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Product listing: MBP Tag (8G1) Mouse mAb #2396 to α-Smooth Muscle Actin (D4K9N) XP® Rabbit mAb (Alexa Fluor® 488 Conjugate), UniProt ID P62736 #34105

$260
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

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

Background: Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein’s biochemical properties.

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Integrin-linked kinases (ILKs) couple integrins and growth factors to downstream pathways involved in cell survival, cell cycle control, cell-cell adhesion and cell motility (1). ILK functions as a scaffold bridging the extracellular matrix (ECM) and growth factor receptors to the actin cytoskeleton through interactions with integrin, PINCH (which links ILK to the RTKs via Nck2), CH-ILKBP and affixin (1). ILK phosphorylates Akt at Ser473, GSK-3 on Ser9, myosin light chain 2 (MLC2) on Ser18/Thr19, as well as affixin (2-5). These phosphorylation events are key regulatory steps in modulating the activities of the targets. ILK activity is stimulated by PI3 kinase and negatively regulated by the tumor suppressor PTEN and a PP2C protein phosphatase, ILKAP (1,3,6). It has been suggested that the conserved Ser343 residue in the activation loop plays a key role in the activation of ILK1 (2).

$364
100 tests
100 µl
This Cell Signaling Technology (CST) Antibody was conjugated to Alexa Fluor® 555 fluorescent dye and tested in-house for immunofluorescence in human and mouse cells. The unconjugated Phospho-Histone H3 (Ser10) (D2C8) XP® Rabbit mAb #3377 reacts with phospho-histone H3 (Ser10) from human, mouse, rat, and monkey. CST expects that Phospho-Histone H3 (Ser10) (D2C8) XP® Rabbit mAb (Alexa Fluor® 555 Conjugate) will also recognize phospho-histone H3 (Ser10) in these species.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat, Zebrafish

Application Methods: Immunofluorescence (Immunocytochemistry)

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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The cellular oncogene c-Yes and its viral homologue v-Yes (the transforming gene of Yamaguchi 73 and Esh avian sarcoma viruses) encode a 60 kDa, cytoplasmic, membrane-associated, protein-tyrosine kinase (1). Yes belongs to the Src kinase family and is ubiquitously expressed in many tissues and cells. Like other Src family members, Yes contains several conserved functional domains such as an N-terminal myristoylation sequence for membrane targeting, SH2 and SH3 domains, a kinase domain, and a C-terminal non-catalytic domain (2). Although several lines of evidence support redundancy in signaling between Yes and other Src family kinases, there is also a growing body of evidence indicating specificity in Yes signaling (2). Yes is activated downstream of a multitude of cell surface receptors, including receptor tyrosine kinases, G protein-coupled receptors, and cytokine receptors (3). In addition, both Yes and Src kinases are activated during the cell cycle transition from G2 to M phase (3). Investigators have found that dysfunction of Yes is associated with the development of various cancers (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: NDP52 (CALCOCO2) is ubiquitously expressed and composed of an amino-terminal SKICH domain, followed by a coiled-coil domain, and two zinc finger domains (1). It has recently been reported to act as an autophagy receptor that binds cytosolic ubiquitinated bacteria, leading to autophagy activation and pathogen clearance (1-3). NDP52 binds ubiquitin through its zinc finger domain and simultaneously binds LC3, which directs the bacteria into autophagosomes. In addition, NDP52 interacts with Nap1 and SINTBAD to recruit TBK1 to ubiquitinated bacteria (1).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to the carbohydrate groups of horseradish peroxidase (HRP) via its amine groups. The HRP conjugated antibody is expected to exhibit the same species cross-reactivity as the unconjugated Myc-Tag (71D10) Rabbit mAb #2278.
APPLICATIONS

Application Methods: Western Blotting

Background: Epitope tags are useful for the labeling and detection of proteins using immunoblotting, immunoprecipitation, and immunostaining techniques. Because of their small size, they are unlikely to affect the tagged protein’s biochemical properties.

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

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

Background: The mTORC1 kinase complex is a critical regulator of cell growth (1,2). Its activity is modulated by energy levels, growth factors, and amino acids via signaling through Akt, MAPK, and AMPK pathways (3,4). Recent studies found that the four related GTPases, RagA, RagB, RagC, and RagD, interact with raptor within the mTORC1 complex (1,2). These interactions are both necessary and sufficient for mTORC1 activation in response to amino acid signals (1,2).

