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Rat Endosome Organization and Biogenesis

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: CHMP2B is a component of the ESCRT III (endosomal sorting required for transport complex III) complex (1, 2). The ESCRT system is composed of the ESCRT-0, -I, -II, and -III complexes, which function sequentially to direct the transport of ubiquitinated transmembrane proteins into the intralumenal vesicles (ILVs), which will eventually mature into multivesicular bodies (MVBs). CHMP2B is a homolog of yeast Vps2, which functions in the ESCRT-II complex to change the initial spiral-structure of snf7 into membrane-sculpting helices for the final pinch off process (3). CHMP2B probably functions similarly in mammalian cells. Research studies show that manipulation of the ESCRT-III complex leads to accumulation of CHMP2B at the plasma membrane and overexpressed CHMP2B polymerizes into a tight helical structure that deforms the shape of associated plasma membrane (4).Research studies have shown that mutation of CHMP2B is associated with frontotemporal dementia, (5, 6). Studies have further shown that the dysfunction of mutant CHMP2B expression may disrupts the normal endo-autophagosome and endo-lysosome pathways and lead to neurodegenerative diseases (6-9).

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

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

Background: mTORC1 kinase complex is a critical component in the regulation of cell growth (1,2). Its activity is modulated by energy levels, growth factors, and amino acids (3,4). The four related GTPases, RagA, RagB, RagC, and RagD, have been shown to interact with raptor in mTORC1 (1,2). These interactions are both necessary and sufficient for mTORC1 activation in response to amino acid signals (1,2). A protein complex consisting of LAMTOR1/C11orf59, LAMTOR2/ROBLD3, and LAMTOR3/MAPKSP1 has been identified to interact with and recruit the four Rag GTPases to the surface of lysosomes (5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Three distinct types of phosphoinositide 3-kinases (PI3K) have been characterized. Unlike other PI3Ks, PI3K class III catalyzes the phosphorylation of phosphatidylinositol at the D3 position, producing phosphatidylinositol-3-phosphate (PIP3) (1). PI3K class III is the mammalian homolog of Vps34, first identified in yeast. PI3K class III interacts with the regular subunit p150, the mammalian homolog of Vps15, which regulates cellular membrane association through myristoylation (2,3). PIP3 recruits several proteins with FYVE or PX domains to membranes regulating vesicular transport and protein sorting (4). Moreover, PI3K class III has been shown to regulate autophagy, trimeric G-protein signaling, and the mTOR nutrient-sensing pathway (5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Three distinct types of phosphoinositide 3-kinases (PI3K) have been characterized. Unlike other PI3Ks, PI3K class III catalyzes the phosphorylation of phosphatidylinositol at the D3 position, producing phosphatidylinositol-3-phosphate (PIP3) (1). PI3K class III is the mammalian homolog of Vps34, first identified in yeast. PI3K class III interacts with the regular subunit p150, the mammalian homolog of Vps15, which regulates cellular membrane association through myristoylation (2,3). PIP3 recruits several proteins with FYVE or PX domains to membranes regulating vesicular transport and protein sorting (4). Moreover, PI3K class III has been shown to regulate autophagy, trimeric G-protein signaling, and the mTOR nutrient-sensing pathway (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Three distinct types of phosphoinositide 3-kinases (PI3K) have been characterized. Unlike other PI3Ks, PI3K class III catalyzes the phosphorylation of phosphatidylinositol at the D3 position, producing phosphatidylinositol-3-phosphate (PIP3) (1). PI3K class III is the mammalian homolog of Vps34, first identified in yeast. PI3K class III interacts with the regular subunit p150, the mammalian homolog of Vps15, which regulates cellular membrane association through myristoylation (2,3). PIP3 recruits several proteins with FYVE or PX domains to membranes regulating vesicular transport and protein sorting (4). Moreover, PI3K class III has been shown to regulate autophagy, trimeric G-protein signaling, and the mTOR nutrient-sensing pathway (5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Syntaxin 6 is a ubiquitously expressed S25C family member of the SNARE proteins (1,2). The protein has an amino-terminal H1 domain followed by an H2 SNARE domain and a carboxy-terminal membrane anchor (3). Syntaxin 6 protein is localized to the trans-Golgi and within endosomes and regulates membrane trafficking by partnering with a variety of other SNARE proteins (3-5). Depending on cell type and SNARE parter, syntaxin 6 is involved in the regulation of GLUT4 trafficking, neutrophil exocytosis and granule secretion (6-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Dynamin is a family of large GTPases that has been implicated in the formation of vesicles of both the endocytotic and secretory processes (1). Dynamin plays an important role in the internalization of cell surface receptors, a process that attenuates the response to extracellular signals. It has been illustrated that dynamin interacts with signaling proteins such as Src, PLCγ, PKC and G-proteins. PKC and Src phosphorylate dynamin, and its phosphorylation may regulate the endocytosis of cell surface receptors (2,3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Dynamin is a family of large GTPases that has been implicated in the formation of vesicles of both the endocytotic and secretory processes (1). Dynamin plays an important role in the internalization of cell surface receptors, a process that attenuates the response to extracellular signals. It has been illustrated that dynamin interacts with signaling proteins such as Src, PLCγ, PKC and G-proteins. PKC and Src phosphorylate dynamin, and its phosphorylation may regulate the endocytosis of cell surface receptors (2,3).

