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Monoclonal Antibody Western Blotting Forebrain Cell Migration

$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 downstream signaling pathways (1). TAM family receptors are involved in the development of immune, nervous, vascular and reproductive systems, autoimmune disease, cancer drug resistance and tumor immunity response (2-5). Axl (Tyr698), Axl (Tyr702), Mer Tyr(749) and Tyro3 (Tyr681) are conserved autophosphorylation sites located in the activation loop of the respective tyrosine kinase domains. 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

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).

$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, 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, 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).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Tyro3 is a receptor tyrosine kinase belonging to the TAM subfamily (Tyro3, Axl and Mer). All three members have similar domain structure composed of an extracellular region with 2 Ig-like domains, followed by 2 FNII-like domains, a single transmembrane region, and a cytoplasmic tyrosine kinase domain (1). The natural ligand for Tyro3, as well as Axl and Mer, is Gas6 (growth arrest-specific gene 6) (1,2). Expression pattern and target knockout data indicate an important role of Tyro3 in apoptotic cell phagocytosis of dendritic cells and macrophages (3), NK cell differentiation (4), reproductive neuron survival and migration (5), osteoclast stimulation (6,7), as well as cortical and hippocampal neuron function (8). Both MAPK and PI3K pathways have been suggested as downstream targets of Tyro3 activation (7,8). Tyro3 has also been shown to be correlated to melanoma tumorigenesis, likely through its reglulatory role in the expression of oncogenic microphthalmia-associated transcription factor (MITF) (9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Paired box (PAX) proteins are a family of transcription factors that play important and diverse roles in animal development (1). Nine PAX proteins (PAX1-9) have been described in humans and other mammals. They are defined by the presence of an amino-terminal "paired" domain, consisting of two helix-turn-helix motifs, with DNA binding activity (2). PAX proteins are classified into four structurally distinct subgroups (I-IV) based on the absence or presence of a carboxy-terminal homeodomain and a central octapeptide region. Subgroup I (PAX1 and 9) contains the octapeptide but lacks the homeodomain; subgroup II (PAX2, 5, and 8) contains the octapeptide and a truncated homeodomain; subgroup III (PAX3 and 7) contains the octapeptide and a complete homeodomain; and subgroup IV (PAX4 and 6) contains a complete homeodomain but lacks the octapeptide region (2). PAX proteins play critically important roles in development by regulating transcriptional networks responsible for embryonic patterning and organogenesis (3); a subset of PAX proteins also maintain functional importance during postnatal development (4). Research studies have implicated genetic mutations that result in aberrant expression of PAX genes in a number of cancer subtypes (1-3), with members of subgroups II and III identified as potential mediators of tumor progression (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Thyroid Transcription Factor 1 (TTF-1, also known as NKX2-1), a member of the NKX homeobox transcription factor family, was initially discovered in the FRTL-5 rat thyroid cell line (1). Subsequent studies have shown that TTF-1 plays an important role in differentiation and morphogenesis of the developing thyroid, lung, and ventral forebrain (2). TTF-1 controls the expression of several genes, some of which are tissue specific, such as: thyroglobulin, thyroperoxidase, and the thyrotropin receptor in the thyroid; and surfactant proteins and clara cell secretory protein in the lung (2,3). Investigators have found that TTF-1 is expressed in malignant tumors of the thyroid and lung, and it is commonly used as a marker for both primary and malignant lung cancers (4-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Chromatin IP-seq, Flow Cytometry, Western Blotting

Background: LEF1 and TCF are members of the high mobility group (HMG) DNA binding protein family of transcription factors that consists of the following: Lymphoid Enhancer Factor 1 (LEF1), T Cell Factor 1 (TCF1/TCF7), TCF3/TCF7L1, and TCF4/TCF7L2 (1). LEF1 and TCF1/TCF7 were originally identified as important factors regulating early lymphoid development (2) and act downstream in Wnt signaling. LEF1 and TCF bind to Wnt response elements to provide docking sites for β-catenin, which translocates to the nucleus to promote the transcription of target genes upon activation of Wnt signaling (3). LEF1 and TCF are dynamically expressed during development and aberrant activation of the Wnt signaling pathway is involved in many types of cancers including colon cancer (4,5).

