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Product listing: TCEB3/Elongin A Antibody, UniProt ID Q14241 #3685 to SATB1 (L745) Antibody, UniProt ID Q01826 #3650

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: The Elongin complex is a heterotrimer composed of TCEB3/Elongin A, Elongin B (TCEB2), and Elongin C (TCEB1) subunits (1-3). The Elongin complex regulates the rate of RNA polymerase II (RNAPII) transcription elongation by releasing the transient pausing of RNAPII at multiple sites along the DNA. TCEB3/Elongin A is the transcriptionally active subunit, while Elongin B and C subunits play a regulatory role (3,4). TCEB3/Elongin A may be required for expression of a subset of cell cycle regulated genes, and embryonic stem (ES) cells lacking TCEB3/Elongin A show abnormalities in cell size, growth, and cell cycle distribution (5). In addition, the Elongin complex has been shown to interact with the cullin family and RING finger proteins Cul5/Rbx2 upon UV-induced DNA damage, removing arrested RNAPII at sites of DNA damage by ubiquitination and degradation as part of an E3 ubiquitin ligase (6).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Apoptosis mediated by death factors like FasL and TNF-α involves the formation of a death-inducing signaling complex (DISC) to their respective receptors (1). Upon ligand activation to their receptors, Fas and TNF-R1 associate with death domain (DD) containing adaptor proteins FADD (Fas associated death domain) (2,3) and TRADD (TNF-R1 associated death domain) (4). In addition to its carboxy-terminal DD, FADD contains an amino-terminal death effector domain (DED) that binds to DEDs found on caspase-8 which leads to activation of this initiator caspase (5,6). Caspase-8 subsequently activates downstream effector caspases, like caspase-3, resulting in the cleavage of proteins involved in the execution of apoptosis. Unlike FADD, TRADD does not contain a DED (4). Apoptosis driven by TNF-R1 binding to TRADD involves association of TRADD and FADD which then leads to activation of caspase-8 (7).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The unconjugated GAPDH (14C10) Rabbit mAb #2118 reacts with human, mouse, rat and monkey GAPDH. CST expects that GAPDH (14C10) (HRP conjugate) #3683 will also recognize GAPDH in these species.
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Pig, Rat

Application Methods: Western Blotting

Background: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyzes the phosphorylation of glyceraldehyde-3-phosphate during glycolysis. Though differentially expressed from tissue to tissue (1), GAPDH is thought to be a constitutively expressed housekeeping protein. For this reason, GAPDH mRNA and protein levels are often measured as controls in experiments quantifying specific changes in expression of other targets. Recent work has elucidated roles for GAPDH in apoptosis (2), gene expression (3), and nuclear transport (4). GAPDH may also play a role in neurodegenerative pathologies such as Huntington and Alzheimer's diseases (4,5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Mammalian sterile-20-like (MST) kinases are upstream regulators of mitogen-activated protein kinase (MAPK) signaling pathways that regulate multiple cellular processes, including proliferation, apoptosis, migration, and cytoskeletal rearrangement (1). This family of serine/threonine kinases includes MST1 (STK4) and MST2 (STK3), two functionally related proteins with conserved amino-terminal kinase domains and carboxy-terminal regulatory domains that contain nuclear export signals (1-3). During apoptosis, caspase-mediated cleavage of MST1/2 removes the inhibitory regulatory domain, triggering autophosphorylation and activation of the kinase domain, which is translocated to the nucleus. Nuclear translocation of the active kinase induces chromatin condensation and other events associated with apoptotic progression (4).Research studies indicate that MST1/2 are orthologous to Drosophila Hippo (Hpo), one of the core regulatory proteins in the Hippo signaling pathway. This evolutionarily conserved program controls tissue growth and organ size by regulating cell proliferation, apoptosis, and stem cell self-renewal. The mammalian Hippo signaling pathway involves a kinase cascade, where the MST1/2 kinases and the SAV1 scaffold protein form a complex that leads to phosphorylation and activation of LATS1/2. The LATS1/2 kinases phosphorylate YAP and TAZ, promoting cytoplasmic sequestration and inhibition of these transcription coactivators (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Guinea Pig, Human, Mouse

