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Monoclonal Antibody Clathrin Coat of Coated Pit

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Clathrin-coated vesicles provide for the intracellular transport of cargo proteins following endocytosis and during multiple vesicle trafficking pathways. Vesicles form at specialized areas of the cell membrane where clathrin and associated proteins form clathrin-coated pits. Invagination of these cell membrane-associated pits internalizes proteins and forms an intracellular clathrin-coated vesicle (1,2). Clathrin is the most abundant protein in these vesicles and is present as a basic assembly unit called a triskelion. Each clathrin triskelion is composed of three clathrin heavy chains and three clathrin light chains. Clathrin heavy chain proteins are composed of several functional domains, including a carboxy-terminal region that permits interaction with other heavy chain proteins within a triskelion, and a globular amino-terminal region that associates with other vesicle proteins (2). Adaptor proteins, such as AP2, epsin and EPS15, are responsible for the recruitment of vesicle proteins to sites of pit formation and the assembly of the clathrin-coated vesicle. Following vesicle invagination, the GTPase dynamin constricts the neck of the nascent vesicle to complete formation of the free, cytosolic vesicle (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Disabled homologue 2 (Dab2) is a mitogen responsive phosphoprotein that exerts multiple functions through association with numerous proteins. Dab2 modulates signaling pathways through interactions with proteins such as Smads and TGF-β receptors (1,2), axin (3), GRB (4) and Src (5). Dab2 also serves as a cargo-specific adaptor of clathrin-mediated endocytosis via interaction with clathrin (6), AP2 (7), NPXY-containing cargo (8-10), and myosin VI (11,12). In addition, Dab2 regulates cell adhesion by directly binding integrins (13,14). The diverse functions of Dab2 enable it to coordinate cell adhesion, cell motility, membrane trafficking, and signaling. Research studies have shown Dab2 is down-regulated in a number of cancers, thereby suggesting a role as a tumor suppressor (15-17). Phosphorylation of Dab2 decreases its endocytotic function (18).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: A group of related glucose transporters (Glut1-5 and 7) mediate the facilitated diffusion of glucose in nonepithelial mammalian tissues. Within insulin-responsive tissues such as muscle and fat, Glut1 contributes to basal glucose uptake while Glut4 is responsible for insulin-stimulated glucose transport (1-3). Glut4 is a 12-transmembrane domain protein that facilitates glucose transport in the direction of the glucose gradient. This transporter localizes to intracellular organelles (endosomes) in unstimulated cells and translocates to the cell surface following insulin stimulation (1,2,4). Translocation of Glut4 is dependent on Akt, which may act by phosphorylating AS160, a RabGAP protein involved in membrane trafficking (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The mTORC1 kinase complex is a critical regulator of cell growth (1,2). Its activity is modulated by enviromental factors such as energy levels, growth factors, and amino acids (3, 4). The GTPases RagA, RagB, RagC, and RagD mediate amino acid signaling to activate mTORC1 (1, 2). SH3BP4 (SH3 domain-binding protein 4) binds to the inactive Rag GTPase complex during amino acid starvation and prevents the association of Rag GTPase complex with mTORC1 resulting in the suppression of mTORC1 activation and cell growth (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Dog, Human

Application Methods: Western Blotting

Background: The myosin family of motor proteins drive ATP-dependent actin-based motility in eukaryotic cells and contain a conserved amino-terminal motor domain (reviewed in 1,2).Myosin VI is an unconventional minus-end-directed myosin involved in the transport of vesicles and organelles within the cell, endocytosis, and organelle biogenesis (3-6). The movement of myosin VI and its cargo along actin filaments is unique among myosin family members in its mechanism; its tail domain structure allows it to take larger than predicted steps along the actin filament (reviewed in 1,7).Myosin VI has been shown to regulate the polarized delivery of proteins to specialized subcellular locations, including the delivery of EGFR to the leading edge of migrating cells (8), as well as the delivery of specialized axonal proteins in neurons (9). Myosin VI has also been shown to mediate activity of the tumor suppressor p53 during DNA damage (10,11).