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We validate the specificity of these antibodies to M6PR by testing them on tissues known to express M6PR positively and negatively. Browse below to find the M6PR antibody that suites your experiment. We have 6 of these antibodies and many publications and validation images.
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Facts about Cation-dependent mannose-6-phosphate receptor.
000 Man6PR; 46 kDa mannose 6-phosphate receptor; 46-kDa mannose 6-phosphate receptor; cation-dependent mannose-6-phosphate receptor; CD Man-6-P receptor; CDM6PR; CD-M6PR; CD-MPR; FLJ32994; M6PR; mannose-6-phosphate receptor (cation dependent); MPR 46; MPR46; MPRD; Mr 46; SMPR
|Sequence:||12; NC_000012.12 (8940361..8949761, complement)|
Lysosome membrane; Single-pass type I membrane protein.
A variety of biological assays use the anti-mannose 6phosphate receptor (M6PR), antibody. The antibodies can be monoclonal as well as polyclonal. They bind to Perilipin-3 on a variety of samples. Boster Bio develops antibodies using mouse and rabbit species. The antibody recognizes Perilipin-3 both in the core of lipid bodies and the envelope, including the fatty oils that make the sails.
A Mannose 6 phosphate receptor (M6PR) antibody is used to detect this protein. The M6PR antibody is marked with PE and HRP to detect the protein in whole blood or cell culture supernatants. Flow Cytometry is useful for measuring Mannose6 phosphate receptor gene expression in cell cultures. The M6P receptor can be analyzed by immunohistochemistry on paraffin embedded sections.
The IGF-IIR (insulin-like growth factor-like growth factor-II receptor) is a cytoplasmic protein with a high-quality monoclonal antibody. It is also known as the MPRI or 300-kDa Mannose 6-Phosphate Receptor. It is available in agarose and HRP forms, as well as multiple-conjugated versions.
The M6P/IGF2R cellular signal transduction protein controls several key events. It is frequently mutated in tumors of animals and humans. Cancer progression is linked to loss-offunction mutations of M6P/IGF2R. The mutations are located in the receptor's domains nine, 10, and 11.
Matrigel has shown that the M6P/IGF2R Protein has anti-invasive characteristics in parental SCCVII symbionts. The M6P/IGF2R Dom11mut (wt M6P) inhibits SCC-VII cell invasion by 42-46%, compared to mock-transfected cells.
Double transfection of two human hepatoma cell line lines, HepG2 & BHK, was used to study the structure of M6PR. Both are present in trans-Golgi reticulum, endosomes, and at the plasma membrane. Recombinant M6PR was obtained from Escherichia coli. The structure of M6PR was then determined using immunoprecipitation, SDS–PAGE and quantification radioactive bands.
The extracellular region of the M6PR marker consists of 15 domains, each with a distinct binding site for the Man-6-P peptide. Domain 5 prefers phosphodiester-containing lysosomal enzymes. Domain 5 adopts a conserved fold, enabling its structure to be determined by NMR. The structure of Domain 5 bound to an diester revealed a specific residue for the phosphodiester.
The M6PR is a disulfide -bridged glycoprotein. It contains a single A-helix and C-terminal, methyl groups. Each domain is organized in a single ring that has one hydroxyl. The N-terminal MPR domain is similar to domain 3. However, it lacks two cysteine residuals. Cysteine and tryptophan are found in domains three and four, respectively.
The M6PR cannot enter the liver lysosome. It is therefore protected from degradation in cytosol. It is able to interact with the Rab9/TIP47 group, which then transports them back to the TGN. This process, known recycling, is vital for M6PR traffic within the endosomal–lysosomal system. The M6PR-bound cargo is transported through the clathrin coated vesicles.
CI-MPR has a dimer in its membrane. Domain 3 binds mannose 6-phosphate with high affinity, while domain 5 binds to it with a lower affinity. The M6PR binds phosphodiester Man-phosphate-GlcNAc, which serves as a safety mechanism for the cell. It prevents formation of a divalent compound, which protects cells against the phosphodiester.