Application Methods: Western Blotting

Background: Mammalian sterile-20-like (MST) kinases are upstream regulators of mitogen-activated protein kinase (MAPK) signaling pathways that regulate multiple cellular processes, including proliferation, apoptosis, migration, and cytoskeletal rearrangement (1). This family of serine/threonine kinases includes MST1 (STK4) and MST2 (STK3), two functionally related proteins with conserved amino-terminal kinase domains and carboxy-terminal regulatory domains that contain nuclear export signals (1-3). During apoptosis, caspase-mediated cleavage of MST1/2 removes the inhibitory regulatory domain, triggering autophosphorylation and activation of the kinase domain, which is translocated to the nucleus. Nuclear translocation of the active kinase induces chromatin condensation and other events associated with apoptotic progression (4).Research studies indicate that MST1/2 are orthologous to Drosophila Hippo (Hpo), one of the core regulatory proteins in the Hippo signaling pathway. This evolutionarily conserved program controls tissue growth and organ size by regulating cell proliferation, apoptosis, and stem cell self-renewal. The mammalian Hippo signaling pathway involves a kinase cascade, where the MST1/2 kinases and the SAV1 scaffold protein form a complex that leads to phosphorylation and activation of LATS1/2. The LATS1/2 kinases phosphorylate YAP and TAZ, promoting cytoplasmic sequestration and inhibition of these transcription coactivators (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin)

Background: Modulation of chromatin structure plays an important role in the regulation of transcription in eukaryotes. The nucleosome, made up of DNA wound around eight core histone proteins (two each of H2A, H2B, H3, and H4), is the primary building block of chromatin (1). The amino-terminal tails of core histones undergo various post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (2-5). These modifications occur in response to various stimuli and have a direct effect on the accessibility of chromatin to transcription factors and, therefore, gene expression (6). In most species, histone H2B is primarily acetylated at Lys5, 12, 15, and 20 (4,7). Histone H3 is primarily acetylated at Lys9, 14, 18, 23, 27, and 56. Acetylation of H3 at Lys9 appears to have a dominant role in histone deposition and chromatin assembly in some organisms (2,3). Phosphorylation at Ser10, Ser28, and Thr11 of histone H3 is tightly correlated with chromosome condensation during both mitosis and meiosis (8-10). Phosphorylation at Thr3 of histone H3 is highly conserved among many species and is catalyzed by the kinase haspin. Immunostaining with phospho-specific antibodies in mammalian cells reveals mitotic phosphorylation at Thr3 of H3 in prophase and its dephosphorylation during anaphase (11).

$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Mitogen- and stress-activated protein kinase 1 (MSK1) and MSK2 are serine/threonine kinases that promote immediate early gene transcription in stress- or mitogen-induced cells (1-4,7, 8) and LPS-stimulated macrophages (9). MSK2, also known as RSKB, contains two catalytic domains and has been shown to interact directly with p38 MAP kinase (10). MSK2 is phosphorylated and activated in response to tumor necrosis factor, epidermal growth factor or phorbol ester in HeLa cells or murine embryonic fibroblasts (MEFs) in a p38- and ERK-dependent manner (8,11). Phosphorylation on residues Ser196 and Thr568 within the activation loop of both catalytic domains is required for full kinase activation (11). Both MSK1 and MSK2 contain a functional nuclear localization sequence that is sufficient and required for nuclear targeting (10). Consistent with their nuclear localization, these kinases play an important role in regulating transcriptional responses to stress and mitogens. Activation of MSK2 in HeLa cells or MEFs results in rapid phosphorylation of histone H3, HMG-14, CREB and ATF1 and acetylation of histone H3 associated with immediate early gene transcription (3,4,6,7).

$146
100 µl
Affinity purified mouse anti-rabbit IgG (Conformation Specific) antibody. This product has been optimized for use as a secondary antibody in Western blotting applications.
APPLICATIONS

Application Methods: Western Blotting

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

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

Background: Acetyl-CoA carboxylase (ACC) catalyzes the carboxylation of acetyl-CoA to malonyl-CoA (1). It is the key enzyme in the biosynthesis and oxidation of fatty acids (1). In rodents, the 265 kDa ACC1 (ACCα) form is primarily expressed in lipogenic tissues, while 280 kDa ACC2 (ACCβ) is the main isoform in oxidative tissues (1,2). However, in humans, ACC2 is the predominant isoform in both lipogenic and oxidative tissues (1,2). Phosphorylation by AMPK at Ser79 or by PKA at Ser1200 inhibits the enzymatic activity of ACC (3). ACC is a potential target of anti-obesity drugs (4,5).

