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- Table of Contents
Facts about Solute carrier family 22 member 3.
.
Human | |
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Gene Name: | SLC22A3 |
Uniprot: | O75751 |
Entrez: | 6581 |
Belongs to: |
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major facilitator (TC 2.A.1) superfamily |
EMTEMTH; Extraneuronal monoamine transporter; OCT3EMT organic cation transporter 3; Organic cation transporter 3; solute carrier family 22 (extraneuronal monoamine transporter), member 3; solute carrier family 22 member 3
Mass (kDA):
61.28 kDA
Human | |
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Location: | 6q25.3 |
Sequence: | 6; NC_000006.12 (160348378..160454982) |
Expressed in placenta, skeletal muscle, prostate, aorta, liver, fetal lung, salivary gland, adrenal gland, kidney and brain cortex. No expression detected in spleen.
Membrane; Multi-pass membrane protein.
As the name suggests, the SLC22A3 Marker is a protein that is involved in the metabolism of fats and carbohydrates. In this article, we will discuss the Best Uses Of The SLC22A3 Marker and the Synthetic peptides that correspond to this protein. These antibodies have high affinity and have been validated in Western blotting, Immunohistochemistry, and ELISA.
SLC22A1 immunohistochemistry was performed using a polyclonal rabbit antiserum raised against the carboxy-terminal region of the human SLC22A1 gene. Tissue specimens were cut into 5 mm sections and transferred to Superfrost-Plus slides. After deparaffinization with xylene, samples were rehydrated with serial dilutions of ethanol. Heat-induced antigen retrieval was performed with a solution buffer at pH 6.0 for 30 minutes.
Molecular mimics of protein binding sites are promising candidates for therapeutic interventions. Chemical peptide synthesis and recombinant protein synthesis are useful in producing these drugs. Synthetic peptides are exact copies of proteins and can be modified with non-proteinogenic amino acids and peptide backbone modifications to enhance their proteolytic stability. In addition to their biological activity, these molecules are able to mimic protein binding sites and inhibit protein-protein interactions in disease processes.
The success of this method is attributed to the fact that the peptides bind b12 better than the monomeric mimotope. By employing a click reaction, these synthetic peptides were produced. They were also highly sensitive to antibiotics. This discovery marked the beginning of the development of novel antibiotic compounds against gram-negative bacteria. Once these molecules are produced, they will be available in clinical trials as a powerful ally for drug discovery.
Chemical peptides can be synthesized using amino acid derivatives with modified backbone lengths, side-chain orientation, or aromatic side chains. By incorporating these molecules into the drug, the peptides can be assembled into scaffolds for multivalent or discontinuous peptide presentation. The peptides will be ready for testing on patients with SLC22A3 disease.
Recombinant proteins require cell expression and complex purification. The latter method involves the creation of synthetic peptides that are specific for a given target protein. The peptides can be used in a variety of applications, including custom antibody generation. A polyclonal antibody can be produced with greater precision than monoclonal antibodies. The advantage of synthetic peptides is the increased control over the epitope and the ability to select a particular amino acid sequence.
In vitro translation systems, in which crude cell extracts such as wheat germ or rabbit reticulocytes are used, are also suitable for the production of synthetic peptides. This method doesn't require the growth of cells and is a more cost-effective method than recombinant proteins. Synthetic peptides are also superior to recombinant proteins.
Flow cytometry has many applications in science, including the study of cells and particles. Primary antibodies can detect specific antigens and are defined by their affinity and specificity. The greater the affinity of a given antibody, the greater its specificity. On the other hand, poor specificity means that it may bind to non-target antigens. In order to identify antigens, primary antibodies must be highly specific, allowing researchers to measure their levels of interest.
A primary antibody enables researchers to ask more questions about their specimens, enabling more precise answers. Additionally, this antibody is also compatible with other primary antibodies, allowing them to work together. By combining primary and secondary antibodies, researchers can use a single antibody to detect multiple antigens in a single sample. This makes it possible to perform more studies with the same specimen, allowing for more in-depth and contextual analysis.
The SLC22A3 gene is expressed in many human tissues, but is mostly found in the cellular plasma membrane, where it plays a role in regulating metabolism and transporting endogenous cations and xenobiotics. It is a bidirectional transporter with distinct patterns of expression in normal and cancerous tissues. This gene is also associated with lung cancer and bladder cancer, but fewer studies have investigated its role in HNSCC.
The SLC22A3 gene encodes a plasma integral membrane protein that is one of three cloned similar cation transporter genes. This gene contains twelve putative transmembrane domains. SLC22A3 is a member of the extraneuronal monoamine transporter family. It contains twelve putative transmembrane domains and is found in all human tissues.
Although the SLC22A3 gene is found on chromosome 6, the coding region encodes a protein called organic cation transporter (OCT3). This gene is widely expressed in tissues and is regulated by cholestasis and is responsible for the bidirectional transport of molecules and drugs. The SLC22A3 gene has been associated with lipid traits, including Lp(a) concentration and LDL-C levels.
Clinical studies have linked high-expression levels of SLC22A3 with increased sensitivity to chemotherapy. This protein was found to increase the sensitivity of various chemotherapeutics to melphalan, irinotecan, and vincristine. This may explain the observed survival benefits among patients with higher levels of SLC22A3 expression. Hence, SLC22A3 has been found to be beneficial in cancer research.
A potential clinical application of SLC22A3 is to monitor drug resistance. Studies have shown that SLC22A3 expression correlates with long survival in advanced T-stage patients. Furthermore, SLC22A3 expression increases cisplatin uptake in SCC-4 cells. Knocking down SLC22A3 decreases cisplatin uptake in hepatic cancer cells. These findings suggest the potential for SLC22A3 as a biomarker for cisplatin.
Other applications of SLC22A3 include tracing the source of pork products and determining a pig's karyomites. Using this marker can improve cellular uptake and disposition. Further, it could help in expanding tracing to source. Therefore, it has many applications. This molecular marker may have a major impact on the field of cancer research. In addition to improving tracing to source, it is also useful for drug safety and security.
PMID: 10196521 by Gruendemann D., et al. Molecular identification of the corticosterone-sensitive extraneuronal catecholamine transporter.
PMID: 9933568 by Verhaagh S., et al. Cloning of the mouse and human solute carrier 22a3 (Slc22a3/SLC22A3) identifies a conserved cluster of three organic cation transporters on mouse chromosome 17 and human 6q26-q27.