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We validate the specificity of these antibodies to ABCG2 by testing them on tissues known to express ABCG2 positively and negatively. Browse below to find the ABCG2 antibody that suites your experiment. We have 6 of these antibodies and many publications and validation images.
If you cannot find antibodies that fit your needs, contact us for making custom antibodies. We have a full suite of custom antibody services covering from research to diagnostic and therapeutic applications.
Facts about Broad substrate specificity ATP-binding cassette transporter ABCG2.
Xenobiotic transporter that may play an important role in the exclusion of xenobiotics from the brain. Appears to play a significant role in the multidrug resistance phenotype of many cancer cell lines.
|ABC transporter superfamily|
ABC transporter; ABC15; ABCG2; ABCP; ABCPMGC102821; ATP-binding cassette sub-family G member 2; ATP-binding cassette transporter G2; ATP-binding cassette, sub-family G (WHITE), member 2; BCRP; BCRP1; BCRPMRX; BMDP; Breast cancer resistance protein; CD338 antigen; CD338; CDw338; EST157481; mitoxantrone resistance protein; Mitoxantrone resistance-associated protein; MXR; MXRMXR1; placenta specific MDR protein; Placenta-specific ATP-binding cassette transporter
|Sequence:||4; NC_000004.12 (88090264..88231626, complement)|
Highly expressed in placenta. Low expression in small intestine, liver and colon.
Cell membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Mitochondrion membrane; Multi-pass membrane protein. Enriched in membrane lipid rafts.
If you're looking to use this specific biomarker the best way to do so is to report your results. Boster scientists can utilize this marker to submit results for species, applications or for special samples. Scientists around the world can submit their results to receive credit for their work. Continue reading for more information. Also, read our article on the biomarker Y6 and Cys 603 to learn more about this crucial marker.
The discovery of Y6 could be a promising for reversing the ABCG2-mediated resistance to drugs in cancer cells. The compound blocks ABCG2 efflux and is a well-known competitive substrate for this enzyme. This compound is unlikely to be a powerful reversal agent since it has no impact on subcellular location or expression of ABCG2 genes. The funding for the discovery of Y6 came from the National Natural Science Foundation of China and the NIH grant 1R15CA143701.
Utilizing a t-test the Y6 protein was tested for cytotoxicity in Hepatoma human cells. It was tested in triplicate two concentrations ABCG2-overexpressing cell lines. The results showed that Y6 increased the sensitivity of cells to cisplatin but did not increase their cytotoxic capacity. The compound was also effective in reversing ABCG2-mediated drug resistance in the presence of adenosine triphosphatase-resistant cells.
This compound also has potential to interact with the ABCG2 transporter. Simulations of docking of Y6 revealed that it can bind to the ABCG2 transporter, both in two and three-dimensional structures. Y6 creates hydrogen bonds during docking with the Asn436 & Thr542 residues of the ABCG2 protein. These interactions suggest that Y6 may be an attractive reversible drug to use in the treatment of cancer cells.
The ABCG2 marker is also involved in the progression of cancer. ABCG2 is believed to play a role in the process of tumorigenesis. It could also be utilized in stem cell research and treatment. Recently, the protein was isolated from cancerous cells and proved as a possible substrate for anticancer drugs. Future research in ABCG2 could lead to the development of anti-cancer drugs that are more resistant. In the meantime ABCG2 is a vital marker for monitoring the progression of cancer.
Antibodies to PPARg are available in the market. Boster Bio Anti-PPARg Antibody (phospho-S112) reacts with Rat, Mouse, and Human. It also has been proven to work with the human PPAR Gamma. Numerous publications have demonstrated that this antibody can be useful in the study of T2D. However, the exact mechanism of action of the antibody is not known yet.
The PPARg gene regulates the expression of genes involved in adipocyte differentiation. It has been demonstrated that lipodystrophy and insulin resistance are linked to a loss in function of this gene. A common P12A mutation has been linked to an increased risk of developing type 2 diabetes. Furthermore, rare variations in this gene could also affect the risk of T2D. Recently, a sequencing of PPARG revealed that there are 49 nonsynonymous PPARG variants.