$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Mouse, Pig, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Myosin is composed of six polypeptide chains: two identical heavy chains and two pairs of light chains. Myosin light chain 2 (MLC2), also known as myosin regulatory light chain (MRLC), RLC, or LC20, has many isoforms depending on its distribution. In smooth muscle, MLC2 is phosphorylated at Thr18 and Ser19 by myosin light chain kinase (MLCK) in a Ca2+/calmodulin-dependent manner (1). This phosphorylation is correlated with myosin ATPase activity and smooth muscle contraction (2). ROCK also phosphorylates Ser19 of smooth muscle MLC2, which regulates the assembly of stress fibers (3). Phosphorylation of smooth muscle MLC2 at Ser1/Ser2 and Ser9 by PKC and cdc2 has been reported to inhibit myosin ATPase activity (4,5). Phosphorylation by cdc2 controls the timing of cytokinesis (5). Transgenic mice lacking phosphorylation sites on the cardiac muscle isoform show morphological and functional abnormalities (6).

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

Application Methods: Western Blotting

Background: Myosin is composed of six polypeptide chains: two identical heavy chains and two pairs of light chains. Myosin light chain 2 (MLC2), also known as myosin regulatory light chain (MRLC), RLC, or LC20, has many isoforms depending on its distribution. In smooth muscle, MLC2 is phosphorylated at Thr18 and Ser19 by myosin light chain kinase (MLCK) in a Ca2+/calmodulin-dependent manner (1). This phosphorylation is correlated with myosin ATPase activity and smooth muscle contraction (2). ROCK also phosphorylates Ser19 of smooth muscle MLC2, which regulates the assembly of stress fibers (3). Phosphorylation of smooth muscle MLC2 at Ser1/Ser2 and Ser9 by PKC and cdc2 has been reported to inhibit myosin ATPase activity (4,5). Phosphorylation by cdc2 controls the timing of cytokinesis (5). Transgenic mice lacking phosphorylation sites on the cardiac muscle isoform show morphological and functional abnormalities (6).

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

Application Methods: Western Blotting

Background: The initiation of DNA replication in mammalian cells is a highly coordinated process that ensures duplication of the genome only once per cell division cycle. Origins of replication are dispersed throughout the genome and their activities are regulated via the sequential binding of pre-replication and replication factors. The origin recognition complex (ORC) is thought to bind to chromatin throughout the cell cycle (1,2). The pre-replication complex (Pre-RC) forms in late mitosis/early G1 phase with the binding of CDT1 and cdc6 to the origin, which allows binding of the heterohexameric MCM2-7 complex. The MCM complex is thought to be the replicative helicase and formation of the Pre-RC is referred to as chromatin licensing. Subsequent initiation of DNA replication requires the activation of the S-phase promoting kinases cdk2 and cdc7. Cdc7 phosphorylates MCM proteins bound to chromatin and, in conjunction with CDT1, recruits the replication factor cdc45 (3-5). Cdc45 is required for formation of pre-initiation complexes at the G1/S transition and for activation of replication origins. The level of cdc45 protein expression is associated with the proliferative status of the cell or tissue. Terminally differentiated and senescent cells lack cdc45 and highly proliferative cell lines express high levels of cdc45 (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Myosin is composed of six polypeptide chains: two identical heavy chains and two pairs of light chains. Myosin light chain 2 (MLC2), also known as myosin regulatory light chain (MRLC), RLC, or LC20, has many isoforms depending on its distribution. In smooth muscle, MLC2 is phosphorylated at Thr18 and Ser19 by myosin light chain kinase (MLCK) in a Ca2+/calmodulin-dependent manner (1). This phosphorylation is correlated with myosin ATPase activity and smooth muscle contraction (2). ROCK also phosphorylates Ser19 of smooth muscle MLC2, which regulates the assembly of stress fibers (3). Phosphorylation of smooth muscle MLC2 at Ser1/Ser2 and Ser9 by PKC and cdc2 has been reported to inhibit myosin ATPase activity (4,5). Phosphorylation by cdc2 controls the timing of cytokinesis (5). Transgenic mice lacking phosphorylation sites on the cardiac muscle isoform show morphological and functional abnormalities (6).

