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Product listing: PU.1 (9G7) Rabbit mAb (PE Conjugate), UniProt ID P17947 #81886 to NXF1 (D5X4G) Rabbit mAb, UniProt ID Q9UBU9 #12735

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated PU.1 (9G7) Rabbit mAb #2258.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: PU.1 is a member of the Ets family of transcription factors and activates target genes through the purine-rich PU-box (1). PU.1 plays a pivotal role in the differentiation of myeloid cells and lymphocytes and is expressed in several hematopoietic cells including B lymphocytes, macrophages, neutrophils, mast cells, early erythroid cells, and megakaryocytes (1,2). The concentration of PU.1 is critical for both the determination of hematopoietic cell lineage and the regulation of differentiation versus stem cell proliferation (3,4). In addition, PU.1 activity is influenced by phosphorylation and interactions with other hematopoietic transcription factors. Phosphorylation of PU.1 at Ser146 by CK2 promotes binding to IRF4 and synergistic activation through the immunoglobulin κ 3' enhancer (5). Treatment of pro-B cells with IL-3 leads to phosphorylation of PU.1 at Ser140, resulting in increased PU.1 activity and activation of the anti-apoptotic gene MCL-1 (6). GATA1 binding blocks PU.1 activity during erythroid cell development (7). Overexpression of PU.1 resulting from proviral insertion during Friend virus infection can induce erythroleukemia, while reduced expression has been associated with acute myeloid leukemia (8).

$327
100 µl
This Cell Signaling Technology (CST) antibody is conjugated to biotin under optimal conditions. The unconjugated Phospho-NF-κB p65 (Ser536) (93H1) Rabbit mAb #3033 reacts with human, mouse, rat, monkey, hamster, and pig phospho-NF-κB. CST expects that Phospho-NF-κB p65 (Ser536) (93H1) Rabbit mAb (Biotinylated) will also recognize phospho-NF-κB in these species.
APPLICATIONS
REACTIVITY
Hamster, Human, Monkey, Mouse, Pig, Rat

Application Methods: Western Blotting

Background: Transcription factors of the nuclear factor κB (NF-κB)/Rel family play a pivotal role in inflammatory and immune responses (1,2). There are five family members in mammals: RelA, c-Rel, RelB, NF-κB1 (p105/p50), and NF-κB2 (p100/p52). Both p105 and p100 are proteolytically processed by the proteasome to produce p50 and p52, respectively. Rel proteins bind p50 and p52 to form dimeric complexes that bind DNA and regulate transcription. In unstimulated cells, NF-κB is sequestered in the cytoplasm by IκB inhibitory proteins (3-5). NF-κB-activating agents can induce the phosphorylation of IκB proteins, targeting them for rapid degradation through the ubiquitin-proteasome pathway and releasing NF-κB to enter the nucleus where it regulates gene expression (6-8). NIK and IKKα (IKK1) regulate the phosphorylation and processing of NF-κB2 (p100) to produce p52, which translocates to the nucleus (9-11).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Members of the F-box family of proteins are characterized by the approximate 40 amino acid F-box motif named after cyclin F (1,2). F-box proteins constitute one of the four subunits of the Skp1-Cullin-F-box (SCF) ubiquitin ligase complex. The substrate specificity of SCF complexes is determined by the interchangeable F-box proteins, which act as adaptors by associating with phosphorylated substrate proteins and recruiting them to the SCF core. F-box proteins contain two fundamental domains: the F-box motif mediates binding to Skp1 and a leucine rich repeat (LRR) domain mediates substrate interactions.

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 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 antibody (GAPDH (14C10) Rabbit mAb #2118).
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Pig, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

