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Human Establishment of Vesicle Localization

$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).

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

Application Methods: Western Blotting

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

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

Application Methods: Western Blotting

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state, complexed with the inhibitory IκB proteins (1-3). Most agents that activate NF-κB do so through a common pathway based on phosphorylation-induced, proteasome-mediated degradation of IκB (3-7). The key regulatory step in this pathway involves activation of a high molecular weight IκB kinase (IKK) complex whose catalysis is generally carried out by three tightly associated IKK subunits. IKKα and IKKβ serve as the catalytic subunits of the kinase and IKKγ serves as the regulatory subunit (8,9). Activation of IKK depends upon phosphorylation at Ser177 and Ser181 in the activation loop of IKKβ (Ser176 and Ser180 in IKKα), which causes conformational changes, resulting in kinase activation (10-13).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Postsynaptic Density protein 95 (PSD95) is a member of the membrane-associated guanylate kinase (MAGUK) family of proteins. These family members consist of an amino-terminal variable segment followed by three PDZ domains, a SH3 domain, and an inactive guanylate kinase (GK) domain. PSD95 is a scaffolding protein involved in the assembly and function of the postsynaptic density complex (1-2). PSD95 participates in synaptic targeting of AMPA receptors through an indirect manner involving Stargazin and related transmembrane AMPA receptor regulatory proteins (TARPs) (3). It is implicated in experience-dependent plasticity and plays an indispensable role in learning (4). Mutations in PSD95 are associated with autism (5).

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

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: Postsynaptic Density protein 95 (PSD95) is a member of the membrane-associated guanylate kinase (MAGUK) family of proteins. These family members consist of an amino-terminal variable segment followed by three PDZ domains, a SH3 domain, and an inactive guanylate kinase (GK) domain. PSD95 is a scaffolding protein involved in the assembly and function of the postsynaptic density complex (1-2). PSD95 participates in synaptic targeting of AMPA receptors through an indirect manner involving Stargazin and related transmembrane AMPA receptor regulatory proteins (TARPs) (3). It is implicated in experience-dependent plasticity and plays an indispensable role in learning (4). Mutations in PSD95 are associated with autism (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Postsynaptic Density protein 95 (PSD95) is a member of the membrane-associated guanylate kinase (MAGUK) family of proteins. These family members consist of an amino-terminal variable segment followed by three PDZ domains, a SH3 domain, and an inactive guanylate kinase (GK) domain. PSD95 is a scaffolding protein involved in the assembly and function of the postsynaptic density complex (1-2). PSD95 participates in synaptic targeting of AMPA receptors through an indirect manner involving Stargazin and related transmembrane AMPA receptor regulatory proteins (TARPs) (3). It is implicated in experience-dependent plasticity and plays an indispensable role in learning (4). Mutations in PSD95 are associated with autism (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Postsynaptic Density protein 95 (PSD95) is a member of the membrane-associated guanylate kinase (MAGUK) family of proteins. These family members consist of an amino-terminal variable segment followed by three PDZ domains, a SH3 domain, and an inactive guanylate kinase (GK) domain. PSD95 is a scaffolding protein involved in the assembly and function of the postsynaptic density complex (1-2). PSD95 participates in synaptic targeting of AMPA receptors through an indirect manner involving Stargazin and related transmembrane AMPA receptor regulatory proteins (TARPs) (3). It is implicated in experience-dependent plasticity and plays an indispensable role in learning (4). Mutations in PSD95 are associated with autism (5).

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

Application Methods: Western Blotting

Background: LIS1 is a cytoskeleton-interacting protein that contains an N-terminal dimerization domain and a C-terminal β-propeller domain that interacts with the motor domain of dynein (1-3). Research studies have shown that mutations in the LIS1 gene are involved in lissencephaly, a disease characterized by severe defects in brain development (4). LIS1 also plays a critical role in cortical migration and development in the brain (5). LIS1 activity is required for retrograde translocation of excitatory synapses in developing interneuron dendrites in a microtubule-dependent fashion (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Postsynaptic Density protein 95 (PSD95) is a member of the membrane-associated guanylate kinase (MAGUK) family of proteins. These family members consist of an amino-terminal variable segment followed by three PDZ domains, a SH3 domain, and an inactive guanylate kinase (GK) domain. PSD95 is a scaffolding protein involved in the assembly and function of the postsynaptic density complex (1-2). PSD95 participates in synaptic targeting of AMPA receptors through an indirect manner involving Stargazin and related transmembrane AMPA receptor regulatory proteins (TARPs) (3). It is implicated in experience-dependent plasticity and plays an indispensable role in learning (4). Mutations in PSD95 are associated with autism (5).