$122
20 µl
$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Myosin is composed of six polypeptide chains: two identical heavy chains and two pairs of light chains. Myosin light chain 2 (MLC2), also known as myosin regulatory light chain (MRLC), RLC, or LC20, has many isoforms depending on its distribution. In smooth muscle, MLC2 is phosphorylated at Thr18 and Ser19 by myosin light chain kinase (MLCK) in a Ca2+/calmodulin-dependent manner (1). This phosphorylation is correlated with myosin ATPase activity and smooth muscle contraction (2). ROCK also phosphorylates Ser19 of smooth muscle MLC2, which regulates the assembly of stress fibers (3). Phosphorylation of smooth muscle MLC2 at Ser1/Ser2 and Ser9 by PKC and cdc2 has been reported to inhibit myosin ATPase activity (4,5). Phosphorylation by cdc2 controls the timing of cytokinesis (5). Transgenic mice lacking phosphorylation sites on the cardiac muscle isoform show morphological and functional abnormalities (6).

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

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

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. Major types of intermediate filaments are specifically expressed in particular cell types: cytokeratins in epithelial cells, glial fibrillary acidic protein (GFAP) in glial cells, desmin in skeletal, visceral, and certain vascular smooth muscle cells, vimentin in cells of mesenchymal origin, and neurofilaments in neurons. GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). In addition, GFAP intermediate filaments are also present in nonmyelin-forming Schwann cells in the peripheral nervous system (3).

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

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

Background: The Rho family small GTPases, including Rho, Rac and cdc42, act as molecular switches, regulating processes such as cell migration, adhesion, proliferation and differentiation. They are activated by guanine nucleotide exchange factors (GEFs), which catalyze the exchange of bound GDP for GTP, and inhibited by GTPase activating proteins (GAPs), which catalyze the hydrolysis of GTP to GDP. A third level of regulation is provided by the stoichiometric binding of Rho GDP dissociation inhibitor (RhoGDI) (1).G-protein coupled receptors (GPCRs) at the cell surface signal through heteromeric G proteins to small GTPases such as Rho, which then signal to downstream effector molecules (2). p115 RhoGEF/ArhGEF1 and its family members PDZ-RhoGEF (PRG), and LARG are stimulated by heteromeric G proteins and thus couple signaling from GPCRs to Rho small GTPases (3-6). In a mouse model of asthma, p115 RhoGEF is necessary for T cells to enable airway inflammation and hyperreactivity (7).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: RCC2/TD-60 is a member of the RCC1 (regulator of chromosome condensation 1) family of guanine nucleotide exchange factors. RCC2/TD-60 is associated with the chromosome passenger complex (CPC), which also consists of aurora B kinase, borealin, INCENP (inner centromere protein) and survivin. The CPC acts at various stages of mitosis, interacts with microtubules and is required for proper chromosome segregation and cytokinesis. Regulation of aurora B kinase is key in the regulation of the CPC (reviewed in 1,2). In late mitosis, RCC2/TD-60 is required for spindle assembly and recruitment of survivin and aurora B (3). RCC2/TD-60 is also required for aurora B activation in vitro and localization of the CPC to centromeres (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Annexin A7/ANXA7 is a member of the annexin family of calcium/phospholipid-binding proteins, and is involved in the process of membrane fusion and exocytosis (1). Annexin A7 is a GTPase, and both GTP-binding and PKC activity are important in regulating protein function (2,3). Membrane binding of annexin A7 is calcium dependent (4). Two isoforms exist due to alternative splicing. Subcellular localization of annexin A7 has been shown to be in the cytoplasm, vesicular structures, membrane and in adrenal chromaffin granules (5,6). Nuclear localization has been shown in the developing mouse central nervous system as well as in adult mouse brain (7). Annexin A7-deficient mouse studies show that the protein has a role in insulin secretion and calcium signaling (8) as well as cardiac intracellular calcium homeostasis electrical stability (9). The gene for annexin A7 is a putative tumor suppressor (10), and alterations in the copy number have been reported in prostate cancer (11). Annexin A7 expression has also been correlated with survival in human glioblastoma patients (12), and haploinsufficiency in mice may promote genetic instability leading to tumorigenesis (13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Rho family small GTPases act as molecular switches that regulate processes such as cell migration, adhesion, proliferation and differentiation. Typically, they are activated by guanine nucleotide exchange factors (GEFs), which catalyze the exchange of bound GDP for GTP, and are inhibited by GTPase activating proteins (GAPs), which catalyze the hydrolysis of GTP to GDP (1). Rnd1, Rnd2 and RhoE/Rnd3 comprise the evolutionarily divergent Rnd family of Rho-type small GTPases, which lack GTPase activity and therefore remain in a GTP-bound state (2, reviewed in 3). RhoE/Rnd3 activity leads to a decrease in stress fibers and increased cell migration, at least in part through regulation of the Rho-dependent kinase ROCK1 (4). Activity of RhoE/Rnd3 itself is regulated by ROCK1, which phosphorylates RhoE/Rnd3 at Ser11, enhancing its activity (5). RhoE/Rnd3 has been implicated in inhibition of DNA-damage induced apoptosis (6) and cell cycle arrest (7). In keratinocytes, RhoE/Rnd3 regulates differentiation through its effects on both proliferation and adhesion (8).