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).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Docking proteins are substrates of tyrosine kinases that function in the recruitment and assembly of specific signal transduction molecules. There are five members in the p62dok family, p62Dok (Dok-1), p56Dok-2 (Dok-2, or DoK-R), Dok-3, Dok-4 and Dok-5 (1-3), characterized by the presence of an amino-terminal PH domain, a central PTB domain and numerous potential sites of tyrosine phosphorylation. Tyrosine phosphorylation of p56Dok-2 occurs upon stimulation of cells with a variety of stimuli, or in cells transformed by oncogenic tyrosine kinases such as v-Src and Bcr-Abl (3-5). Based on the presence of several signaling domains (PH, PTB domain, tyrosine residue and proline-rich regions), it has been proposed that the p62dok family act as docking proteins that link RTKs to signal transduction pathways. p56Dok-2 has been proposed to be a negative regulator of cytokine-induced proliferation in T cells (5). Phosphorylated Tyr351 of p56Dok-2 mediates an association with the SH2 domain of Nck (4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Vascular endothelial growth factor receptor 2 (VEGFR2, KDR, Flk-1) is a major receptor for VEGF-induced signaling in endothelial cells. Upon ligand binding, VEGFR2 undergoes autophosphorylation and becomes activated (1). Major autophosphorylation sites of VEGFR2 are located in the kinase insert domain (Tyr951/996) and in the tyrosine kinase catalytic domain (Tyr1054/1059) (2). Activation of the receptor leads to rapid recruitment of adaptor proteins, including Shc, GRB2, PI3 kinase, NCK, and the protein tyrosine phosphatases SHP-1 and SHP-2 (3). Phosphorylation at Tyr1212 provides a docking site for GRB2 binding and phospho-Tyr1175 binds the p85 subunit of PI3 kinase and PLCγ, as well as Shb (1,4,5). Signaling from VEGFR2 is necessary for the execution of VEGF-stimulated proliferation, chemotaxis and sprouting, as well as survival of cultured endothelial cells in vitro and angiogenesis in vivo (6-8).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 594 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 LC3A/B (D3U4C) XP® Rabbit mAb #12741.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation, but it has also been associated with a number of physiological processes including development, differentiation, neurodegenerative diseases, infection, and cancer (3). Autophagy marker Light Chain 3 (LC3) was originally identified as a subunit of microtubule-associated proteins 1A and 1B (termed MAP1LC3) (4) and subsequently found to contain similarity to the yeast protein Apg8/Aut7/Cvt5 critical for autophagy (5). Three human LC3 isoforms (LC3A, LC3B, and LC3C) undergo post-translational modifications during autophagy (6-9). Cleavage of LC3 at the carboxy terminus immediately following synthesis yields the cytosolic LC3-I form. During autophagy, LC3-I is converted to LC3-II through lipidation by a ubiquitin-like system involving Atg7 and Atg3 that allows for LC3 to become associated with autophagic vesicles (6-10). The presence of LC3 in autophagosomes and the conversion of LC3 to the lower migrating form, LC3-II, have been used as indicators of autophagy (11).

$303
100 µl
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Immunoprecipitation, Peptide ELISA (DELFIA), Western Blotting

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Etk, also known as BMX, is a member of the Bruton's tyrosine kinase (Btk) family (1). It is expressed in a variety of hematopoietic, epithelial and endothelial cells. Etk, like other Btk family members, contains a pleckstrin homology (PH) domain and Src homology SH3 and SH2 domains. It participates in multiple signal transduction pathways (2). Phosphorylation of Tyr566 by Src kinase is required for activation of Etk in vivo (3). In endothelial and epithelial cells, Etk is regulated by FAK through phosphorylation at Tyr40 (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 flow cytometric and immunofluorescent analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated COX IV (3E11) Rabbit mAb #4850.
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Pig, Rat, Zebrafish

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Cytochrome c oxidase (COX) is a hetero-oligomeric enzyme consisting of 13 subunits localized to the inner mitochondrial membrane (1-3). It is the terminal enzyme complex in the respiratory chain, catalyzing the reduction of molecular oxygen to water coupled to the translocation of protons across the mitochondrial inner membrane to drive ATP synthesis. The 3 largest subunits forming the catalytic core are encoded by mitochondrial DNA, while the other smaller subunits, including COX IV, are nuclear-encoded. Research studies have shown that deficiency in COX activity correlates with a number of human diseases (4). The COX IV antibody can be used effectively as a mitochondrial loading control in cell-based research assays.

