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Monoclonal Antibody Western Blotting Phosphatidylserine Binding

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Axl, Sky, and Mer are three members of a receptor tyrosine kinase (RTK) family that share a conserved intracellular tyrosine kinase domain and an extracellular domain similar to those seen in cell adhesion molecules. These RTKs bind the vitamin K-dependent protein growth-arrest-specific 6 (Gas6), which is structurally related to the protein S anticoagulation factor (1). Upon binding to its receptor, Gas6 activates phosphatidylinositol 3-kinase (PI3K) and its downstream targets Akt and S6K, as well as NF-κB (2,3). A large body of evidence supports a role for Gas6/Axl signaling in cell growth and survival in normal and cancer cells (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Axl, Sky, and Mer are three members of a receptor tyrosine kinase (RTK) family that share a conserved intracellular tyrosine kinase domain and an extracellular domain similar to those seen in cell adhesion molecules. These RTKs bind the vitamin K-dependent protein growth-arrest-specific 6 (Gas6), which is structurally related to the protein S anticoagulation factor (1). Upon binding to its receptor, Gas6 activates phosphatidylinositol 3-kinase (PI3K) and its downstream targets Akt and S6K, as well as NF-κB (2,3). A large body of evidence supports a role for Gas6/Axl signaling in cell growth and survival in normal and cancer cells (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Axl, Sky, and Mer are three members of a receptor tyrosine kinase (RTK) family that share a conserved intracellular tyrosine kinase domain and an extracellular domain similar to those seen in cell adhesion molecules. These RTKs bind the vitamin K-dependent protein growth-arrest-specific 6 (Gas6), which is structurally related to the protein S anticoagulation factor (1). Upon binding to its receptor, Gas6 activates phosphatidylinositol 3-kinase (PI3K) and its downstream targets Akt and S6K, as well as NF-κB (2,3). A large body of evidence supports a role for Gas6/Axl signaling in cell growth and survival in normal and cancer cells (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: GAP43 is a nervous system specific, growth-associated protein enriched in growth cones and areas of high plasticity (1). Phosphorylation of GAP43 at Ser41 by PKC is regulated by intracellular Ca2+ and affects the ability of GAP43 to bind calmodulin (2,3). GAP43 is integral to growth cone formation, neurite outgrowth, and the development of a functional cerebral cortex (4,5). Aberrant GAP43 expression can be seen in patients diagnosed with schizophrenia and Alzheimer's disease (6,7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Axl, Mer and Tyro3 are three members of the TAM family receptor tyrosine kinase that share a common NCAM (neural adhesion molecule)-related extracellular domain and a conserved intracellular tyrosine kinase domain. These receptors bind common homologous vitamin K dependent protein GAS6 and protein S to activate down stream signaling pathway (1). TAM family receptors is involved in the development of immune, nervous, vascular and reproductive systems, autoimmune disease, cancer drug resistance and tumor immunity response (2-5). Axl Tyr698, Mer Tyr749 and Tyro3 Tyr681 are conserved autophosphorylation sites located at the activation loop of the tyrosine kinase domain. Phosphorylation at these sites is required for full kinase activation of each of the corresponding receptors (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Pig

Application Methods: Western Blotting

Background: Axl, Sky, and Mer are three members of a receptor tyrosine kinase (RTK) family that share a conserved intracellular tyrosine kinase domain and an extracellular domain similar to those seen in cell adhesion molecules. These RTKs bind the vitamin K-dependent protein growth-arrest-specific 6 (Gas6), which is structurally related to the protein S anticoagulation factor (1). Upon binding to its receptor, Gas6 activates phosphatidylinositol 3-kinase (PI3K) and its downstream targets Akt and S6K, as well as NF-κB (2,3). A large body of evidence supports a role for Gas6/Axl signaling in cell growth and survival in normal and cancer cells (4).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: GAS6 (Growth Arrest Specific gene 6) is a vitamin K-dependent ligand of the TAM (Tyro3, Axl and MerTK) RTK family. It has an N-terminal Gla domain containing multiple Asp gamma-carboxylation sites, followed by four EGF repeats and two C-terminal LG domains. Vitamin K mediates multiple gamma-carboxylations of glutamic acid residues in the GAS6 Gla domain. These modifications are required for GAS6 to to activate its receptor (1,2). The two C-terminal LG (SHBG) domains form a V-shaped structure and provide a direct binding site for receptor interaction. Among the TAM family members, GAS6 has high affinity for Axl and low affinity for Tyro3 and MerTK. Ligand/receptor interaction activates multiple downstream signaling pathways such as PI3K/AKT, STAT/SOCS, PLC/FAK, and Grb2/RAS, and promotes cell survival, proliferation, migration and differentiation (3,4). GAS6 has been implicated in cancer development and immune-related disorders (inflammation and multiple sclerosis), and as such has been identified as a potential therapeutic target (3-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The adhesive glycoprotein thrombospondin-1 (THBS1, TSP1) localizes to the extracellular matrix (ECM) and mediates interactions between cells and the ECM and among cells. Thrombospondin-1 is a multi-domain, glycosylated protein that interacts with a wide variety of extracellular targets, including matrix metalloproteinases (MMPs), collagens, cell receptors, growth factors, and cytokines (1). The protein structure of THBS1 includes an amino-terminal laminin G-like domain, a von Willebrand factor-binding domain, and multiple thrombospondin (TSP) repeated sequences designated as type I, type II, or type III repeats. Each thrombospondin domain interacts with a distinct type of cell surface ligands or protein targets. The amino-terminal domain interacts with aggrecan, heparin, and integrin proteins. Type I TSP repeats interact with MMPs and CD36, while carboxy-terminal repeats bind the thrombospondin receptor CD47 (1). Through these interactions, THBS1 exerts diverse effects on different signaling pathways, such as VEGF receptor/NO signaling, TGFβ signaling, and the NF-κB pathway (2-5). Thrombospondin-1 is an important regulator of many biological processes, including cell adhesion/migration, apoptosis, angiogenesis, inflammation, vascular function, and cancer development (2-5). The activity of thrombospondin-1 is mainly regulated by extracellular proteases. The metalloproteinase ADAMTS1 cleaves thrombospondin, resulting in the release of peptides with anti-angiogenic properties. Elastase and plasmin proteases degrade the THBS1 protein and down regulate its activity (6). As THBS1 is an important protein inhibitor of angiogenesis, the development of thrombospondin-based compounds and their use in therapeutic studies may provide a beneficial approach to the treatment of cancer (7,8).

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

Application Methods: Western Blotting

Background: Glutamate oxaloacetate transaminase 1 (GOT1) catalyzes the interconversion of aspartate and oxaloacetate (1). The increased transamination primarily catalyzed by GOT1 leads to elevated levels of 2-hydroxyglutarate, which promotes methylation of the Foxp3 gene locus, inhibits Foxp3 expression and activates T helper 17 (TH17) cell differentiation (2). In addition, GOT1 is critical to the survival of cells with electron transport chain inhibition by generating aspartate, a metabolite determining the proliferation of these cells (3-4). Studies also show that GOT1 plays a key role in the noncanonical glutamine pathway that supports liver tumorigenesis (5).