There are many advantages to using Cys 603 in Boster Bio. These antibodies are high-affinity and have been utilized by researchers for over 25 years. They have also been validated on Western Blotting, Immunohistochemistry, and ELISA. If you're not sure if Cys 603 is the right amino acid for your experiments These troubleshooting steps will help you select the appropriate antibody.
The PPARg RXR heteromer has many distinctive characteristics apart from its unique properties in pharmacology. The most notable differences are its dissimilarity from the C2-symmetry as well as the increased surface area between the RXR and PPARg monomers. These properties improve the stability of heterodimers. There are many uncertainties regarding the working of heterodimers.
The DBD-DBD interface is one of the three distinct heterodimerization surfaces. The two LBDs create a dimer interface, which utilizes the helices 7, 9 , and 10 in each receptor. Additionally, the PPARg-RXR heterodimer creates a completely new and previously unexplored heterodimerization interface between the PPARg LBD and the CTE region in the DBD of the RXR-a. These results also suggest that the interaction is DNA dependent.
The heteromer PPARg-RXR also interacts with DNA and the NR complex binds to the phosphorylated proteins. Additionally, heterodimers of PPARg-RXR in Boster Bio have been found to interact with DNA. They are able to interact with each other in both the 5’ and 3’ orientations.
To determine if the PPARg RXR heteromer in the serum of a patient is ligand dependent, it is important to measure the activity of both receptors. However it is the case that the PPARg and RXR heterodimers form a permissive heterodimer, and ligands for either receptor can cause the transcription of PPARg target genes.
The possibility of using this compound for cancer treatment has been sparked due to the discovery that Y6 can reverse ABCG2-mediated MDR in cancer cells. This compound reverses ABCG2-mediated MDR. But how does it reverse the ABCG2 signaling? The authors outline a set of experiments to understand the mechanism of Y6 action. In the first study, Y6 inhibited ABCG2 efflux and did not affect ABCG2 localization.
In a study, the cytotoxic effect on ABCG2-overexpressing cell through Y6 have been determined. Y6 reduced doxorubicin-resistant cell growth in the presence of EGCG and ABCG2-overexpressing cells. It also reduced the levels of hypoxia-inducible factor-1a and multidrug resistance 1/P-glycoprotein. The Y6 inhibitor also reduced the expression of ABCG2 anti-apoptotic proteins kinase.
Further research has confirmed that Y6 has the ability to block the growth of cancerous cells in HEK293R2 cells that have been transfected with ABCG2. It significantly increased sensitivity, and reduced the cytotoxicity of cisplatin in both cell lines. Furthermore, the drug reduced the IC50 value of resistance to ABCG2-mediated drugs. This suggests that it could be used in cancer treatment. These findings also support the use of Y6 as a treatment for reversal.
Many types of cancers have been recently studied the role of ABCG2 in transporting human cancers. ABCG2 is linked to drug resistance and cell differentiation. Previous studies have investigated ABCG2 mRNA in vitro and in vivo models as well as its role in human hepatic cell lines , as well as HCC samples. The most recent study published in Cell has shed light on the role of ABCG2 in the treatment of leukemia.
The role of ABCG2 as a transporter in cancer cells has been linked to its ability to regulate release of cytokines, hormones, and other chemicals. The ability of the transporter to select specific substrates may depend on its ability to change the conformation and prime opposing NBDs for ATP binding. As opposed to Pgp, ABCG2 has a unique closed-to-open transition that is unique to specific substrates.
To assess the role of ABCG2 as a transporter in cancer cells, we examined the TM helices of intact cells. In ABCG2 cells Cys603Ser and Val534Cys form inter-monomer disulfide bonds when they are apo-closed but inward-facing ABCG2 is unable to form these bonds. This is why ABCG2 as a transporter in cancer cells is believed to be a suitable candidate for research into drugs.
*More publications can be found for each product on its corresponding product page