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

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

Background: LEF1 and TCF are members of the high mobility group (HMG) DNA binding protein family of transcription factors that consists of the following: Lymphoid Enhancer Factor 1 (LEF1), T Cell Factor 1 (TCF1/TCF7), TCF3/TCF7L1, and TCF4/TCF7L2 (1). LEF1 and TCF1/TCF7 were originally identified as important factors regulating early lymphoid development (2) and act downstream in Wnt signaling. LEF1 and TCF bind to Wnt response elements to provide docking sites for β-catenin, which translocates to the nucleus to promote the transcription of target genes upon activation of Wnt signaling (3). LEF1 and TCF are dynamically expressed during development and aberrant activation of the Wnt signaling pathway is involved in many types of cancers including colon cancer (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: LEF1 and TCF are members of the high mobility group (HMG) DNA binding protein family of transcription factors that consists of the following: Lymphoid Enhancer Factor 1 (LEF1), T Cell Factor 1 (TCF1/TCF7), TCF3/TCF7L1, and TCF4/TCF7L2 (1). LEF1 and TCF1/TCF7 were originally identified as important factors regulating early lymphoid development (2) and act downstream in Wnt signaling. LEF1 and TCF bind to Wnt response elements to provide docking sites for β-catenin, which translocates to the nucleus to promote the transcription of target genes upon activation of Wnt signaling (3). LEF1 and TCF are dynamically expressed during development and aberrant activation of the Wnt signaling pathway is involved in many types of cancers including colon cancer (4,5).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Neurofibromin is a Ras-specific GTPase activating protein (RasGAP), down-regulating Ras signaling (1). Studies have shown, that mutations in NF1 inhibit its activity, resulting in benign tumors such as neurofibromas, which may form along nerves throughout the body resulting in neurofibromatosis type 1 (NF1) (2). NF1 is one of the most common autosomal dominant diseases however it remains unclear how mutation of NF1 may lead to other features of NF1 (3). In addition, NF1 mutations occur in 5-10% of human sporadic malignancies such as glioblastomas, lung adenocarcinomas, melanomas, breast and ovarian cancers, and acute myeloid leukemias. Mutations in NF1 can cause resistance to therapies including chemotherapy and radiation therapy (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Chromatin IP-seq, Immunofluorescence (Frozen), Immunoprecipitation, Western Blotting

Background: Brn2/POU3F2 is a POU domain-containing transcription factor involved in neuronal differentiation and activation of the corticotrophin-releasing hormone gene (1,2). In mice, disruption of the Brn2 gene results in loss of specific neuronal lineages in the hypothalamus (3). In addition to its role in mammalian neurogenesis, Brn2 has also been implicated in melanoma tumorigenesis and has been shown in the literature to be overexpressed in human melanoma cells compared to normal melanocytes (4,5). Recent studies also identify Brn2 as a transcription factor playing an important role in keratinocyte differentiation (6). Recent reports demonstrate that overexpression of three transcription factors (Brn2, Ascl1, and Myt1L) can directly convert human fibroblasts into functional neurons under precisely defined conditions (7,8).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: HES1 (Hairy and Enhancer of Split 1) is one of seven members of the HES family of basic helix-loop-helix (bHLH) transcription factors which function primarily to repress transcription of bHLH-dependent genes (1). HES1 is understood to play an important conserved role in maintaining pluripotency of embryonic and adult stem/progenitor cells via the transcriptional repression of genes that promote differentiation (1,2). HES1 is particularly well known as a repressive mediator of the canonical Notch signaling pathway (3). HES1 plays a key role in mediating Notch-dependent T cell lineage commitment (4), and has been reported to be an essential mediator of Notch-induced T cell acute lymphoblastic leukemia (T-ALL) (4,5). HES1 is also reported to mediate Notch-induced repression of differentiation in a number of cancer cell types. A conditional deletion of HES1 from intestinal tumor cells in APC-mutant mice reduced tumor cell proliferation, while promoting differentiation toward epithelial lineages (6). Overexpression of HES1 in a human osteosarcoma (OS) cell line was shown to repress expression of the Notch antagonist Dtx1, leading to increased OS cell invasiveness (7). Other genes subject to transcriptional repression by HES1 include Neurogenin-2, Math1/Atoh1 and the NOTCH ligands DLL1 and Jagged1 (6,8,9).