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

Application Methods: Western Blotting

Background: Filamins are a family of dimeric actin binding proteins that function as structural components of cell adhesion sites. They also serve as a scaffold for subcellular targeting of signaling molecules (1). The actin binding domain (α-actinin domain) located at the amino terminus is followed by as many as 24 tandem repeats of about 96 residues and the dimerization domain is located at the carboxy terminus. In addition to actin filaments, filamins associate with other structural and signaling molecules such as β-integrins, Rho/Rac/Cdc42, PKC and the insulin receptor, primarily through the carboxy-terminal dimerization domain (1-3). Filamin A, the most abundant, and filamin B are widely expressed isoforms, while filamin C is predominantly expressed in muscle (1). Filamin A is phosphorylated by PAK1 at Ser2152, which is required for PAK1-mediated actin cytoskeleton reorganization (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Vascular endothelial growth factor (VEGF) is a highly specific mitogen for vascular endothelial cells. VEGF and its close relatives VEGF-B, -C and -D form a subfamily within PDGF family of growth factors, which belongs to the cysteine knot class of cytokines. Five VEGF isoforms of 121, 145, 165, 189 and 206 amino acids (VEGF121–206) are generated as a result of alternative splicing from a single VEGF gene (1).The various VEGF forms bind to three tyrosine-kinase receptors, VEGFR-1, VEGFR-2 and VEGFR-3 which are expressed almost exclusively in endothelial cells. VEGFR-2 is the main angiogenic signal transducer for VEGF, while VEGFR-3 is specific for VEGF-C and -D and is necessary and sufficient for lymphangiogenic signaling. However, upon proteolytic processing VEGF-C and -D gain the ability to also bind and activate VEGFR-2 (2). Guided by the binding properties of the ligands, the VEGFRs are able to form both homodimers and heterodimers. Receptor dimerization is accompanied by activation of receptor kinase activity leading to receptor autophosphorylation. Phosphorylated receptors recruit interacting proteins and induce downstream signaling (3). Recently, tumor therapies based on neutralizing anti-VEGF antibodies and small molecule tyrosine kinase inhibitors targeting VEGFRs have been developed. These new strategies for tumor treatment show the clinical relevance of inhibiting VEGF signal transduction pathways that are exaggerated in pathological angiogenesis (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Chromatin IP-seq, Immunoprecipitation, Western Blotting

Background: Mastermind-like (MAML) family of proteins are homologs of Drosophila Mastermind. The family is composed of three members in mammals: MAML1, MAML2, and MAML3 (1,2). MAML proteins form complexes with the intracellular domain of Notch (ICN) and the transcription factor CSL (RBP-Jκ) to regulate Notch target gene expression (3-5). MAML1 also interacts with myocyte enhancer factor 2C (MEF2C) to regulate myogenesis (6). MAML2 is frequently found to be fused with Mucoepidermoid carcinoma translocated gene 1 (MECT1, also know as WAMTP1 or TORC1) in patients with mucoepidermoid carcinomas and Warthin's tumors (7).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Grp75, also known as mortalin, is a member of Hsp70 family of chaperone proteins that is not heat-inducible (1,2). This protein is essential for transporting many mitochondrial proteins from the cytoplasm to mitochondria (3). Grp75 inactivates the tumor suppressor p53 (4). Studies found that Grp75 is overexpressed in many tumor tissues and immortalized human cell lines, suggesting its role in the tumor formation (5). Grp75 is also implicated in cell aging, as its overexpression appears to prolong the life span of human fibroblasts (6).