$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: N-methyl-D-aspartate receptor (NMDAR) forms a heterodimer of at least one NR1 and one NR2A-D subunit. Multiple receptor isoforms with distinct brain distributions and functional properties arise by selective splicing of the NR1 transcripts and differential expression of the NR2 subunits. NR1 subunits bind the co-agonist glycine and NR2 subunits bind the neurotransmitter glutamate. Activation of the NMDA receptor or opening of the ion channel allows flow of Na+ and Ca2+ ions into the cell, and K+ out of the cell (1). Each subunit has a cytoplasmic domain that can be directly modified by the protein kinase/phosphatase (2). PKC can phosphorylate the NR1 subunit (NMDAR1) of the receptor at Ser890/Ser896, and PKA can phosphorylate NR1 at Ser897 (3). The phosphorylation of NR1 by PKC decreases its affinity for calmodulin, thus preventing the inhibitory effect of calmodulin on NMDAR (4). The phosphorylation of NR1 by PKA probably counteracts the inhibitory effect of calcineurin on the receptor (5). NMDAR mediates long-term potentiation and slow postsynaptic excitation, which play central roles in learning, neurodevelopment, and neuroplasticity (6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Class II phosphatidylinositol 3-kinases (PI3K) contain a C-terminal C2 domain that is unique to the class II isoforms of the PI3K family. This C2 domain mediates protein and phospholipid binding acitivities (1,2). PI3K Class II α generates phosphatidylinositol 3-phosphate (PIP3) and phosphatidylinositol 3,4-bisphosphate (PI(3, 4)P2) from phosphatidylinositol and phosphatidylinositol 4-phosphate (3). PI3K Class II α is located in various intracellular locations such as the trans-Golgi network, endocytic compartments, clathrin-coated vesicles, and nuclear speckles (1,4,5). Research studies have indicated that PI3K Class II α regulates the assembly and distribution of clathrin, resulting in the modulation of clathrin-dependent trafficking and sorting within the trans Golgi network (5,6). PI3K Class II α also mediates translocation of the glucose transporter GLUT4 to the plasma membrane in response to insulin (7). PI3K Class II α has also been shown to regulate neurosecretory granule exocytosis (8) and vascular smooth muscle contraction (9). Unlike other PI3K family members, PI3K Class II α is less sensitive to the PI3K inhibitors wortmannin and LY294002 (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Bcr gene was orginally identified by its presence in the chimeric Bcr-Abl oncogene (1). The amino-terminal region of Bcr contains an oligomerization domain, a serine/threonine kinase domain, and a region that binds SH2 domains. The middle of the protein has a PH domain and a region of sequence similarity to the guanine nucleotide exchange factors for the Rho family of GTP binding proteins. The carboxy-terminal region may be involved in a GTPase activating function for the small GTP-binding protein Rac (2,3). The function of wild type Bcr in cells remains unclear. PDGF receptor may use Bcr as a downstream signaling mediator (4). Research studies have shown that the Bcr-Abl fusion results in production of a constitutively active tyrosine kinase, which causes chronic myelogenous leukemia (CML) (5). Tyr177 of Bcr is phosphorylated in the Bcr-Abl fusion protein, which plays an important role in transforming the activity of Bcr-Abl (6). Phosphorylated Tyr177 provides a docking site for Gab2 and GRB2 (7,8).

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Ras activity is regulated by GAP (GTPase activating proteins) and GEFs (guanine nucleotide exchange factors). Ras-GRF1 (also known as CDC25Mm) is neuronal RasGEF and is regulated by heterotrimeric G proteins and calcium influx (1,2). Binding to calmodulin and phosphorylation stimulate Ras-GRF1 activity (1,2). Multiple PKA phosphorylation sites on Ras-GRF have been identified. Phosphorylation on the two major sites, Ser54 and Ser822, inhibits Ras-GRF activity (3). Carbachol (a muscarinic agonist)-induced phosphorylation on Ser916 is essential but not sufficient for maximal Ras-GRF activity (4). It has been reported that Ras-GRF1 also shows GEF activity toward Rac after phosphorylation by the tyrosine kinase Src (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Bim/Bod is a pro-apoptotic protein belonging to the BH3-only group of Bcl-2 family members including Bad, Bid, Bik, Hrk, and Noxa that contain a BH3 domain but lack other conserved BH1 or BH2 domains (1,2). Bim induces apoptosis by binding to and antagonizing anti-apoptotic members of the Bcl-2 family. Interactions have been observed with Bcl-2, Bcl-xL, Mcl-1, Bcl-w, Bfl-1, and BHRF-1 (1,2). Bim functions in regulating apoptosis associated with thymocyte negative selection and following growth factor withdrawal, during which Bim expression is elevated (3-6). Three major isoforms of Bim are generated by alternative splicing: BimEL, BimL, and BimS (1). The shortest form, BimS, is the most cytotoxic and is generally only transiently expressed during apoptosis. The BimEL and BimL isoforms may be sequestered to the dynein motor complex through an interaction with the dynein light chain and released from this complex during apoptosis (7). Apoptotic activity of these longer isoforms may be regulated by phosphorylation (8,9). Environmental stress triggers Bim phosphorylation by JNK and results in its dissociation from the dynein complex and increased apoptotic activity.