$348
100 µl
This Cell Signaling Technology (CST) antibody is conjugated to biotin under optimal conditions. The unconjugated PTEN (D4.3) XP® Rabbit mAb #9188 reacts with human, mouse, rat and monkey PTEN protein. PTEN (D4.3) XP® Rabbit mAb (Biotinylated) also recognizes PTEN in these species.
APPLICATIONS
REACTIVITY
Dog, Hamster, Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: PTEN (phosphatase and tensin homologue deleted on chromosome ten), also referred to as MMAC (mutated in multiple advanced cancers) phosphatase, is a tumor suppressor implicated in a wide variety of human cancers (1). PTEN encodes a 403 amino acid polypeptide originally described as a dual-specificity protein phosphatase (2). The main substrates of PTEN are inositol phospholipids generated by the activation of the phosphoinositide 3-kinase (PI3K) (3). PTEN is a major negative regulator of the PI3K/Akt signaling pathway (1,4,5). PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382, and Thr383) that regulate PTEN stability and may affect its biological activity (6,7). PTEN regulates p53 protein levels and activity (8) and is involved in G protein-coupled signaling during chemotaxis (9,10).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: PTEN (phosphatase and tensin homologue deleted on chromosome ten), also referred to as MMAC (mutated in multiple advanced cancers) phosphatase, is a tumor suppressor implicated in a wide variety of human cancers (1). PTEN encodes a 403 amino acid polypeptide originally described as a dual-specificity protein phosphatase (2). The main substrates of PTEN are inositol phospholipids generated by the activation of the phosphoinositide 3-kinase (PI3K) (3). PTEN is a major negative regulator of the PI3K/Akt signaling pathway (1,4,5). PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382, and Thr383) that regulate PTEN stability and may affect its biological activity (6,7). PTEN regulates p53 protein levels and activity (8) and is involved in G protein-coupled signaling during chemotaxis (9,10).

$122
20 µl
$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: PTEN (phosphatase and tensin homologue deleted on chromosome ten), also referred to as MMAC (mutated in multiple advanced cancers) phosphatase, is a tumor suppressor implicated in a wide variety of human cancers (1). PTEN encodes a 403 amino acid polypeptide originally described as a dual-specificity protein phosphatase (2). The main substrates of PTEN are inositol phospholipids generated by the activation of the phosphoinositide 3-kinase (PI3K) (3). PTEN is a major negative regulator of the PI3K/Akt signaling pathway (1,4,5). PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382, and Thr383) that regulate PTEN stability and may affect its biological activity (6,7). PTEN regulates p53 protein levels and activity (8) and is involved in G protein-coupled signaling during chemotaxis (9,10).

$111
20 µl
$260
100 µl
$637
300 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: PTEN (phosphatase and tensin homologue deleted on chromosome ten), also referred to as MMAC (mutated in multiple advanced cancers) phosphatase, is a tumor suppressor implicated in a wide variety of human cancers (1). PTEN encodes a 403 amino acid polypeptide originally described as a dual-specificity protein phosphatase (2). The main substrates of PTEN are inositol phospholipids generated by the activation of the phosphoinositide 3-kinase (PI3K) (3). PTEN is a major negative regulator of the PI3K/Akt signaling pathway (1,4,5). PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382, and Thr383) that regulate PTEN stability and may affect its biological activity (6,7). PTEN regulates p53 protein levels and activity (8) and is involved in G protein-coupled signaling during chemotaxis (9,10).