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

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

Background: Acetyl-CoA carboxylase (ACC) catalyzes the carboxylation of acetyl-CoA to malonyl-CoA (1). It is the key enzyme in the biosynthesis and oxidation of fatty acids (1). In rodents, the 265 kDa ACC1 (ACCα) form is primarily expressed in lipogenic tissues, while 280 kDa ACC2 (ACCβ) is the main isoform in oxidative tissues (1,2). However, in humans, ACC2 is the predominant isoform in both lipogenic and oxidative tissues (1,2). Phosphorylation by AMPK at Ser79 or by PKA at Ser1200 inhibits the enzymatic activity of ACC (3). ACC is a potential target of anti-obesity drugs (4,5).

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

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

Background: Acetyl-CoA carboxylase (ACC) catalyzes the carboxylation of acetyl-CoA to malonyl-CoA (1). It is the key enzyme in the biosynthesis and oxidation of fatty acids (1). In rodents, the 265 kDa ACC1 (ACCα) form is primarily expressed in lipogenic tissues, while 280 kDa ACC2 (ACCβ) is the main isoform in oxidative tissues (1,2). However, in humans, ACC2 is the predominant isoform in both lipogenic and oxidative tissues (1,2). Phosphorylation by AMPK at Ser79 or by PKA at Ser1200 inhibits the enzymatic activity of ACC (3). ACC is a potential target of anti-obesity drugs (4,5).

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

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

Background: Glucocorticoid hormones control cellular proliferation, inflammation, and metabolism through their association with the glucocorticoid receptor (GR)/NR3C1, a member of the nuclear hormone receptor superfamily of transcription factors (1). GR is composed of several conserved structural elements, including a carboxy-terminal ligand-binding domain (which also contains residues critical for receptor dimerization and hormone-dependent gene transactivation), a neighboring hinge region containing nuclear localization signals, a central zinc-finger-containing DNA-binding domain, and an amino-terminal variable region that participates in ligand-independent gene transcription. In the absence of hormone, a significant population of GR is localized to the cytoplasm in an inactive form via its association with regulatory chaperone proteins, such as HSP90, HSP70, and FKBP52. On hormone binding, GR is released from the chaperone complex and translocates to the nucleus as a dimer to associate with specific DNA sequences termed glucocorticoid response elements (GREs), thereby enhancing or repressing transcription of specific target genes (2). It was demonstrated that GR-mediated transcriptional activation is modulated by phosphorylation (3-5). Although GR can be basally phosphorylated in the absence of hormone, it becomes hyperphosphorylated upon binding receptor agonists. It has been suggested that hormone-dependent phosphorylation of GR may determine target promoter specificity, cofactor interaction, strength and duration of receptor signaling, receptor stability, and receptor subcellular localization (3).

