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Product listing: RARα (E6Z6K) Rabbit mAb, UniProt ID P10276 #62294 to RCAS1 (D2B6N) XP® Rabbit mAb (PE Conjugate), UniProt ID O00559 #98856

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Retinoids (vitamin A and its active retinoic acid derivatives) are non-steroid hormones that regulate cell proliferation, differentiation and apoptosis. Retinoic acid receptors (RARalpha, -beta and -gamma) and retinoid X receptors (RXRalpha, -beta and -gamma) are nuclear receptors that function as RAR-RXR heterodimers or RXR homodimers (1-2). In response to retinoid binding, these dimers control gene expression by binding to specific retinoic acid response elements, by recruiting cofactors and the transcriptional machinery, and by indirectly regulating chromatin structure. Finally, ligand binding and phosphorylation of RARalpha by JNK at Thr181, Ser445 and Ser461 controls the stability of RAR-RXR through the ubiquitin-proteasome pathway (3-4). At least four distinct genetic lesions affect RARalpha and result in acute promyelocytic leukemia (APL). The t(15;17) translocation that results in the PML-RARalpha fusion protein is responsible for more than 99% of APL cases, and the fusion protein inhibits PML-dependent apoptotic pathways in a dominant negative fashion. In addition PML-RARalpha inhibits transcription of retinoic acid target genes by recruiting co-repressors, attenuating myeloid differentiation (5-6).

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

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

Background: Nuclear retinoic acid (RA) receptors (RARs) consist of three subtypes encoded by separate genes: α (NR1B1), β (NR1B2), and γ (NR1B3). For each subtype, there are at least two isoforms, which are generated by differential promoter usage and alternative splicing and differ only in their N-terminal regions. Retinoids, which are metabolites of vitamin A, serve as ligands for RARs (1). RARs function as ligand-dependent transcriptional regulators and are found to be heterodimerized with retinoid X receptors (RXRs). These transcriptionally active dimers regulate the expression of genes involved in cellular differentiation, proliferation, and apoptosis (2,3). Consequently, RARs play critical roles in a variety of biological processes, including development, reproduction, immunity, and organogenesis (4-6). RAR mutations, fusion proteins, altered expression levels, or aberrant post-translational modifications result in multiple diseases due to altered RAR function and disruption of homeostasis.In contrast to the ubiquitously expressed RARα subtype, RARγ displays a complex tissue-specific expression pattern (7). The hematopoietic system expresses significant levels of RARγ, and a recent study identified a role for RARγ in hematopoietic stem cell maintenance (8). RARγ is the predominant subtype in human and mouse epidermis, representing 90% of the RARs in this tissue (9-11). Given the high level of RARγ expression in the skin, it has been suggested that this nuclear receptor participates in a transcriptional program that governs maintenance and differentiation of normal epidermis and skin appendages. The transcriptional activity of RARγ is under stringent control, in part, through retinoic acid-induced phosphorylation and proteasomal degradation (12).

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

Application Methods: Western Blotting

Background: The 21 kDa guanine-nucleotide binding proteins (K-Ras, H-Ras, and N-Ras) cycle between active (GTP-bound) and inactive (GDP-bound) forms (1). Receptor tyrosine kinases and G protein-coupled receptors activate Ras, which then stimulates the Raf-MEK-MAPK pathway (2-4). GTPase-activating proteins (GAP) normally facilitate the inactivation of Ras. However, research studies have shown that in 30% of human tumors, point mutations in Ras prevent the GAP-mediated inhibition of this pathway (5). The most common oncogenic Ras mutation found in tumors is Gly12 to Asp12 (G12D), which prevents Ras inactivation, possibly by increasing the overall rigidity of the protein (5,6).