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

Application Methods: Immunoprecipitation, Western Blotting

Background: TAK1 is a mitogen-activated protein kinase kinase kinase activated by TGF-β and various pro-inflammatory signals (1,2). In vivo, TAK1 activation requires its association with TAK1 binding protein 1 (TAB1), which triggers TAK1 autophosphorylation at Thr184 and Thr187 (3,4). The TAB2 adaptor protein links TAK1 with TRAF6 to mediate TAK1 activation following IL-1 stimulation (5). Once activated, TAK1 phosphorylates the MAPK kinases MKK4 and MKK3/6, which activate JNK and p38 MAPK, respectively. TAK1 and TRAF6 also activate the NF-κB pathway by phosphorylating the NF-κB inducing kinase (NIK) to trigger subsequent activation of IKK (2,6). In addition to TAK1, TAB1 interacts with and activates p38α MAPK (7). Targeted disruption of the TAB1 gene in mice causes a drastic reduction in TAK1 activity and leads to embryonic lethality (8).

$305
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 in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated mTOR (7C10) Rabbit mAb #2983.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The mammalian target of rapamycin (mTOR, FRAP, RAFT) is a Ser/Thr protein kinase (1-3) that functions as an ATP and amino acid sensor to balance nutrient availability and cell growth (4,5). When sufficient nutrients are available, mTOR responds to a phosphatidic acid-mediated signal to transmit a positive signal to p70 S6 kinase and participate in the inactivation of the eIF4E inhibitor, 4E-BP1 (6). These events result in the translation of specific mRNA subpopulations. mTOR is phosphorylated at Ser2448 via the PI3 kinase/Akt signaling pathway and autophosphorylated at Ser2481 (7,8). mTOR plays a key role in cell growth and homeostasis and may be abnormally regulated in tumors. For these reasons, mTOR is currently under investigation as a potential target for anti-cancer therapy (9).

$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: PZR (Protein zero related) is an immunoglobulin superfamily protein that specifically binds the tyrosine phosphatase SHP-2 through its intracellular immunoreceptor tyrosine-based inhibitory motifs (ITIMs) (1,2). PZR is phosphorylated by c-Src, c-Fyn, c-Lyn, Csk, and c-Abl (3). PP1, a Src family kinase inhibitor, inhibits PZR phosphorylation (4,5). There are three alternatively spliced isoforms, designated as PZR, PZRa, and PZRb; both PZRa and PZRb lack ITIMs (6,7). PZR is the main receptor of ConA and has an important role in cell signaling via c-Src (4). PZR is expressed in many cell types and is localized to cell contacts and intracellular granules in BAECs and mesothelioma (REN) cells. PZR has been implicated as a cell adhesion protein that may be involved in SHP-2-dependent signaling at interendothelial cell contacts (3). Hypertyrosine phosphorylation of PZR was observed during embryogenesis in a mouse model of Noonan syndrome (8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Human progesterone receptor (PR) is expressed as two forms: the full length PR-B and the short form PR-A. PR-A lacks the first 164 amino acid residues of PR-B (1,2). Both PR-A and PR-B are ligand activated, but differ in their relative ability to activate target gene transcription (3,4). The activity of PR is regulated by phosphorylation; at least seven serine residues are phosphorylated in its amino-terminal domain. Three sites (Ser81, Ser102, and Ser162) are unique to full length PR-B, while other sites (Ser190, Ser294, Ser345, and Ser400) are shared by both isoforms (5). Phosphorylation of PR-B at Ser190 (equivalent to Ser26 of PR-A) is catalyzed by CDK2 (6). Mutation of Ser190 results in decreased activity of PR (7), suggesting that the phosphorylation at Ser190 may be critical to its biological function.