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

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

Background: Wiskott-Aldrich syndrome proteins (WASPs) mediate actin dynamics by activating the Arp2/3 actin nucleation complex in response to activated Rho family GTPases. In mammals, five WASP family members have been described. Hematopoietic WASP and ubiquitously expressed N-WASP are autoinhibited in unstimulated cells. Upon stimulation they are activated by cdc42, which relieves the autoinhibition in conjunction with phosphatidyl inositol 4,5-bisphosphate. Three WAVE (Wasf, SCAR) family proteins are similar in sequence to WASP and N-WASP but lack the WASP/N-WASP autoinhibition domains and are indirectly activated by Rac (reviewed in 1). Both WASP and WAVE functions appear to be essential, as knockout of either N-WASP or Scar-2 in mice results in cardiac and neuronal defects and embryonic lethality (2,3). Loss of WASP results in immune system defects and fewer immune cells (4). WAVE-2 (WASF2) is widely distributed, while WAVE-1 and WAVE-3 are strongly expressed in brain (5). WAVE-3 may act as a tumor suppressor in neuroblastoma, a childhood disease of the sympathetic nervous system (6). Increased expression of WAVE-3 is seen in breast cancer, and studies in breast adenocarcinoma cells indicate that WAVE-3 regulates breast cancer progression, invasion and metastasis through the p38 mitogen-activated protein kinase (MAPK) pathway (7,8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Cytoplasmic acetyl-CoA synthetase (AceCS1) catalyzes the conversion of acetate and CoA to acetyl-CoA (1, 2). Acetyl-CoA synthesized by AceCS1 is used for fatty acid and lipid biosynthesis (1, 2). Studies suggest that this enzyme is regulated by sterol regulatory element-binding proteins (2). It was also shown that this enzyme is acetylated by protein acetyltransferases in cells (3, 4). SIRT1 deacetylates this enzyme at Lys661 resulting in its activation and the increase of fatty acid synthesis (3, 4).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct immunofluorescence of rat cells. The unconjugated antibody #3670 reacts with human, mouse and rat GFAP protein. CST expects that GFAP (GA5) Mouse mAb (Alexa Fluor® 647 Conjugate) will also recognize GFAP in these species.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen)

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. Major types of intermediate filaments are specifically expressed in particular cell types: cytokeratins in epithelial cells, glial fibrillary acidic protein (GFAP) in glial cells, desmin in skeletal, visceral, and certain vascular smooth muscle cells, vimentin in cells of mesenchymal origin, and neurofilaments in neurons. GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). In addition, GFAP intermediate filaments are also present in nonmyelin-forming Schwann cells in the peripheral nervous system (3).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for direct immunofluorescence of rat cerebellum. The unconjugated antibody #3670 reacts with human, mouse and rat GFAP protein. CST expects that GFAP (GA5) Mouse mAb (Alexa Fluor® 555 Conjugate) will also recognize GFAP in these species.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen)

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. Major types of intermediate filaments are specifically expressed in particular cell types: cytokeratins in epithelial cells, glial fibrillary acidic protein (GFAP) in glial cells, desmin in skeletal, visceral, and certain vascular smooth muscle cells, vimentin in cells of mesenchymal origin, and neurofilaments in neurons. GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). In addition, GFAP intermediate filaments are also present in nonmyelin-forming Schwann cells in the peripheral nervous system (3).

$305
100 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct immunofluorescence of rat cells. The unconjugated antibody GFAP (GA5) Mouse mAb #3670 reacts with human, mouse and rat GFAP protein. CST expects that GFAP (GA5) Mouse mAb (Alexa Fluor® 488 Conjugate) will also recognize GFAP in these species.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen)

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments, and microtubules. Major types of intermediate filaments are specifically expressed in particular cell types: cytokeratins in epithelial cells, glial fibrillary acidic protein (GFAP) in glial cells, desmin in skeletal, visceral, and certain vascular smooth muscle cells, vimentin in cells of mesenchymal origin, and neurofilaments in neurons. GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). In addition, GFAP intermediate filaments are also present in nonmyelin-forming Schwann cells in the peripheral nervous system (3).