$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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Huntington's Disease (HD) is a fatal neurodegenerative disorder characterized by psychiatric, cognitive, and motor dysfunction. Neuropathology of HD involves specific neuronal subpopulations: GABA-ergic neurons of the striatum and neurons within the cerebral cortex selectively degenerate (1,2). The genetic analysis of HD has been the flagship study of inherited neurological diseases from initial chromosomal localization to identification of the gene.Huntingtin is a large (340-350 kD) cytosolic protein that may be involved in a number of cellular functions such as transcription, gastrulation, neurogenesis, neurotransmission, axonal transport, neural positioning, and apoptosis (2,3). The HD gene from unaffected individuals contains between 6 and 34 CAG trinucleotide repeats, with expansion beyond this range causing the onset of disease symptoms. A strong inverse correlation exists between the age of onset in patients and the number of huntingtin gene CAG repeats encoding a stretch of polyglutamine peptides (1,2). The huntingtin protein undergoes numerous post-translational modifications including phosphorylation, ubiquitination, sumoylation, palmitoylation, and cleavage (2). Phosphorylation of Ser421 by Akt can partially counteract the toxicity that results from the expanded polyglutamine tract. Varying Akt expression in the brain correlates with regional differences in huntingtin protein phosphorylation; this pattern inversely correlates with the regions that are most affected by degeneration in diseased brain (2). A key step in the disease is the proteolytic cleavage of huntingtin protein into amino-terminal fragments that contain expanded glutamine repeats and translocate into the nucleus. Caspase mediated cleavage of huntingtin at Asp513 is associated with increased polyglutamine aggregate formation and toxicity. Phosphorylation of Ser434 by CDK5 protects against cleavage (2,3).

$293
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Huntington's Disease (HD) is a fatal neurodegenerative disorder characterized by psychiatric, cognitive, and motor dysfunction. Neuropathology of HD involves specific neuronal subpopulations: GABA-ergic neurons of the striatum and neurons within the cerebral cortex selectively degenerate (1,2). The genetic analysis of HD has been the flagship study of inherited neurological diseases from initial chromosomal localization to identification of the gene.Huntingtin is a large (340-350 kD) cytosolic protein that may be involved in a number of cellular functions such as transcription, gastrulation, neurogenesis, neurotransmission, axonal transport, neural positioning, and apoptosis (2,3). The HD gene from unaffected individuals contains between 6 and 34 CAG trinucleotide repeats, with expansion beyond this range causing the onset of disease symptoms. A strong inverse correlation exists between the age of onset in patients and the number of huntingtin gene CAG repeats encoding a stretch of polyglutamine peptides (1,2). The huntingtin protein undergoes numerous post-translational modifications including phosphorylation, ubiquitination, sumoylation, palmitoylation, and cleavage (2). Phosphorylation of Ser421 by Akt can partially counteract the toxicity that results from the expanded polyglutamine tract. Varying Akt expression in the brain correlates with regional differences in huntingtin protein phosphorylation; this pattern inversely correlates with the regions that are most affected by degeneration in diseased brain (2). A key step in the disease is the proteolytic cleavage of huntingtin protein into amino-terminal fragments that contain expanded glutamine repeats and translocate into the nucleus. Caspase mediated cleavage of huntingtin at Asp513 is associated with increased polyglutamine aggregate formation and toxicity. Phosphorylation of Ser434 by CDK5 protects against cleavage (2,3).

