VDAC1 Antibodies

Voltage-dependent anion-selective channel protein 1 (VDAC1)

Forms a channel through the mitochondrial outer membrane as well as the plasma membrane. The channel in the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; at the plasma membrane it's involved in cell volume regulation and apoptosis.

It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open country has a weak anion selectivity whereas the closed state is cation-selective (PubMed:11845315, PubMed:18755977, PubMed:20230784, PubMed:8420959).

Gene Information

Human
Gene Name:	VDAC1
Uniprot:	P21796
Entrez:	7416

Family

Belongs to:
eukaryotic mitochondrial porin family

Alternative Names

hVDAC1; MGC111064; Outer mitochondrial membrane protein porin 1; Plasmalemmal porin; Porin 31HL; Porin 31HM; PORIN; PORIN-31-HL; VDAC; VDAC-1; voltage-dependent anion channel 1; voltage-dependent anion-selective channel protein 1

Molecular Weight

Mass (kDA):
30.773 kDA

Genomic Context

Human
Location:	5q31.1
Sequence:	5; NC_000005.10 (133971871..134070987, complement)

Tissue Specificity

Heart, liver and skeletal muscle.

Subcellular Localizations

Mitochondrion outer membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Membrane raft; Multi-pass membrane protein.

Diseases

• Malignant Neoplasms
• Neoplasms
• Alzheimer's Disease
• Neurodegenerative Disorders
• Carcinoma
• Hypoxia
• Edema
• Neuroblastoma
• Posttransfusion Purpura
• Malignant Paraganglionic Neoplasm
• Nervousness
• Malignant Neoplasm Of Lung
• Tumor Progression

• Steroid Sulfatase Deficiency Disease
• Tissue Adhesions
• Mitochondrial Diseases
• Fibrosis
• Colonic Neoplasms
• Lung Neoplasms
• Melanoma

Interacting Proteins

• CDK1
• HK1
• ITPR1
• LRRK2
• PRDX6

• RTL10
• SLC25A6
• VDAC2
• VDAC3
• YWHAE

Pathways

• Cell Death
• Transport
• Localization
• Pathogenesis
• Oxidative Phosphorylation
• Cell Growth
• Glycolysis
• Flight
• Mitochondrial Translocation
• Cell Differentiation
• Protein Import
• Cell Proliferation
• Cell Cycle

• Bioluminescence
• Mitochondrial Depolarization
• Programmed Cell Death
• Electron Transport
• Aging
• Immune Response
• Apoptotic Process

PTMs

• Phosphorylation
• Cleavage
• Reduction
• Oxidation

• Nitration
• Biotinylation
• Acetylation
• Ubiquitination

Research Areas

• Cellular Markers
• Mitochondrial Markers

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/VDAC1

Best Uses Of The VDAC1 Marker

What are the best uses for the VDAC1 (VDAC-1) Marker? Learn more about the most effective method for your research. Boster Bio offers a broad range of ELISA kits that have been tested and validated with many different samples. The validation process and images are available upon request. Picoband(tm), an immunogen, reduces time and improves background. Its immunogen is powered with understanding of the traits of a reliable immunogen and is backed by extensive technical support.

Immunoprecipitation

Boster Bio offers over 12,000 antibodies, including ELISA kits and picogram-sensitive polyclonal antibodies. These antibodies have been validated against IHC, WB, and Flow, and have been tested against a range of 250 different tissues. Boster Bio antibodies have also been validated quantitatively against known levels of recombinant proteins. Boster Bio offers the VDAC1 Marker on its website tebubio.com.

The Boster Bio Anti-VDAC/Porin/VDAC1 Marker is part of the Picoband(tm) antibody catalog, and has undergone extensive testing in IHC and WB. It reacts with mouse, human and rat tissue. Additionally, it was designed to meet strict gold standard validation requirements, ensuring that users are able to trust their data. Best Uses of the VDAC1 Marker

This marker allows researchers to determine the presence of this protein within human cells. These cells express hundreds of thousands of cell surface antigens, and fluorochrome-conjugated antibodies are used to analyze cells directly. Direct immunofluorescence staining is different from indirect staining. It involves incubating cells with antibodies that are directly conjugated to fluorescent agents. This eliminates non-specific binding. Another important advantage of this method is the removal of the possibility of non-specific binding as secondary antibodies do not enter the cells.

Immunoprecipitation with StAR

We have carried out immunoprecipitation studies using StAR and VDAC1 markers. This method permits an antibody to be conjugated with a target protein in a solution. The complex of antibody/target protein is then removed from the sample by using Agarose beads with Protein A/G coupling. The protein isolated can be analysed by western blot using the primary antibody. To detect the target proteins we utilized rabbit anti-TOM20 (1:140) and STAR RED (1;140) antibodies.

The research revealed that StAR treatment does nothing to alter the interactions between VDAC1 and 14-3-3e. Interestingly, the 14-3-3e-VDAC1 interaction was inhibited by treatment with TVS167. Similar to the inhibition of 14-3-3e binding, VDAC1 is also inhibited by StAR. The protein lysates that were precipitated were subjected to SDS-PAGE in order to determine the binding sites.