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

Application Methods: Western Blotting

Background: Pim proteins (Pim-1, Pim-2 and Pim-3) are oncogene-encoded serine/threonine kinases (1). Pim-1, a serine/threonine kinase highly expressed in hematopoietic cells, plays a critical role in the transduction of mitogenic signals and is rapidly induced by a variety of growth factors and cytokines (1-4). Pim-1 cooperates with c-Myc in lymphoid cell transformation and protects cells from growth factor withdrawal and genotoxic stress-induced apoptosis (5,6). Pim-1 also enhances the transcriptional activity of c-Myb through direct phosphorylation within the c-Myb DNA binding domain as well as phosphorylation of the transcriptional coactivator p100 (7,8). Hypermutations of the Pim-1 gene are found in B-cell diffuse large cell lymphomas (9). Phosphorylation of Pim-1 at Tyr218 by Etk occurs following IL-6 stimulation and correlates with an increase in Pim-1 activity (10). Various Pim substrates have been identified; Bad is phosphorylated by both Pim-1 and Pim-2 at Ser112 and this phosphorylation reverses Bad-induced cell apoptosis (11,12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: CCR2 is a member of the “CC-branch” of chemokine G protein-coupled receptors that regulate monocyte chemotaxis and T cell migration/activation and drive inflammation in a number of pathological conditions (1). CCR2 is the receptor for several chemokines including MCP-1, MCP-3, and MCP-4 (2-5). CCR2 transduces signals through increases in intracellular calcium levels. It has two alternative isoforms, CCR2A and CCR2B, differing in their carboxy-terminal tails with CCR2B trafficking more efficiently to the membrane (2,6). CCR2 was originally identified in the THP-1 monocyte cell line, and its expression is decreased following differentiation into macrophages (7). Knockout studies demonstrate that CCR2 is a major regulator of macrophage trafficking (8-10). In addition, research studies have shown that CCR2 functions as an alternative coreceptor with CD4 for infection of some strains of HIV (11,12).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Inositol 1,4,5-triphosphate receptor, also known as IP3R or InsP3R, is a member of the intracellular calcium release channel family and is located in the endoplasmic reticulum. IP3R functions as a Ca2+ release channel for intracellular stores of calcium ions. There are three types of IP3 receptors (IP3R1, 2, and 3) that require the second messenger inositol 1,4,5-triphosphate (IP3) for activation (1). Four individual subunits homo- or hetero-oligomerize to form the receptor's functional channel (2). Phosphorylation of IP3R1 at Ser1756 by cyclic AMP-dependent protein kinase A (PKA) regulates the sensitivity of IP3R1 to IP3 and may be a mode of regulation for Ca2+ release (3,4). IP3R1-mediated Ca2+ release appears to have an effect on the induction of long term depression (LTD) in Purkinje cells (5).

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

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

Background: The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (1). Histone methylation is a major determinant for the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (2,3). Arginine methylation of histones H3 (Arg2, 17, 26) and H4 (Arg3) promotes transcriptional activation and is mediated by a family of protein arginine methyltransferases (PRMTs), including the co-activators PRMT1 and CARM1 (PRMT4) (4). In contrast, a more diverse set of histone lysine methyltransferases has been identified, all but one of which contain a conserved catalytic SET domain originally identified in the Drosophila Su(var)3-9, Enhancer of zeste, and Trithorax proteins. Lysine methylation occurs primarily on histones H3 (Lys4, 9, 27, 36, 79) and H4 (Lys20) and has been implicated in both transcriptional activation and silencing (4). Methylation of these lysine residues coordinates the recruitment of chromatin modifying enzymes containing methyl-lysine binding modules such as chromodomains (HP1, PRC1), PHD fingers (BPTF, ING2), tudor domains (53BP1), and WD-40 domains (WDR5) (5-8). The discovery of histone demethylases such as PADI4, LSD1, JMJD1, JMJD2, and JHDM1 has shown that methylation is a reversible epigenetic marker (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Forkhead box (Fox) proteins are a family of evolutionarily conserved transcription factors containing a sequence known as Forkhead box or winged helix DNA binding domain (1). The human genome contains 43 Fox proteins that are divided into subfamilies. The FoxP subfamily has four members, FoxP1 - FoxP4, which are broadly expressed and play important roles in organ development, immune response and cancer pathogenesis (2-4). The FoxP subfamily has several characteristics that are atypical among Fox proteins: their Forkhead domain is located at the carboxy-terminal region and they contain motifs that promote homo- and heterodimerization. FoxP proteins usually function as transcriptional repressors (4,5).FoxP3 is crucial for the development of T cells with regulatory properties (Treg) (6). Mutations in FoxP3 are associated with immune dysregulation, polyendocrinopathy, enteropathy, and X-linked syndrome (IPEX) (7), while overexpression in mice causes severe immunodeficiency (8). Research studies have shown that FoxP3 functions as a tumor suppressor in several types of cancer (9-11).