$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, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: CHMP4B, the human homologue of yeast Snf7, interacts with Alix and is a core component of the ESCRT-III complex (endosomal sorting for transport complex III) (1,2). The ESCRT system is comprised of multiple protein complexes denoted as ESCRT-0, -I, -II, -III, and VPS4 ATPase that together contribute to a number of membrane fission events, including multivesicular body (MVB) and exosome formulation, viral budding, abscission during cytokinesis, and plasma membrane repair (3,4). Interestingly, it was found that the ESCRT-III complex, including CHMP4B is recruited to the plasma membrane during the regulated process of necrosis, necroptosis, and thereby controls membrane integrity sustaining these cells and allowing continued signaling and cytokine/chemokine secretion (5). Elevated expression of CHMP4B has been associated with neuronal apoptosis following intracerebral hemorrhage (6). In addition, high CHMP4B expression was associated with increased proliferation and resistance to doxorubicin in hepatocellular carcinoma (7).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of proteins activated in response to nutrient deprivation and in neurodegenerative conditions (1). One of the proteins critical to this process is Beclin-1, the mammalian orthologue of the yeast autophagy protein Apg6/Vps30 (2). Beclin-1 can complement defects in yeast autophagy caused by loss of Apg6 and can also stimulate autophagy when overexpressed in mammalian cells (3). Mammalian Beclin-1 was originally isolated in a yeast two-hybrid screen for Bcl-2 interacting proteins and has been shown to interact with Bcl-2 and Bcl-xL, but not with Bax or Bak (4). While Beclin-1 is generally ubiquitously expressed, research studies have shown it is monoallelically deleted in 40-75% of sporadic human breast and ovarian cancers (5). Beclin-1 is localized within cytoplasmic structures including the mitochondria, although overexpression of Beclin-1 reveals some nuclear staining and CRM1-dependent nuclear export (6). Investigators have demonstrated that Beclin-1-/- mice die early in embryogenesis and Beclin-1-/+ mice have a high incidence of spontaneous tumors. Stem cells from the null mice demonstrate an altered autophagic response, although responses to apoptosis appeared normal (7). Researchers have also found that overexpression of Beclin-1 in virally infected neurons in vivo resulted in significant protection against Sindbis virus-induced disease and neuronal apoptosis (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of proteins activated in response to nutrient deprivation and in neurodegenerative conditions (1). One of the proteins critical to this process is Beclin-1, the mammalian orthologue of the yeast autophagy protein Apg6/Vps30 (2). Beclin-1 can complement defects in yeast autophagy caused by loss of Apg6 and can also stimulate autophagy when overexpressed in mammalian cells (3). Mammalian Beclin-1 was originally isolated in a yeast two-hybrid screen for Bcl-2 interacting proteins and has been shown to interact with Bcl-2 and Bcl-xL, but not with Bax or Bak (4). While Beclin-1 is generally ubiquitously expressed, research studies have shown it is monoallelically deleted in 40-75% of sporadic human breast and ovarian cancers (5). Beclin-1 is localized within cytoplasmic structures including the mitochondria, although overexpression of Beclin-1 reveals some nuclear staining and CRM1-dependent nuclear export (6). Investigators have demonstrated that Beclin-1-/- mice die early in embryogenesis and Beclin-1-/+ mice have a high incidence of spontaneous tumors. Stem cells from the null mice demonstrate an altered autophagic response, although responses to apoptosis appeared normal (7). Researchers have also found that overexpression of Beclin-1 in virally infected neurons in vivo resulted in significant protection against Sindbis virus-induced disease and neuronal apoptosis (4).

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

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

Background: Eps15 (EGFR pathway substrate 15) was originally discovered as a substrate for the kinase activity of EGFR (1). Eps15 has a tripartite structure comprising an amino terminal portion, which contains three evolutionarily conserved EH protein-protein interaction domains, a central putative coiled-coil region required for constitutive oligmerization, and a carboxy terminal domain containing multiple copies of the amino acid triplet Asp-Pro-Phe that constitute the AP2 binding domain. The carboxy terminal domain also contains two ubiquitin interaction motifs (UIMs), the last of which is indespensible for Eps15 binding to ubiquitin (1). Several lines of evidence support a role for Eps15 in clathrin-mediated endocytosis, including the endocytosis of synaptic vesicles. Eps15 binds to AP2 as well as other proteins involved in endocytosis and/or synaptic vesicle recycling, such as synaptojanin1 and epsin. Furthermore, Eps15 colocalizes with markers of the plasma membrane clathrin-coated pits and vesicles (2). Eps15 regulates the endosomal trafficking of c-Met (3) and EGFR (4), possibly by recruiting the ubiquitinated receptors to the rims of clathrin-coated pits through interaction between the ubiquitin tag and its UIMs.The EPS15 gene yields two isoforms that are believed to reside in distinct subcellular locations and are thus implicated in different facets of endosomal trafficking (5). Human EPS15 has been mapped to chromosome 1p31-p32, a region displaying several nonrandom chromosomal abnormalities, including deletions in neuroblastoma and translocations in acute lymphoblastic and myeloid leukemias. Research has shown two translocations t(1;11)(p32;q11) are found in rare cases of myeloid leukemia where the Eps15 gene was fused to the HRX gene, resulting in two reciprocal fusion genes (6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Cytoplasmic dynein is a multi-subunit motor complex that regulates microtubule organization as well as the transport and positioning of organelles. Dynactin is a multi-subunit dynein-activating complex, which regulates the interaction of the dynein motor with various cellular cargoes, and enhances dynein’s processivity. p150Glued/DCTN1/Dynactin 1 is the largest subunit of the dynactin complex (1-3). In mitosis, cytoplasmic dynein regulates spindle organization, chromosome movement and centrosome separation (4). The dynactin subunit p150Glued is phosphorylated at serine 19 by the mitotic kinase aurora A during anaphase, and this phosphorylation is required for the appropriate regulation of spindle assembly (5). In neurons, axonal transport is important for cellular function and survival. Dysfunction and mutations in dynein and dynactin subunits, including p150Glued, have been linked to human neurodegenerative diseases such as Alzheimer’s Disease (6-7), Perry Syndrome (8) and ALS (9).