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The cdc2-like kinase (CLK) family contains at least four highly conserved isoforms: CLK1, CLK2, CLK3 and CLK4 (1,2). CLKs are dual specificity kinases that autophosphorylate on serine, threonine and tyrosine residues and phosphorylate exogenous substrates on serine and threonine residues (2). CLK family members exist as both a full-length catalytically active form and an alternatively-spliced, inactive truncated form (1). A family of highly phosphorylated proteins, called serine and arginine rich (SR) proteins, are phosphorylated by CLKs (3-5). SR proteins are splicing factors that regulate the assembly of the spliceosome, a macromolecular complex where RNA splicing occurs in the nucleus. They are also involved in the selection of splice sites. Thus, CLKs may play important roles in regulating RNA splicing.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Forkhead box M1 (FoxM1) is a forkhead box family transcription factor that regulates a number of genes throughout the cell cycle to help control DNA replication, mitosis, and cell proliferation. FoxM1 expression increases during G1 and S and reaches maximum levels in G2/M (1-3). Nuclear translocation occurs just before entry into G2/M and is associated with FoxM1 phosphorylation (4). Phosphorylation of FoxM1 by MAPK (Ser331, Ser704), Cyclin/Cdk (Ser4, Ser35, Thr600, Thr611, Thr620, Thr627, Ser638), Plk1 (Ser715, Ser724), and Chk2 (Ser376) stabilizes and activates FoxM1 (4-8). Forkhead box M1 is expressed in all embryonic tissues but is restricted to proliferating tissues in adults (9). Research studies show that FoxM1 expression is negatively regulated by p53 (10,11). Upregulation of FoxM1 is associated with many human cancers, including prostate, breast, lung, ovary, colon, pancreas, stomach, bladder, liver, and kidney, and may be associated with p53 mutations in some tumors (11,12). As a result, FoxM1 inhibitors have become a topic of interest for potential cancer therapy (13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Engulfment and cell motility 1 (ELMO1) is a cell motility and migration protein that interacts with DOCK180 to form an atypical, two-part guanine nucleotide exchange factor (GEF) for the small GTPase Rac (1). The resultant localized Rac activation allows actin nucleation via WAVE family proteins, signaling to integrins, formation of lamellipodia and filopodia, and regulation of processes including phagocytosis and cell migration (2-4). Research studies indicate that DOCK180 and ELMO1 regulate cell migration in lymphocytes (5) and in ovarian cancer cells (6). ELMO1 also promotes Rac1-dependent cell motility through its interaction with the adaptor protein Nck-1 (7), and binds Arhgef16 to promote RhoG/Rac1-dependent engulfment of apoptotic cells by phagocytes (8). Polymorphisms in the corresponding ELMO1 gene may be associated with susceptibility to diabetic neuropathy seen in selected populations of type II diabetic patients (9,10).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Rat