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Tyrosine hydroxylase (TH) catalyzes the rate-limiting step in the synthesis of the neurotransmitter dopamine and other catecholamines. TH functions as a tetramer, with each subunit composed of a regulatory and catalytic domain, and exists in several different isoforms (1,2). This enzyme is required for embryonic development since TH knockout mice die before or at birth (3). Levels of transcription, translation and posttranslational modification regulate TH activity. The amino-terminal regulatory domain contains three serine residues: Ser9, Ser31 and Ser40. Phosphorylation at Ser40 by PKA positively regulates the catalytic activity of TH (4-6). Phosphorylation at Ser31 by CDK5 also increases the catalytic activity of TH through stabilization of TH protein levels (7-9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Ubiquitin can be covalently linked to many cellular proteins by the ubiquitination process, which targets proteins for degradation by the 26S proteasome. Three components are involved in the target protein-ubiquitin conjugation process. Ubiquitin is first activated by forming a thiolester complex with the activation component E1; the activated ubiquitin is subsequently transferred to the ubiquitin-carrier protein E2 and then from E2 to ubiquitin ligase E3 for final delivery to the epsilon-NH2 of the target protein lysine residue (1-3). Combinatorial interactions of different E2 and E3 proteins result in substrate specificity (4). Recent data suggests that activated E2 associates transiently with E3, and the dissociation is a critical step for ubiquitination (5). S phase kinase-associated protein 1 (Skp1) is a critical scaffold protein of the Skp1/CUL1/F-box (SCF) E3 ubiquitin ligase protein complex. Various F-box proteins (e.g., β-TrCP, Skp2) mediate an interaction with Skp1, via their defining and conserved domain of 40 amino acids, and with substrates to be ubiquitinated (e.g., β-catenin, p27) (4).

$327
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometric and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Tri-Methyl-Histone H3 (Lys4) (C42D8) Rabbit mAb #9751.
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat, S. cerevisiae

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: The nucleosome, made up of four core histone proteins (H2A, H2B, H3, and H4), is the primary building block of chromatin. Originally thought to function as a static scaffold for DNA packaging, histones have now been shown to be dynamic proteins, undergoing multiple types of post-translational modifications, including acetylation, phosphorylation, methylation, and ubiquitination (1). Histone methylation is a major determinant for the formation of active and inactive regions of the genome and is crucial for the proper programming of the genome during development (2,3). Arginine methylation of histones H3 (Arg2, 17, 26) and H4 (Arg3) promotes transcriptional activation and is mediated by a family of protein arginine methyltransferases (PRMTs), including the co-activators PRMT1 and CARM1 (PRMT4) (4). In contrast, a more diverse set of histone lysine methyltransferases has been identified, all but one of which contain a conserved catalytic SET domain originally identified in the Drosophila Su(var)3-9, Enhancer of zeste, and Trithorax proteins. Lysine methylation occurs primarily on histones H3 (Lys4, 9, 27, 36, 79) and H4 (Lys20) and has been implicated in both transcriptional activation and silencing (4). Methylation of these lysine residues coordinates the recruitment of chromatin modifying enzymes containing methyl-lysine binding modules such as chromodomains (HP1, PRC1), PHD fingers (BPTF, ING2), tudor domains (53BP1), and WD-40 domains (WDR5) (5-8). The discovery of histone demethylases such as PADI4, LSD1, JMJD1, JMJD2, and JHDM1 has shown that methylation is a reversible epigenetic marker (9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Nuclear respiratory factor 1 (NRF1) was identified as a transcription activator for the gene encoding cytochrome c (1). It was later found to play a role in the nuclear control of mitochondrial function (1). PGC-1 induces the expression of NRF1 and NRF2 (2). NRF1, along with the coactivator PGC-1, stimulates the promoter of mitochondrial transcription factor A, which regulates mitochondrial biogenensis and function (2).

