyclonal
form
buffered aqueous solution
mol wt
antigen ~34 kDa
species reactivity
human, rat, mouse
technique(s)
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:3,000 using protease-digested sections of human and mouse skeletal muscle.
western blot: 1:1,000 using extract of E. coli expressing UCP3
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... UCP3(7352)
mouse ... Ucp3(22229)
rat ... Ucp3(25708)
General description
Anti-Uncoupling Protein 3 (UCP3) is developed in rabbit using a synthetic peptide corresponding to amino acid residues 254-267 of human UCP3, with N-terminal lysine added, conjugated to keyhole limpet hemocyanin (KLH). The uncoupling proteins (UCPs) are mitochondrial inner membrane proteins which comprises UCP1, 2, 3, 4 and 5. UCP3 displays two forms, a long mature, UCP3L and a short, UCP3S form. UCP3 is preferentially expressed in skeletal muscle and in brown adipose tissue (BAT).
UCP3 is a skeletal muscle protein that functions to uncouple mitochondrial respiration from ATP production. UCP3 regulates fatty acid and energy metabolism. This protein inhibits lipid-induced oxidative stress in the mitochondrial components of heart and skeletal muscle cells. UCP3 may also be involved in the pathogenesis of type 2 diabetes . Anti-UCP-3 antibody is specific for UCP3 in humans, rats and mice and does not react with UCP1 and UCP2. Staining of the UCP3 band by immunoblotting is specifically inhibited with the immunizing peptide.
Immunogen
The corresponding sequence in rat and mouse UCP3 differ by 4 and 3 amino acids, respectively.
synthetic peptide corresponding to human UCP-3 sequence (amino acids 254-267) with N-terminal lysine added, conjugated to KLH.
Application
Anti-UCP-3 antibody is suitable for use in immunohistochemistry (formalin-fixed, paraffin-embedded sections at 1:3,000 dilution, using protease-digested sections of human and mouse skeletal muscle). The antibody may also be used in immunoblot (approx. 34 kDa, additional weak bands may be detected in some preparations of brown adipose tissue extracts) and western blot (at 1:1,000 dilution, extract of E. coli expressing UCP3).
Anti-UCP-3 antibody produced in rabbit has been used in immunohistochemistry and western blotting.
Biochem/physiol Actions
The uncoupling proteins (UCPs) are considered as transporters functioning as enzymatic uncouplers of oxidative phosphorylation. They are capable of returning protons pumped by the respiratory chain to the mitochondrial matrix. UCP3 is an active proton transporter, regulated by CoQ (ubiquinone), fatty acids or nucleotides.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% BSA and 15 mM sodium azide
Disclaimer
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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Storage Class Code
12 - Non Combustible Liquids
WGK
WGK 2
Certificates of Analysis (COA)
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Patrick Schrauwen et al.
The Proceedings of the Nutrition Society, 62(3), 635-643 (2003-12-25)
Physical activity influences energy metabolism in human subjects by increasing activity-induced energy expenditure and resting metabolic rate for several hours after exercise. On the other hand, physical activity increases mechanical energy efficiency, suggesting that trained subjects would need less energy
Age-associated declines in mitochondrial biogenesis and protein quality control factors are minimized by exercise training
Koltai E, et al.
American Journal of Physiology. Regulatory, Integrative and Comparative Physiology, 303(2), R127-R134 (2012)
Ana Isabel Padrão et al.
Biochimica et biophysica acta, 1822(8), 1189-1197 (2012-05-01)
Hyperglycaemia-related mitochondrial impairment is suggested as a contributor to skeletal muscle dysfunction. Aiming a better understanding of the molecular mechanisms that underlie mitochondrial dysfunction in type 1 diabetic skeletal muscle, the role of the protein quality control system in mitochondria
The mitochondrial uncoupling proteins
Ledesma A, et al.
Genome Biology, 3(12), reviews3015-reviews3011 (2002)
Erika Koltai et al.
American journal of physiology. Regulatory, integrative and comparative physiology, 303(2), R127-R134 (2012-05-11)
A decline in mitochondrial biogenesis and mitochondrial protein quality control in skeletal muscle is a common finding in aging, but exercise training has been suggested as a possible cure. In this report, we tested the hypothesis that moderate-intensity exercise training
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