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

Application Methods: Western Blotting

Background: The 21 kDa guanine-nucleotide binding proteins (K-Ras, H-Ras, and N-Ras) cycle between active (GTP-bound) and inactive (GDP-bound) forms (1). Receptor tyrosine kinases and G protein-coupled receptors activate Ras, which then stimulates the Raf-MEK-MAPK pathway (2-4). GTPase-activating proteins (GAP) normally facilitate the inactivation of Ras. However, research studies have shown that in 30% of human tumors, point mutations in Ras prevent the GAP-mediated inhibition of this pathway (5). The most common oncogenic Ras mutation found in tumors is Gly12 to Asp12 (G12D), which prevents Ras inactivation, possibly by increasing the overall rigidity of the protein (5,6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The 21 kDa guanine-nucleotide binding proteins (K-Ras, H-Ras, and N-Ras) cycle between active (GTP-bound) and inactive (GDP-bound) forms (1). Receptor tyrosine kinases and G protein-coupled receptors activate Ras, which then stimulates the Raf-MEK-MAPK pathway (2-4). GTPase-activating proteins (GAP) normally facilitate the inactivation of Ras. However, research studies have shown that in 30% of human tumors, point mutations in Ras prevent the GAP-mediated inhibition of this pathway (5). The most common oncogenic Ras mutation found in tumors is Gly12 to Asp12 (G12D), which prevents Ras inactivation, possibly by increasing the overall rigidity of the protein (5,6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The 21 kDa guanine-nucleotide binding proteins (K-Ras, H-Ras, and N-Ras) cycle between active (GTP-bound) and inactive (GDP-bound) forms (1). Receptor tyrosine kinases and G protein-coupled receptors activate Ras, which then stimulates the Raf-MEK-MAPK pathway (2-4). GTPase-activating proteins (GAP) normally facilitate the inactivation of Ras. However, research studies have shown that in 30% of human tumors, point mutations in Ras prevent the GAP-mediated inhibition of this pathway (5). The most common oncogenic Ras mutation found in tumors is Gly12 to Asp12 (G12D), which prevents Ras inactivation, possibly by increasing the overall rigidity of the protein (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Small GTPases 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. RASAL2 was initially identified as a GAP for the small GTPase, Ras, and later shown to interact with the Rho-GEF ECT2, and to regulate Rho activity in human astrocytoma cells (1).Researchers have implicated RASAL2 as a suppressor of migration and metastasis in human cancer (2), and have shown that RASAL2 downregulation promotes epithelial-mesenchymal transition and metastasis in ovarian cancer (3) and lung cancer (4). Conversely, other research studies show that RASAL2 can be oncogenic in triple negative breast cancer through activation of Rac1 signaling (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Lymphocyte activation occurs in part through activation of the Ras signaling pathway following lymphocyte receptor stimulation. The RasGRP family of guanine nucleotide exchange factors (GEFs) catalyzes the exchange of GDP for GTP on Ras family small GTPases, promoting their active GTP-bound form. Diacylglycerol (DAG) or phorbol ester binding to RasGRP family members causes their translocation to the cell membrane and stimulates their activity (1,2). While T-Cells express RasGRP1, B-cells express both RasGRP1 and RasGRP3. RasGRP3 is important in linking B-cell receptor (BCR) activation to Ras signaling (3). In response to BCR stimulation, RasGRP3 is phosphorylated at Thr133 by PKC. This phosphorylation event further activates RasGRP3 in response to DAG, which stimulates PKC activity (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Ras association domain-containing protein 1 (RASSF1) is a member of the RASSF protein family (RASSF1-10), scaffold proteins whose members are unified by the presence of a Ras association (RA) domain that gives them structural similarity to Ras effector proteins (1). The RASSF1 gene is located in a genomic region exhibiting loss of heterozygosity in a more than 90% of small cell lung cancers, and up to 50% of non-small cell lung cancers (2), strongly implicating the RASSF1 gene as a tumor suppressor. Moreover, RASSF1 expression in tumor cells has been shown to be frequently suppressed by promoter hypermethylation, further suggesting a tumor suppressor function (3-5). Although multiple isoforms (RASSF1A-H) have been described, generated by alternative splicing and/or promoter usage, RASSF1A and RASSF1C appear to be the most widely expressed in normal tissues, with RASSF1A expression lost most frequently in tumor cells (6). Notably, RASSF1A has been identified as an effector protein in the Hippo signaling pathway, where it promotes association between MST1/2 and LATS1/2, leading to suppressive phosphorylation of the transcriptional co-activators YAP and TAZ (7).

$139
100 µg
This Cell Signaling Technology antibody is conjugated to APC under optimal conditions and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS

Application Methods: Flow Cytometry

Background: Isotype control antibodies are used to estimate the nonspecific binding of target primary antibodies due to Fc receptor binding or other protein-protein interactions. An isotype control antibody should have the same immunoglobulin type and be used at the same concentration as the test antibody.

$169
100 µg
This Cell Signaling Technology antibody is conjugated to APC-Cy7® under optimal conditions and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS

Application Methods: Flow Cytometry

Background: Isotype control antibodies are used to estimate the nonspecific binding of target primary antibodies due to Fc receptor binding or other protein-protein interactions. An isotype control antibody should have the same immunoglobulin type and be used at the same concentration as the test antibody.

$119
100 µg
This Cell Signaling Technology antibody is conjugated to FITC under optimal conditions and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS

Application Methods: Flow Cytometry

Background: Isotype control antibodies are used to estimate the nonspecific binding of target primary antibodies due to Fc receptor binding or other protein-protein interactions. An isotype control antibody should have the same immunoglobulin type and be used at the same concentration as the test antibody.

$129
100 µg
This Cell Signaling Technology antibody is conjugated to PE under optimal conditions and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS

Application Methods: Flow Cytometry

Background: Isotype control antibodies are used to estimate the nonspecific binding of target primary antibodies due to Fc receptor binding or other protein-protein interactions. An isotype control antibody should have the same immunoglobulin type and be used at the same concentration as the test antibody.