We have previously shown that StAR converts to a 30kDa protein in transcription and is imported into mitochondria. This results in the immunoprecipitated proteins being inaccessible to mitochondria without TritonX100. The same test with VDAC1 demonstrated that the Tim9/StAR immunoprecipitated proteins bind to the OMM and are activated when there MA-10 mitochondria.

The beads must be added to the lysate, and the mixture is turned down to 14,000 rpm, at 4degC. The supernatant must be removed. To minimize background and nonspecific binding it might be necessary to perform pre-clearing. The process can also be done with an antibody that is not targeted. A cell culture lysate can be a good example.

Immunoprecipitation with DAPI

The VDAC1 protein encodes numerous antigens, and is widely expressed throughout the human body. While the VDAC1 protein is found in all tissues and cells, its expression is most prominent in the heart and liver. The VDAC2 isoform, on the other hand is only expressed in the heart. This protein plays an important role in the body's defense mechanisms.

ELISA

The ELISA test for VDAC1 is used for measuring the protein's concentration. This marker plays an important role in mitochondrial transport and regulates entry of adenine nucleotides, Ca2+, and various metabolites. It is found throughout the body but is most abundant in the liver and skeletal muscle. It also forms channels in the plasma membrane.

The reagents utilized to induce the apoptosis process include STS or selenite. As2O3. The reagents were then incubated for 15 minutes in HeLa cells. After two washes with PBS before incubating with 250 mM EGS for another two hours. Antibodies to VDAC1 then immunoblotted using a specific detection antibody. The presence of BRET2 indicates that the recombinant enzyme forms an oligomer.

A polar metabolite can be detected by taking its charge. The greater the charge, the greater the concentration of the molecule. The signal strength is also affected by the size of the molecules. This signal can be used in clinical settings to identify cancer cells. It is also used to determine if the cancer cell line has started to grow. In addition to ELISAs, there are other methods to measure VDAC1 expression.

The results of the test for VDAC1 expression in blood are highly reproducible. The ELISA test of VDAC1 marker can be utilized for many research studies that deal with apoptosis, for instance. In cancer cells, VDAC1 is involved in the protection against Apoptosis. It is important to know that the markers employed in the ELISA are drawn from human blood samples.

Supernatants from cell culture

To determine the vesicle content in CCM The samples were cleared and incubated for a night at 4°C with the primary antibody. Then they were incubated for one hour at 37degC , using the secondary antibody. Following this the samples were then subjected to NTA measurements and the pellets were lysed prior to quantification of protein. The Journal of Cell Culture published an article on the results of the experiment.

We used human GBM cells lines to identify the peptides which were derived from VDAC1. To determine the concentrations of peptides that cause cell death, we carried out flow cytometry analysis and staining with propidium Iodide. The IC50 values of the peptides were calculated from the activity of cells dying at half-maximal concentrations. In this study, we investigated the effects of Tf-DLP4 and Retro-Tf -D-LP4 on cell lines.

The majority of solid tumors, such as GSCs and GBM cells, use glucose as their source of energy. Changes in glucose metabolism are linked with the progression of cancer carcinogenesis, treatment responses, and cancer progression. Since VDAC1 regulates mitochondrial functions and plays a role in energy metabolism, it is most likely to be over-expressed in cancerous cells. VDAC1 overexpression could be a contributing factor to the cell's proliferative abilities.

The peptide VDAC1 is highly sensitive to GSCs and causes cell death. Thus, the VDAC1 marker in supernatants of cell cultures can be used to detect GSCs. The peptide was discovered to be sensitive to DsbA, which is a highly active component of the membrane of cancerous cells. This marker is useful for a variety of research purposes such as the identification of VDAC1 in cell culture supernatants.

Immunoprecipitation by VEGF-a

We utilized immunoprecipitation to investigate the metabolic function and biological labelling for its processing products. In this study, we utilized a transfected 293-EBNA cell line. We found that the 21 kDa polypeptide was approximately one-third of the 31 kDa polypeptide found in the same conditioned medium that contained VEGF-C that is wt.

Human fibroblasts are known contain VEGF-C. Therefore, it is possible to utilize immunoprecipitation to detect the presence of the protein. The cells were transfected using an RNA molecule encoding CD146 and then incubated with conditional media. The form of the virus that was soluble was determined by immunofluorescence.

The R102S mutation has no impact on the production of VEGF-C. This mutant is the C-terminal peptide sequence in the VEGF–C protein. Antiserum 905 was unable to precipitate DN VEGF-C, which lacks the N-terminal propeptide. Although it co-precipitated along with other polypeptides of 29-32 kDa but antiserum 882 wasn't capable of recognizing disulfide bonds.

Both antibodies precipitated VEGF-C forms with molecular masses of 15 21, 29/31 and 21 kDa. They also precipitated polypeptides with the N-terminal VEGF–C sequence. Both antibodies precipitated R-3EC but less effectively than antiserum-882. We conclude that VEGF–C is more powerful VEGF–A antagonist that antiserum-882.