$305
400 µl
This Cell Signaling Technology (CST) antibody is immobilized via covalent binding of primary amino groups to N-hydroxysuccinimide (NHS)-activated Sepharose® beads. Akt (pan) (40D4) Mouse mAb (Sepharose® Bead Conjugate) is useful for immunoprecipitation assays. The unconjugated Akt (pan) (40D4) Mouse mAb #2920 reacts with human, mouse, rat, and monkey Akt protein. CST expects that Akt (pan) (40D4) Mouse mAb (Sepharose® Bead Conjugate) will also recognize Akt in these species.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation

Background: Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis (1-3). This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin-sensitive pathway involving PI3 kinase (2,3). Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 (4) and by phosphorylation within the carboxy terminus at Ser473. The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin (mTOR) in a rapamycin-insensitive complex with rictor and Sin1 (5,6). Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad (7), forkhead transcription factors (8), c-Raf (9), and caspase-9. PTEN phosphatase is a major negative regulator of the PI3 kinase/Akt signaling pathway (10). LY294002 is a specific PI3 kinase inhibitor (11). Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK-3α and β (12,13). Akt may also play a role in insulin stimulation of glucose transport (12). In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation by preventing GSK-3β-mediated phosphorylation and degradation of cyclin D1 (14) and by negatively regulating the cyclin dependent kinase inhibitors p27 Kip1 (15) and p21 Waf1/Cip1 (16). Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor (17). More importantly, Akt phosphorylates and inactivates tuberin (TSC2), an inhibitor of mTOR within the mTOR-raptor complex (18,19).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: The cdc25 protein phosphatase family plays a critical role in activating cyclin-dependent kinases (CDKs) via dephosphorylation of conserved Thr14/Tyr15 inhibitory phosphorylation sites. While cdc25C is primarily responsible for activating CDK1 to overcome the G2/M checkpoint and allow mitotic entry, the primary substrate of cdc25A is CDK2, which, when active, allows progression through the G1/S and intra-S checkpoints (1). Abundance, subcellular localization and activity of cdc25A is tightly controlled by a variety of mechanisms, including phosphorylation, ubiquitination, and inhibitory binding to 14-3-3 proteins. During normal cell cycle progression, elevated c-Myc and E2F transcription factor levels lead to increased cdc25A expression (2). When conditions are favorable for DNA synthesis, cdc25A and CDK2 form an activation loop, wherein each activates the other enzyme (1). DNA damage, on the other hand, leads to multisite phosphorylation at inhibitory sites (Ser123, Ser177, Ser278, Ser292, and Thr506) by Chk1 and Chk2, which result in 14-3-3 binding and ubiquitin-mediated degradation (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Special AT-rich binding protein 1 (SATB1) functions as both a global chromatin organizer and a gene-specific transcription factor (1). SATB1 cooperates with promyelocytic leukemia protein (PML) to regulate global chromatin architecture by organizing chromatin into distinct loops via periodic anchoring of matrix attachment regions (MARs) in DNA to the nuclear matrix (1-3). In addition, SATB1 recruits multiple chromatin-remodeling proteins that contribute to specific gene activation and repression, including the chromatin remodeling enzymes ACF and ISWI, the histone deacetylase HDAC1, and the histone acetyltransferases PCAF and p300/CBP (4-6). Phosphorylation of SATB1 on Ser185 by protein kinase C regulates its interaction with HDAC1 and PCAF. While unphosphorylated SATB1 binds to PCAF, phosphorylated SATB1 preferentially binds to HDAC1 (6). Acetylation of SATB1 on Lys136 by PCAF impairs its DNA binding activity, thereby removing SATB1 from gene promoters (6). SATB1 is expressed predominantly in thymocytes and is involved in gene regulation during T cell activation (1). SATB1 is also expressed in metastatic breast cancer cells and is a potential prognostic marker and therapeutic target for metastatic breast cancer (7). In a mouse model system, RNAi-mediated knockdown of SATB1 reversed tumorigenesis by inhibiting tumor growth and metastasis, while ectopic expression of SATB1 in non-metastatic breast cancer cells produced invasive tumors.