The field of cancer treatment has been impacted by the discovery of new molecules that target the CI–M6PR protein. M6P derivatives may be able to deliver therapeutic agents, such as neoplastics, by targeting the receptor at lysosomes. This discovery could also allow for the treatment of other lysosomal illnesses. CI-6PR was previously believed to be a tumour suppressor. Ligands that target this receptor could increase the efficiency of therapies, reduce chemotherapy dosages and side effects, and aid in the treatment of other diseases that affect lysosomal and lysosomal tissues.
M6P analogues must mimic CI-M6PR to inhibit it. For M6P, one negative charge is enough for binding. Binding is not required by the phosphorus atom. Therefore, the best ligands have two negative charges. However, the ability to target CI-M6PR in vitro requires further studies.
CI-6PR regulates granzyme B. It is an essential protein in T cell apoptosis. It also regulates the level of secreted lysosomal enzymes that are involved in tumour dissemination and extracellular matrix degradation. This makes CI-M6PR a promising target for developing new anticancer therapies. It is also well-known to inhibit the growth and progression of hepatocarcinomas.
Ligands that target CIM6PR also have high efficacy and potential in human cancer cell model studies. Ligands that target CI M6PR have a high affinity to slightly acidic extracellular environments in solid tumors. They are therefore a complement to classical chemotherapy. Most anti-neoplastic drugs are weakly basic molecules that target a neutral pH compartment and become inactive in a more acidic environment.
The M6PR gene, which regulates the expression granzymeB, a protein that is important for T cell death, is a potential tumour suppressor. This protein also regulates the secretion levels of lysosomal proteins involved in tumour dissemination as well as extracellular matrix degradation. It is possible to use the M6PR gene as a therapeutic target to deliver chemotherapy drugs to tumour cells, since it is expressed at lower levels in certain cancers than others.
The M6PR-receptor is a large, glycoprotein that facilitates cellular absorption of M6P bearing proteins such as serine protease granzyme -B. Its functions are not well understood, but several molecular mechanisms regulate their expression. Interleukin-2 is an important cytokine that controls the expression M6PR by T cells. This is due to distinct regulation of the Kinesin-3 motor-protein.
The M6PR genes can be used to identify M6PR. This biomarker can also help identify patients who have resisted conventional therapies. To target M6PR-mediated immunity, pharmacological inhibitors for mTORC1 and KIF13A are being studied. These drugs are very specific for M6PR-expressing cancer cell lines.
Alternative pathways for inducing cells death include the M6PR genetic pathway. It binds to Granzyme B, a serine proteinase made by natural killer cells or cytotoxic lymphocytes. It activates the cell death pathway by cleaving cells' cytoplasmic substrates. Perforin-mediated granzyme B accesses its substrates by requiring a pore-forming Protein.
The antibodies to the Perilipin-3 subunit of the membrane glycoprotein were used to identify the M6PR marker. The M6PR is a ubiquitous protein that is present in all eukaryotic cells. It is found at the surface of all cells and is responsible for controlling the expression of many different genes and proteins. Because the M6PR is abundant in the cells, it is used to identify cancer stem cells.
Boster Bio created PLIN3 antibodies using M6PR markers in this study. The PLIN3 markers are a protein that has 11-mer repeats. They are predicted to have a 4-helix bundle structure. Similar structures can be found in the PLIN1 marker and the 2 marker. This marker can be used to develop high-affinity primary antibodies that are useful in a variety clinical settings.
These results suggest that the CD was synthesized from trans-Golgi. Mature MVBs then secrete CD into lysosomes. Tunicamycin prevents the addition mannose 6-phosphate acid hydrolases from blocking this process. Tunicamycin treatment may also cause an increase in CD production. This means that the M6PR marker in cells is removed after the CD is secreted.