$489
96 assays
1 Kit
The PathScan® Total Akt1 Chemiluminescent Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of total Akt1 protein with a chemiluminescent readout. Chemiluminescence ELISAs often have a wider dynamic range and higher sensitivity than conventional chromogenic detection. This chemiluminescent ELISA which is offered in low volume microplates, shows increased signal and sensitivity while using smaller sample size. An Akt rabbit antibody has been coated on the microwells. After incubation with cell lysates, the Akt protein is captured by the coated antibody. Following extensive washing, an Akt1 mouse antibody is added to detect the captured total Akt1 protein. Anti-mouse IgG, HRP-linked antibody is then used to recognize the bound detection antibody. Chemiluminescent reagent is added for signal development. The magnitude of light emission, measured in relative light units (RLU), is proportional to the quantity of total Akt1 protein.
REACTIVITY
Human, Mouse

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, Monkey, Mouse, Rat

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: MTA1 (metastasis associated gene 1) was identified in a differential screening of a cDNA library of metastatic and nonmetastatic adenocarcinoma cell lines (1), and was subsequently found to be an integral member of the nucleosome remodeling and deacetylation (NuRD) complex (2,3). MTA1 expression is upregulated under hypoxic conditions and found to enhance angiogenesis through stabilization of HIF-1α (4,5). MTA1 is overexpressed in a wide range of human cancers, and its expression is associated with malignancy and tumor progression (6). MTA1 is an essential downstream effector of c-Myc transformation (7). Recently, MTA1 was demonstrated to play a role in DNA damage response (8,9).

$269
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme, and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: JunB is a basic region, leucine zipper (bZIP) transcription factor belonging to the Jun family that includes c-Jun and JunD. Jun family members homodimerize or heterodimerize with Fos and ATF proteins to form a functional transcription factor AP-1 (activator protein 1), whose activity is regulated by a variety of physiological and pathological stimuli such as growth factors, infections, and stress signals (1-4). While JunB sometimes antagonizes c-Jun transcriptional activity, it may functionally substitute for c-Jun during development in mice (5-7). JunB regulates hematopoietic stem cell number and plays an important role in the pathogenesis of chronic myelogenous leukemia (CML) and acute myeloid leukemia (AML) (8,9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: TACE (TNF-α converting enzyme), also known as ADAM17, is a transmembrane metalloprotease that plays a key role in the cleavage of a number cell surface molecules in a process known as “shedding". TACE is abundantly expressed in many adult tissues, but in fetal development expression is differentially regulated (1). An important substrate of TACE is pro-TNF-α (1). Increased expression of TACE is associated with several pathological conditions including osteoarthritis and rheumatoid arthritis, where the pro-inflammatory effects of increased TNF-α contribute to disease pathogenesis (2,3). Regulation of other important molecules by TACE such as EGFR and Notch has recently been documented. TACE is responsible for the shedding of EGFR ligands such as amphiregulin and TNF-α. Some tumors have hyperactivated EGFR due to upregulated TNF-α production and upregulated TACE, making TACE a potential target for drug development (4). TACE activates Notch in a ligand-independent manner and has been shown to play a role in the development of the Drosophila nervous system (5). TACE has also been proposed to act as α-secretase for amyloid precursor protein (APP) (6), and to be involved in the renewal and proliferation of neural stem cells (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Western Blotting