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

Application Methods: Western Blotting

Background: Valosin-containing protein (VCP) is a highly conserved and abundant 97 kDa protein that belongs to the AAA (ATPase associated with a variety of cellular activities) family of proteins. VCP assembles as a homo-hexamer, forming a ring with a channel at its center (1,2,3). VCP homo-hexamers associate with a variety of protein cofactors to form many distinct protein complexes, which act as chaperones to unfold proteins and transport them to specific cellular compartments or to the proteosome (4). These protein complexes participate in many cellular functions, including vesicle transport and fusion, fragmentation and reassembly of the golgi stacks during mitosis, nuclear envelope formation and spindle disassembly following mitosis, cell cycle regulation, DNA damage repair, apoptosis, B- and T-cell activation, NF-κB-mediated transcriptional regulation, endoplasmic reticulum (ER)-associated degradation and protein degradation (4). VCP appears to localize mainly to the endoplasmic reticulum; however, tyrosine phosphorylation is associated with relocalization to the centrosome during mitosis (5). In addition, following cellular exposure to ionizing radition, VCP is phosphorylated at Ser784 in an ATM-dependent manner and accumulates in the nucleus at sites of double-stranded DNA breaks (DSBs) (6). Exposure to other types of DNA damaging agents such as UV light, bleomycin or doxorubicin results in phosphorylation of VCP by ATR and DNA-PK in an ATM-independent manner (6).

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

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Valosin-containing protein (VCP) is a highly conserved and abundant 97 kDa protein that belongs to the AAA (ATPase associated with a variety of cellular activities) family of proteins. VCP assembles as a homo-hexamer, forming a ring with a channel at its center (1,2,3). VCP homo-hexamers associate with a variety of protein cofactors to form many distinct protein complexes, which act as chaperones to unfold proteins and transport them to specific cellular compartments or to the proteosome (4). These protein complexes participate in many cellular functions, including vesicle transport and fusion, fragmentation and reassembly of the golgi stacks during mitosis, nuclear envelope formation and spindle disassembly following mitosis, cell cycle regulation, DNA damage repair, apoptosis, B- and T-cell activation, NF-κB-mediated transcriptional regulation, endoplasmic reticulum (ER)-associated degradation and protein degradation (4). VCP appears to localize mainly to the endoplasmic reticulum; however, tyrosine phosphorylation is associated with relocalization to the centrosome during mitosis (5). In addition, following cellular exposure to ionizing radition, VCP is phosphorylated at Ser784 in an ATM-dependent manner and accumulates in the nucleus at sites of double-stranded DNA breaks (DSBs) (6). Exposure to other types of DNA damaging agents such as UV light, bleomycin or doxorubicin results in phosphorylation of VCP by ATR and DNA-PK in an ATM-independent manner (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Scribble (Scrib) was originally identified in a genetic screen in Drosophila along with cell polarity determinants Discs Large (Dlg) and Lethal giant larvae (Lgl). Drosophila mutants homozygous for these genes share similar phenotypes, including the loss of apicobasal cell polarity and neoplastic tissue overgrowth. These phenotypic similarities suggest that these three proteins function in a common pathway important for establishing and maintaining apicobasal polarity in epithelial cells (1,2). Scribble contains many leucine-rich repeats and PDZ domains important for localizing scribble to adherens junctions and basolateral regions of mammalian epithelial cells (3). Scribble reportedly binds β-catenin, APC, E-cadherin and the E6 protein from high-risk virus type of HPV through a short motif important for E6-induced cell transformation (4-8). Overexpression of scribble inhibits transformation of rodent epithelial cells by HPV E6/7 proteins (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Scribble (Scrib) was originally identified in a genetic screen in Drosophila along with cell polarity determinants Discs Large (Dlg) and Lethal giant larvae (Lgl). Drosophila mutants homozygous for these genes share similar phenotypes, including the loss of apicobasal cell polarity and neoplastic tissue overgrowth. These phenotypic similarities suggest that these three proteins function in a common pathway important for establishing and maintaining apicobasal polarity in epithelial cells (1,2). Scribble contains many leucine-rich repeats and PDZ domains important for localizing scribble to adherens junctions and basolateral regions of mammalian epithelial cells (3). Scribble reportedly binds β-catenin, APC, E-cadherin and the E6 protein from high-risk virus type of HPV through a short motif important for E6-induced cell transformation (4-8). Overexpression of scribble inhibits transformation of rodent epithelial cells by HPV E6/7 proteins (8).