Application Methods: Western Blotting

Background: AMPA- (α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid), kainate-, and NMDA- (N-methyl-D-aspartate) receptors are the three main families of ionotropic glutamate-gated ion channels. AMPA receptors (AMPARs) are comprised of four subunits (GluR 1-4), which assemble as homo- or hetero-tetramers to mediate the majority of fast excitatory transmissions in the central nervous system. AMPARs are implicated in synapse formation, stabilization, and plasticity (1). In contrast to GluR 2-containing AMPARs, AMPARs that lack GluR 2 are permeable to calcium (2). Post-transcriptional modifications (alternative splicing, nuclear RNA editing) and post-translational modifications (glycosylation, phosphorylation) result in a very large number of permutations, fine-tuning the kinetic properties of AMPARs. Research studies have implicated activity changes in AMPARs in a variety of diseases including Alzheimer’s, amyotrophic lateral sclerosis (ALS), stroke, and epilepsy (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: Neural cell adhesion molecule L1 (NCAM-L1/L1CAM) is a single pass transmembrane glycoprotein member of the immunoglobulin superfamily, containing six amino-terminal extracellular Ig-like domains followed by five fibronectin type-III domains (1). NCAM-L1 is mainly expressed in the brain, and plays an important role in the developing nervous system, with involvement in neurite fasciculation and outgrowth, myelination, neuronal migration, and neuronal cell adhesion (2). Mutations in the NCAM-L1 gene cause varying degrees of neurological disease including X-linked hydrocephalus, MASA syndrome, spastic paraplegia type 1, and X-linked corpus callosum agenesis, together known as L1 syndrome (3). Apart from the nervous system, NCAM-L1 is overexpressed in many cancers and supports a poor prognosis by facilitating aggressive tumor growth, metastasis and chemoresistance (4,5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Apolipoproteins are plasma lipoproteins that function as transporters of lipids and cholesterol in the circulatory system. Chylomicrons are a fundamental class of apolipoproteins containing very low-density lipoproteins (VLDL), intermediate-density lipoproteins (IDL), low-density lipoproteins (LDL), and high-density lipoproteins (HDL) (1,2).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: AML1 (also known as Runx1, CBFA2, and PEBP2αB) is a member of the core binding factor (CBF) family of transcription factors (1,2). It is required for normal development of all hematopoietic lineages (3-5). AML1 forms a heterodimeric DNA binding complex with its partner protein CBFβ and regulates the expression of cellular genes by binding to promoter and enhancer elements. AML1 is commonly translocated in hematopoietic cancers: chromosomal translocations include t(8;21) AML1-ETO, t(12;21) TEL-AML, and t(8;21) AML-M2 (6). Phosphorylation of AML1 on several potential serine and threonine sites, including Ser249, is thought to occur in an Erk-dependent manner (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The neurotransmitters GABA and glycine activate ligand-gated chloride channels and thus mediate fast synaptic inhibition. Gephyrin is a postsynaptic, scaffolding protein anchoring type A GABA and glycine receptors to the cytoskeleton. In addition to gephyrin’s function clustering synaptic neurotransmitter receptors, it plays an essential role in the biosynthesis of the molybdenum cofactor (MoCo). Molybdenum cofactor chelates and activates sulfite oxidase, an enzyme crucial for survival (1). GSK-3β and Erk1/2 phosphorylate gephyrin at residue Ser270 and Ser268, respectively. These post-translational modifications alter the clustering of gephyrin, effecting the amplitude and frequency of GABAergic inhibitory currents (2,3). Researchers are analyzing the role of abnormal gephyrin clustering and function in major neurological, neuro-developmental and psychiatric disorders (1).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Pacific Blue™ fluorescent dye and tested in-house for direct flow cytometry in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated antibody IκBα (L35A5) Mouse mAb (Amino-terminal Antigen) #4814.
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Mouse, Pig, Rat

Application Methods: Flow Cytometry

Background: The NF-κB/Rel transcription factors are present in the cytosol in an inactive state complexed with the inhibitory IκB proteins (1-3). Activation occurs via phosphorylation of IκBα at Ser32 and Ser36 followed by proteasome-mediated degradation that results in the release and nuclear translocation of active NF-κB (3-7). IκBα phosphorylation and resulting Rel-dependent transcription are activated by a highly diverse group of extracellular signals including inflammatory cytokines, growth factors, and chemokines. Kinases that phosphorylate IκB at these activating sites have been identified (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The breast cancer susceptibility gene, BRCA1, codes for an E3 ubiquitin ligase that functions in the maintenance of genome stability through regulation of DNA damage response and DNA repair. BRCA1 forms at least three distinct complexes (BRCA1 A, B, and C) with other DNA repair proteins, and these interactions are vital for the regulation of BRCA1 function. The BRCA1-Rap80 complex (BRCA1 A complex), including Rap80, BRCC36, BRCC45, Abraxas, and MERIT40/NBA1, functions in G2/M phase checkpoint control (reviewed in 1,2).MERIT40/NBA1 localizes to sites of DNA damage and is required for the appropriate localization of BRCA1 in response to ionizing radiation, as well as maintenance of the BRCA1 A complex (3,4). Proteomics studies have identified Ser29 as a phosphorylated site on MERIT40/NBA1, and the significance of this phosphorylation is under investigation (5-9).

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

Application Methods: Western Blotting

Background: mRNA export is a process that is tightly coupled to mRNA splicing (1-4). Splicing and packaging of mRNAs in the form of an mRNA-protein complex (mRNP) leads to the recruitment of the mRNA export adaptor THOC4/ALY, via its interaction with the splicing factor UAP56, forming a large complex termed the transcription-export complex (TREX) (1,2,5). THOC4/ALY then directly interacts with NXF1/TAP, a part of the heterodimer that targets the mRNP to the nuclear pore complex, resulting in the shuttling of mRNP out of the nucleus and into the cytoplasm (1-3,6).