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Mouse Trans-Golgi Network Transport Vesicle

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Insulin-like growth factor II (IGF-II) receptor, also widely known as cation-independent mannose 6-phosphate receptor (CI-M6PR), is a multifunctional type I transmembrane glycoprotein that participates in the internalization of mannose-6-phosphate modified hydrolases and IGF-II from the plasma membrane (1,2). In the absence of ligands, IGF-II receptor is constitutively endocytosed from the cell surface to accumulate in the Golgi apparatus (3). In the presence of ligands, the receptor transports the mannose-6-phosphate modified hydrolases to acidified endosomes and lysosomes (4). The ligand-free receptor is then transported back to the Golgi compartment or the cell surface (4). In several research studies, IGF-II receptor has been recognized as a tumor suppressor in a number of cancers (5-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: Insulin-like growth factor II (IGF-II) receptor, also widely known as cation-independent mannose 6-phosphate receptor (CI-M6PR), is a multifunctional type I transmembrane glycoprotein that participates in the internalization of mannose-6-phosphate modified hydrolases and IGF-II from the plasma membrane (1,2). In the absence of ligands, IGF-II receptor is constitutively endocytosed from the cell surface to accumulate in the Golgi apparatus (3). In the presence of ligands, the receptor transports the mannose-6-phosphate modified hydrolases to acidified endosomes and lysosomes (4). The ligand-free receptor is then transported back to the Golgi compartment or the cell surface (4). In several research studies, IGF-II receptor has been recognized as a tumor suppressor in a number of cancers (5-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Western Blotting

Background: TMP21, a type I transmembrane protein, is a member of the p24 cargo protein family, which is highly enriched in the ER, the Golgi and coat protein (COP) I and II transport vesicles (1,2). TMP21 is involved in protein transport and vesicular targeting. In particular, TMP21 influences APP trafficking by stabilizing nascent APP. The absence of TMP21 leads to enhanced maturation and cell surface accumulation of APP (3). In addition, TMP21 is a non-essential component of the γ-secretase complex with the potential to modulate γ-secretase mediated cleavage and Aβ production without having an effect on ε-secretase activity (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Rab11a, Rab11b and Rab25 are members of the Rab11 family of small Ras-like GTPases. Rab11 (isoforms Rab11a and Rab11b) functions as a key regulator in the recycling of perinuclear, plasma membrane and Golgi compartment endosomes (1,2). Despite some overlap, distinct differences exist between Rab11a and Rab11b in both their cellular distribution and functional roles. Rab11a is ubiquitously expressed while Rab11b is found mainly in the heart and brain (3,4). Like other Rab proteins, Rab11 exerts its function via interactions with Rab11 family interacting proteins (FIPs). While there are three distinct classes of FIPs, all appear to share a conserved carboxy-terminal Rab-binding domain that allows Rab-FIP protein interaction. When bound together, these proteins are thought to regulate membrane-associated protein sorting (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Rab11a, Rab11b and Rab25 are members of the Rab11 family of small Ras-like GTPases. Rab11 (isoforms Rab11a and Rab11b) functions as a key regulator in the recycling of perinuclear, plasma membrane and Golgi compartment endosomes (1,2). Despite some overlap, distinct differences exist between Rab11a and Rab11b in both their cellular distribution and functional roles. Rab11a is ubiquitously expressed while Rab11b is found mainly in the heart and brain (3,4). Like other Rab proteins, Rab11 exerts its function via interactions with Rab11 family interacting proteins (FIPs). While there are three distinct classes of FIPs, all appear to share a conserved carboxy-terminal Rab-binding domain that allows Rab-FIP protein interaction. When bound together, these proteins are thought to regulate membrane-associated protein sorting (5,6).

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

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

Background: Rab11a, Rab11b and Rab25 are members of the Rab11 family of small Ras-like GTPases. Rab11 (isoforms Rab11a and Rab11b) functions as a key regulator in the recycling of perinuclear, plasma membrane and Golgi compartment endosomes (1,2). Despite some overlap, distinct differences exist between Rab11a and Rab11b in both their cellular distribution and functional roles. Rab11a is ubiquitously expressed while Rab11b is found mainly in the heart and brain (3,4). Like other Rab proteins, Rab11 exerts its function via interactions with Rab11 family interacting proteins (FIPs). While there are three distinct classes of FIPs, all appear to share a conserved carboxy-terminal Rab-binding domain that allows Rab-FIP protein interaction. When bound together, these proteins are thought to regulate membrane-associated protein sorting (5,6).

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

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

Background: The Rab8 GTPase is a member of the Ras superfamily that functions in protein transport and membrane restructuring (1). Studies show that Rab8 is localized to the trans Golgi network (TGN), basolateral membrane, and vesicular structures where it helps regulate target protein transport between TGN and the basolateral membrane (1-3). Overexpression studies and mutation analysis of Rab8 and its associated Rab8GEF indicate additional roles in actin and microtubule remodeling during polarized membrane transport and membrane protrusion formation (4-6). Rab8 associates with myosin Vb and is required for translocation of GLUT4 following insulin stimulation in muscle (7,8). Control of target protein vesicle transport by Rab8 also regulates MT1-MMP activity during extracellular matrix formation and JRAB/MICAL-L2 at tight junction formation (9,10).

$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, Mouse, Rat

Application Methods: Western Blotting

Background: Amyloid β (Aβ) precursor protein (APP) is a 100-140 kDa transmembrane glycoprotein that exists as several isoforms (1). The amino acid sequence of APP contains the amyloid domain, which can be released by a two-step proteolytic cleavage (1). The extracellular deposition and accumulation of the released Aβ fragments form the main components of amyloid plaques in Alzheimer's disease (1). APP can be phosphorylated at several sites, which may affect the proteolytic processing and secretion of this protein (2-5). Phosphorylation at Thr668 (a position corresponding to the APP695 isoform) by cyclin-dependent kinase is cell-cycle dependent and peaks during G2/M phase (4). APP phosphorylated at Thr668 exists in adult rat brain and correlates with cultured neuronal differentiation (5,6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Amyloid β (Aβ) precursor protein (APP) is a 100-140 kDa transmembrane glycoprotein that exists as several isoforms (1). The amino acid sequence of APP contains the amyloid domain, which can be released by a two-step proteolytic cleavage (1). The extracellular deposition and accumulation of the released Aβ fragments form the main components of amyloid plaques in Alzheimer's disease (1). APP can be phosphorylated at several sites, which may affect the proteolytic processing and secretion of this protein (2-5). Phosphorylation at Thr668 (a position corresponding to the APP695 isoform) by cyclin-dependent kinase is cell-cycle dependent and peaks during G2/M phase (4). APP phosphorylated at Thr668 exists in adult rat brain and correlates with cultured neuronal differentiation (5,6).