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- Table of Contents
Facts about AP-2 complex subunit mu.
Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is included in clathrin-dependent endocytosis where cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin- coated vesicles, CCVs) that are destined for fusion with the early endosome.
Human | |
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Gene Name: | AP2M1 |
Uniprot: | Q96CW1 |
Entrez: | 1173 |
Belongs to: |
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adaptor complexes medium subunit family |
Adaptin-mu2; adaptor-related protein complex 2, mu 1 subunit; AP-2 mu chain; Clathrin assembly protein complex 2 medium chain; clathrin coat adaptor protein AP50; Clathrin coat assembly protein AP50; Clathrin coat-associated protein AP50; clathrin-associated/assembly/adaptor protein, medium 1; HA2 50 kDa subunit; KIAA0109; mu subunit; Plasma membrane adaptor AP-2 50 kDa protein; plasma membrane adaptor AP-2 50kDA protein
Mass (kDA):
49.655 kDA
Human | |
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Location: | 3q27.1 |
Sequence: | 3; NC_000003.12 (184174846..184184091) |
Cell membrane. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV.
The AP2M1 genome is responsible for the production of the heterotetrameric complex coat assembly protein complex 2. Its primary function regulates the flexibility and stability of cell walls' membranes. This marker is ideal for studies of membrane integrity and cell-to–cell communications, as well as lipid-mediated signing. It is available to you in many formats.
The AP2M1 markers have a rich gene pool that can be used in defining specific cellular phenotypes. Many global gene expression profiling studies have been focused on human MSCs. Because of the different probe methods, data from different studies cannot be compared. The use of resampling methods has improved the specificity and sensitivity of cell gene signatures.
The AP2M1 genes has many potential uses in cancer research. This includes cancer cell differentiation and ovarian hormonal production. Its use in cancer immunohistochemical analyses will provide useful information about the tumor's origin. This marker may also be used in a test for recombinant cells to identify tumor-related genes.
The AP2M1 gene encodes a member of the RHO family of small oncogenic GTPases that promote reorganisation of the actin cytoskeleton, which controls cell shape, attachment, and motility. It also codes the protein PLOD2, that is responsible for the Lysyl Hydroxylation of collagen Peptides. Although murine mesenchymal-stem cells are not murine endothelial, their role in maintaining microenvironments for cell survival is vital.
Gene-expression studies have been shown to correlate with various cellular processes, including the production of signaling proteins. These studies are difficult because they have not been replicated by humans. The data from this research can be used to find a disease-causing variant of the AP2M1 genes. Further research will reveal its functional roles in the body.
A boster bioAP2M1 anti-AP2M1 was tested and validated. It is highly specific for the AP2M1 gene and can therefore be used for antigen discovery, disease detection, and cloning. On request, detailed mutagenesis and strategies for cloning are provided. Boster has also validated all antibodies against AP2M1 to ensure the best possible results.
The Boster Bio Anti-AP2M1 antibody has been tested in ELISA, Immunohistochemistry, and IF. This antibody reacts with Human and Mouse cells. It is available in a variety of dilutions to meet your research needs. Boster validates all the antibodies to ensure their purity and effectiveness. The antibody works against both mouse and human samples.
AP2M1 represents a subunit within the coat assembly protein compound 2. It links clathrin receptors to coated vesicles. It also interacts with membrane proteins and polyphosphoinositide-containing lipids. It is a critical endocytic regulator and is required for vacuolarATPase activity. There are four chains within AP2M1, including two large chains, one medium chain, and one smaller.
AP2 binds with a clathrin lactice in CCVs, buds, modulating the coat curvature. It is a key adaptor in CME. Moreover, AP2 has a wide range of conformations. These changes could give us clues as to how AP2 functions in endocytosis. This discovery could help us understand the mechanisms of clathrin-mediated endocysis.
This system does not have membrane budding, but AP2 is a non-driver. Its structure was determined by subtomogram average at 9-A resolution. Its Cm2 is five A further away from a than it is in the open conformation. This movement releases the YxxPh cargo binding pocket, which has a density that is consistent with the peptide bound.
The AP2M1 signal is expressed by a variety of cancer cells and correlates with functional metastasis states. The protein is also expressed in different cell types after apoptosis. Although the function of AP2M1 is not known, it could play a role during apoptosis. It has been shown in vitro to inhibit the invasion by a variety of cancer cells.
Druck et.al. identified the AP2M1 chromosome in 2000. Druck et. al. identified the AP2M1 gene in 2000. The marker was later assigned as chromosome 3q28. The gene is involved in the control of CIS escape and transmission of soluble signals produced by senescent cells. The AP2M1 genome, on the contrary, is involved in TOR signaling.
The AP2M1 mark is a member AP-2 coat assemblies protein complex. This heterotetramer consists of a, b, m and s proteins. The AP2M1 subunit is 50 kDa and plays a pivotal role in the interaction between the cargo protein and the clathrin-coated pit. The AP2M1 subunit recognizes a tyrosine based, endocytotic sorting pattern. Different endocytotic signals, including those that are not canonical, promote interaction between cargo protein and AP2M1 unit.
AP2M1 also belongs to the clathrin adaptive protein complex. Figure 1B depicts this complex. Figure 1B shows this complex. This is a significant step towards developing novel therapies for hepatitis C viral infection.
The AP2M1 gene encodes a subunit of heterotetrameric coat assembly protein complex 2 (CAP2). This complex is a part of the adaptor complicatedes medium subunits and is required for activity of vacuolarATPase. This protein is responsible for proton pumps. It may also contribute to intracellular trafficking of CTLA-4 protein. Boster bio sources its antibodies for AP2M1 from rabbit and mouse.
PMID: 12032142 by Geyer M., et al. Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery.
PMID: 14745134 by Nakatsu F., et al. Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network.