Background: Sodium/glucose cotransporter 1 (SGLT1) is an active glucose transporter, which utilizes sodium gradients to transport glucose into cells independent of extracellular glucose concentration. SGLT1 is an essential glucose active transport protein that helps maintain high intracellular glucose levels (1). Expression of SGLT1 is mainly seen in intestinal and kidney epithelial cells, although a recent study also characterized SGLT1 expression in cardiac myocytes (2). Abnormal SGLT1 expression may be associated with cases of type 2 diabetes mellitus and myocardial ischaemia (2). Mutation of the corresponding SGLT1 gene can result in congenital glucose/galactose malabsorption, which can lead to neonatal diarrhea and subsequent death if left untreated (3). A recent study of the role of EGFR in cancer cell survival indicates that EGFR can prevent autophagic cell death independent of EGFR kinase activity because the receptor interacts with and stabilizes SLGT1 to maintain basal intracellular glucose levels (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: GABA (γ-aminobutyric acid) is the primary inhibitory neurotransmitter in the central nervous system and interacts with three different receptors: GABA(A), GABA(B) and GABA(C) receptor. The ionotropic GABA(A) and GABA(C) receptors are ligand-gated ion channels that produce fast inhibitory synaptic transmission. In contrast, the metabotropic GABA(B) receptor is coupled to G proteins that modulate slow inhibitory synaptic transmission (1). Functional GABA(B) receptors form heterodimers of GABA(B)R1 and GABA(B)R2 where GABA(B)R1 binds the ligand and GABA(B)R2 is the primary G protein contact site (2). Two isoforms of GABA(B)R1 have been cloned: GABA(B)R1a is a 130 kD protein and GABA(B)R1b is a 95 kD protein (3). G proteins subsequently inhibit adenyl cylase activity and modulate inositol phospholipid hydrolysis. GABA(B) receptors have both pre- and postsynaptic inhibitions: presynaptic GABA(B) receptors inhibit neurotransmitter release through suppression of high threshold calcium channels, while postsynaptic GABA(B) receptors inhibit through coupled activation of inwardly rectifying potassium channels. In addition to synaptic inhibition, GABA(B) receptors may also be involved in hippocampal long-term potentiation, slow wave sleep and muscle relaxation (1).

$327
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct flow cytometry and immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-S6 Ribosomal Protein (Ser235/236) (2F9) Rabbit mAb #4856.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: One way that growth factors and mitogens effectively promote sustained cell growth and proliferation is by upregulating mRNA translation (1,2). Growth factors and mitogens induce the activation of p70 S6 kinase and the subsequent phosphorylation of the S6 ribosomal protein. Phosphorylation of S6 ribosomal protein correlates with an increase in translation of mRNA transcripts that contain an oligopyrimidine tract in their 5' untranslated regions (2). These particular mRNA transcripts (5'TOP) encode proteins involved in cell cycle progression, as well as ribosomal proteins and elongation factors necessary for translation (2,3). Important S6 ribosomal protein phosphorylation sites include several residues (Ser235, Ser236, Ser240, and Ser244) located within a small, carboxy-terminal region of the S6 protein (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Melanoma cell adhesion molecule (MCAM, MUC18, CD146) is an immunoglobulin superfamily member originally described as a cell surface adhesion protein and marker of the progression and metastasis of melanoma (1,2). Expression of MCAM protein is seen in vascular endothelial cells, activated T lymphocytes, smooth muscle, and bone marrow stromal cells. Research studies demonstrate increased MCAM expression in endothelial cells from angiogenesis-related disorders, including inflammatory bowel disease, Crohn’s disease, rheumatoid arthritis, tumors, and chronic renal failure (3). MCAM-expressing human mesenchymal stromal cells (hMSC) in the hematopoietic microenvironment are responsible for maintaining the self-renewal of hematopoietic stem and progenitor cells (HSPC) through direct contact between hMSC and those cells (2). Related studies suggest that activation of the Notch signaling pathway may also, in part, play a role in HSPC maintenance (4). Additional research indicates that MCAM may play a role in multiple sclerosis, an autoimmune inflammatory disease that affects central nervous system neurons. Endothelial MCAM within the blood-brain barrier act as adhesion receptors that permit lymphocytes to transmigrate across the barrier and produce the inflammatory lesions that characterize the disorder (5).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct immunofluorescent analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated α-Smooth Muscle Actin (D4K9N) XP® Rabbit mAb #19245.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen)

Background: Actin proteins are major components of the eukaryotic cytoskeleton. At least six vertebrate actin isoforms have been identified. The cytoplasmic β- and γ-actin proteins are referred to as “non-muscle” actin proteins as they are predominantly expressed in non-muscle cells where they control cell structure and motility (1). The α-cardiac and α-skeletal actin proteins are expressed in striated cardiac and skeletal muscles, respectively. The smooth muscle α-actin and γ-actin proteins are found primarily in vascular smooth muscle and enteric smooth muscle, respectively. The α-smooth muscle actin (ACTA2) is also known as aortic smooth muscle actin. These actin isoforms regulate the contractile potential of muscle cells (1).