Recombinant Mouse Ap2b1 Protein, Myc/DDK-tagged
|Product Overview :||Purified recombinant protein of mouse full-length adaptor-related protein complex 2, beta 1 subunit (Ap2b1), with C-terminal MYC/DDK tag, expressed in HEK293T cells.|
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|Description :||Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10. The AP-2 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin-associated sorting proteins (CLASPs) are recognized by their [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly.|
|Molecular Mass :||105.7 kDa|
|Purity :||> 80% as determined by SDS-PAGE and Coomassie blue staining|
|Stability :||Stable for 12 months from the date of receipt of the product under proper storage and handling conditions. Avoid repeated freeze-thaw cycles.|
|Storage :||Store at -80 centigrade after receiving vials.|
|Concentration :||>50 μg/mL as determined by microplate BCA method|
|Storage Buffer :||25 mM Tris.HCl, pH 7.3, 100 mM glycine, 10% glycerol.|
|Gene Name :||Ap2b1 adaptor-related protein complex 2, beta 1 subunit [ Mus musculus (house mouse) ]|
|Official Symbol :||Ap2b1|
|Synonyms :||AP2B1; adaptor-related protein complex 2, beta 1 subunit; AP-2 complex subunit beta; AP105B; beta-adaptin; beta2-adaptin; beta-2-adaptin; adaptor protein complex AP-2 subunit beta; adapter-related protein complex 2 beta subunit; clathrin assembly protein complex 2 beta large chain; plasma membrane adaptor HA2/AP2 adaptin beta subunit; AI788979; 1300012O03Rik|
|Gene ID :||71770|
|mRNA Refseq :||NM_001035854|
|Protein Refseq :||NP_001030931|
|UniProt ID :||Q9DBG3|
|◆ Recombinant Protein|
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
Q&As (20)Ask a question
AP2B1 s belong to the chaperone family and contain several domains, the main one being the C-glycosyltransferase domain.
The main difference between AP2B1 and other molecular chaperones is that AP2B1 participates in different biological processes, and its structure and function are also different.
Recombinant AP2B1 protein may be a therapeutic target for some diseases, but further research and experimental validation are needed.
The AP2B1 exists primarily as a molecular chaperone and part of a signaling pathway in protein complexes.
The expression of recombinant AP2B1 protein is influenced by genetic and environmental factors, such as certain gene mutations, drugs, etc.
The AP2B1 is mainly located in the cytoplasm and endoplasmic reticulum.
The biological function of AP2B1 may be influenced by its expression level, but the specific details need to be further studied.
The AP2B1 is associated with a variety of diseases, including cancer, neurodegenerative diseases, and genetic diseases.
Recombinant AP2B1 protein may be involved in tumor growth and metastasis in tumor cells, but further experimental verification is needed.
The role of AP2B1 in cell proliferation and apoptosis still needs further research.
The biosynthesis of recombinant AP2B1 requires participation in multiple protein synthesis pathways, including translation, transport, shearing, modification, etc.
There are many interactions between AP2B1 and other molecules, such as protein-protein interactions, biochemical reactions, etc.
Recombinant AP2B1 protein may be involved in a variety of metabolic, signal transduction and other biological processes in genetic diseases, but the specific role needs to be further studied.
The regulatory mechanism of AP2B1 includes regulation of many signaling pathways and regulatory elements such as transcription factors.
The recombinant AP2B1 protein is a molecular chaperone involved in biological processes such as regulating internal cellular secretion pathways and endoplasmic reticulum function.
The structure, function and regulation of AP2B1 are similar to other proteins in some respects, but the specific differences need to be further studied.
AP2B1 is widely present in various tissues of the human body, including liver, lung, gastrointestinal tract, kidney and so on.
The AP2B1 may have certain research and therapeutic value for the treatment of some neurological diseases.
AP2B1 may be used as a drug, which has certain application value in tumor therapy, nerve cell protection, genetic therapy and so on.
The study of AP2B1 will be helpful in understanding the pathogenesis of the disease and developing treatments.
Customer Reviews (3)Write a review
The performance of AP2B1 recombinant protein was evaluated by measuring its functional activity in the cell, such as interaction with other proteins and efficiency of endocytosis. -
Excellent protein properties also need to be pure enough to play a role, so it is necessary to measure the purity and expression level of AP2B1 recombinant protein. -
The structural stability of proteins can be studied through spectral technology, thermodynamic experiments and other methods to see whether it is easy to denaturate or aggregate. -
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