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Monoclonal Antibody Immunofluorescence Immunocytochemistry Lipid Binding

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

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

Background: Triacylglycerol is stored in lipid droplets as a primary energy reserve. Perilipin is localized at the periphery of lipid droplets and serves as a protective coating against lipases (1-3). Evidence suggests that PKA regulates lipolysis by phosphorylating perilipin (1,2,4,5). Phosphorylation of perilipin results in the conformational change that exposes lipid droplets to endogenous lipases, such as hormone-sensitive lipases (2). Hence, perilipin plays a pivotal role in lipid storage (2,5).

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

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

Background: Cyclooxygenase1 (Cox1) and cyclooxygenase2 (Cox2), family members with 60% homology in humans, catalyze prostaglandin production from arachidonic acid (1,2). While Cox1 expression is constitutive in most tissues, Cox2 expression is induced by lipopolysaccharide (LPS) and peptidoglycan (PGN) (3). PGN activates Ras, leading to phosphorylation of Raf at Ser338 and Erk1/2 at Tyr204. The activation of MAP kinase signaling results in subsequent activation of IKKα/β, phosphorylation of IκBα at Ser32/36, and NF-κB activation. Finally, activation of the transcription factor NF-κB is responsible for the induction of Cox2 expression (4). Investigators have shown that LPS and PGN induce the clinical manifestations of arthritis and bacterial infections, such as inflammation, fever, and septic shock (5). Research studies have indicated that Cox1 and Cox2 may also play a role in the neuropathology of Alzheimer's disease by potentiating γ-secretase activity and β-amyloid generation (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Fatty acid binding proteins (FABPs) bind to fatty acids and other lipids to function as cytoplasmic lipid chaperones (1). They participate in the transport of fatty acids and other lipids to various cellular pathways (2). Differential expression of FABPs is found in several types of tumors and their normal-cell counterparts (3). FABP7 is abundantly expressed in fetal brain and may be essential for development (4). Expression is required for the establishment of the radial glial fiber system, a system that is necessary for the development of cortical layers (5). Increased expression of FABP7 is associated with reduced survival in patients with glioblastoma (6), and is also found in glial cells following nerve injury (7). Investigators have found loss of FABP7 may be involved in the development and progression of breast cancer and expression of FABP7 has been shown to induce mammary differentiation and to inhibit growth of breast cancer cells (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: Endophilin proteins are part of a large family of Bin/Amphiphysin/Rvs (BAR) domain proteins that are involved in cell membrane remodeling (1). The endophilins are encoded by five genes, which produce endophilin A 1-3 and B 1-2 (2). Endophilins are involved in many cellular mechanisms, such as synaptic vesicle recycling, receptor trafficking, and membrane remodeling processes (2). Research studies indicate that endophilin 1 (endophilin A1, SH3GL2) can induce different membrane shapes (3) and participate in the morphogenesis of dendritic spines (4). Endophilin 1 is also involved in regulating blood brain barrier permeability via the EGFR-JNK pathway (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Dynamin-related protein 1 (DRP1) is a member of the dynamin superfamily of GTPases. Members of this family have diverse cellular functions including vesicle scission, organelle fission, viral resistance, and intracellular trafficking (reviewed in 1). DRP1 affects mitochondrial morphology and is important in mitochondrial and peroxisomal fission in mammalian cells (2-5). The yeast ortholog of DRP1 clusters into a spiral-shaped structure on the mitochondrial membrane at the site of fission (reviewed in 6), and this structure is likely conserved in mammalian cells (3). The division of the mitochondria, which is required for apoptosis, as well as normal cell growth and development is controlled, in part, by the phosphorylation of DRP1 at Ser616 by Cdk1/cyclin B and at Ser637 by protein kinase A (PKA) (reviewed in 6). When phosphorylated at Ser616, DRP1 stimulates mitochondrial fission during mitosis. Conversely, fission is inhibited when DRP1 is phosphorylated at Ser637 (reviewed in 6). Dephosphorylation at Ser637 by calcineurin reverses this inhibition (7). In addition to phosphorylation, sumoylation of DRP1 is also an enhancer of mitochondrial fission (8). Balancing fission and fusion events is essential for proper mitochondrial function. Research studies have demonstrated mitochondrial defects in a variety of neurodegenerative diseases including Alzheimer’s disease, Parkinson’s disease, and Huntington’s disease (reviewed in 6).

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

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

Background: Dynamin-related protein 1 (DRP1) is a member of the dynamin superfamily of GTPases. Members of this family have diverse cellular functions including vesicle scission, organelle fission, viral resistance, and intracellular trafficking (reviewed in 1). DRP1 affects mitochondrial morphology and is important in mitochondrial and peroxisomal fission in mammalian cells (2-5). The yeast ortholog of DRP1 clusters into a spiral-shaped structure on the mitochondrial membrane at the site of fission (reviewed in 6), and this structure is likely conserved in mammalian cells (3). The division of the mitochondria, which is required for apoptosis, as well as normal cell growth and development is controlled, in part, by the phosphorylation of DRP1 at Ser616 by Cdk1/cyclin B and at Ser637 by protein kinase A (PKA) (reviewed in 6). When phosphorylated at Ser616, DRP1 stimulates mitochondrial fission during mitosis. Conversely, fission is inhibited when DRP1 is phosphorylated at Ser637 (reviewed in 6). Dephosphorylation at Ser637 by calcineurin reverses this inhibition (7). In addition to phosphorylation, sumoylation of DRP1 is also an enhancer of mitochondrial fission (8). Balancing fission and fusion events is essential for proper mitochondrial function. Research studies have demonstrated mitochondrial defects in a variety of neurodegenerative diseases including Alzheimer’s disease, Parkinson’s disease, and Huntington’s disease (reviewed in 6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The AP-2 coat assembly protein complex is an important component of clathrin-coated pits involved in receptor-mediated endocytosis at the plasma membrane (1-3). Each AP-2 heterotetramer is composed of α, β, μ, and σ protein subunits. The 50 kDa μ subunit (AP-2μ, AP2M1) is located at the core of the AP-2 complex and mediates interaction between the cargo protein and the clathrin-coated pit (1-4). The carboxy-terminal AP2M1 region recognizes the tyrosine-based, endocytotic sorting motif YXXφ found in cargo proteins and helps to bring the cargo protein to the clathrin-coated pit. Non-canonical, tyrosine-based endocytotic sorting signals can also promote interaction between cargo proteins and AP2M1 (5,6). AP2M1 plays an essential role in molecular signaling as it couples receptor-mediated endocytosis and pathways involving membrane receptors (7-9), matrix metalloproteinases (10), and ion channel proteins (11). Phosphorylation of specific AP2M1 residues and binding of lipids to this adaptor protein can regulate AP2M1 activity (12,13). Phosphorylation of AP2M1 at Thr156 by adaptor-associated kinase 1 (AAK1) stimulates affinity binding of AP2M1 to cargo protein signals (14).