Voltage dependent anion channel 1 (VDAC1) is a highly regulated β-barrel membrane protein, encoded by the gene mapped to human chromosome 5q31.1. The encoded protein is a member of VDAC protein family and is mainly localized in the outer mitochondrial membrane.
Immunogen
synthetic peptide located at an internal putative cytoplasmic loop of human VDAC1/Porin (amino acids 152-169) conjugated to KLH. The sequence is identical in bovine and rabbit VDAC1, highly conserved in mouse and rat VDAC1 (single amino acid substitution), and has considerable homology (60-70%) with the human, rat, and mouse VDAC isoforms VDAC2 and VDAC3.
Application
Anti-VDAC/porin antibody produced in rabbit has been used in western blotting.
Biochem/physiol Actions
Voltage dependent anion channel 1 (VDAC1) plays an essential role in several cellular processes. It helps in transport of ions and metabolites between the mitochondria and cytosol of the cell. Oligomerization of this protein facilitates discharge of cytochrome c to the cytoplasm, leading to apoptosis. VDAC1 expression is associated with the development of human papillomavirus (HPV)-related cervical cancer. Thus, VDAC1 knock down can be considered as a potent therapeutic strategy for treating HPV-induced cervical disease.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 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.
The betulinic acid (BetA) purified from Pulsatilla chinensis (PC) has been found to have selective inhibitory effects on hepatitis B virus (HBV). In hepatocytes from HBV-transgenic mice, we showed that BetA substantially inhibited HBV replication by downregulation of manganese superoxide
Proteomics-based identification of VDAC1 as a tumor promoter in cervical carcinoma.
Import of proteins into peroxisomes depends on PEX5, PEX13 and PEX14. By combining biochemical methods and structural biology, we show that the C-terminal SH3 domain of PEX13 mediates intramolecular interactions with a proximal FxxxF motif. The SH3 domain also binds
Crude subcellular fractionation of cultured mammalian cell lines
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.