$189
100 µg
This Cell Signaling Technology antibody is conjugated to PE-Cy5® under optimal conditions and tested in-house for direct flow cytometric analysis in human cells.
APPLICATIONS

Application Methods: Flow Cytometry

Background: Isotype control antibodies are used to estimate the nonspecific binding of target primary antibodies due to Fc receptor binding or other protein-protein interactions. An isotype control antibody should have the same immunoglobulin type and be used at the same concentration as the test antibody.

$169
100 µg
This Cell Signaling Technology antibody is conjugated to PE-Cy7® under optimal conditions and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS

Application Methods: Flow Cytometry

Background: Control antibodies are used to estimate the non-specific binding of target primary antibodies due to Fc receptor binding or other protein-protein interactions.

$199
100 µg
This Cell Signaling Technology antibody is conjugated to PerCP-Cy5.5® under optimal conditions and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS

Application Methods: Flow Cytometry

Background: Isotype control antibodies are used to estimate the nonspecific binding of target primary antibodies due to Fc receptor binding or other protein-protein interactions. An isotype control antibody should have the same immunoglobulin type and be used at the same concentration as the test antibody.

$159
100 µg
This Cell Signaling Technology antibody is conjugated to redFluor™ 710 under optimal conditions and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS

Application Methods: Flow Cytometry

Background: Isotype control antibodies are used to estimate the nonspecific binding of target primary antibodies due to Fc receptor binding or other protein-protein interactions. An isotype control antibody should have the same immunoglobulin type and be used at the same concentration as the test antibody.

$159
100 µg
This Cell Signaling Technology antibody is conjugated to violetFluor™ 450 under optimal conditions and tested in-house for direct flow cytometric analysis in mouse cells.
APPLICATIONS

Application Methods: Flow Cytometry

Background: Isotype control antibodies are used to estimate the nonspecific binding of target primary antibodies due to Fc receptor binding or other protein-protein interactions. An isotype control antibody should have the same immunoglobulin type and be used at the same concentration as the test antibody.

$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. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Rb (4H1) Mouse mAb #9309.
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Pig

Application Methods: Flow Cytometry

Background: The retinoblastoma tumor suppressor protein Rb regulates cell proliferation by controlling progression through the restriction point within the G1-phase of the cell cycle (1). Rb has three functionally distinct binding domains and interacts with critical regulatory proteins including the E2F family of transcription factors, c-Abl tyrosine kinase, and proteins with a conserved LXCXE motif (2-4). Cell cycle-dependent phosphorylation by a CDK inhibits Rb target binding and allows cell cycle progression (5). Rb inactivation and subsequent cell cycle progression likely requires an initial phosphorylation by cyclin D-CDK4/6 followed by cyclin E-CDK2 phosphorylation (6). Specificity of different CDK/cyclin complexes has been observed in vitro (6-8) and cyclin D1 is required for Ser780 phosphorylation in vivo (9).

$111
20 µl
$260
100 µl
$630
300 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey, Pig

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

Background: The retinoblastoma tumor suppressor protein Rb regulates cell proliferation by controlling progression through the restriction point within the G1-phase of the cell cycle (1). Rb has three functionally distinct binding domains and interacts with critical regulatory proteins including the E2F family of transcription factors, c-Abl tyrosine kinase, and proteins with a conserved LXCXE motif (2-4). Cell cycle-dependent phosphorylation by a CDK inhibits Rb target binding and allows cell cycle progression (5). Rb inactivation and subsequent cell cycle progression likely requires an initial phosphorylation by cyclin D-CDK4/6 followed by cyclin E-CDK2 phosphorylation (6). Specificity of different CDK/cyclin complexes has been observed in vitro (6-8) and cyclin D1 is required for Ser780 phosphorylation in vivo (9).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The retinoblastoma tumor suppressor protein Rb regulates cell proliferation by controlling progression through the restriction point within the G1-phase of the cell cycle (1). Rb has three functionally distinct binding domains and interacts with critical regulatory proteins including the E2F family of transcription factors, c-Abl tyrosine kinase, and proteins with a conserved LXCXE motif (2-4). Cell cycle-dependent phosphorylation by a CDK inhibits Rb target binding and allows cell cycle progression (5). Rb inactivation and subsequent cell cycle progression likely requires an initial phosphorylation by cyclin D-CDK4/6 followed by cyclin E-CDK2 phosphorylation (6). Specificity of different CDK/cyclin complexes has been observed in vitro (6-8) and cyclin D1 is required for Ser780 phosphorylation in vivo (9).

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

Application Methods: Western Blotting

Background: Retinoblastoma-associated proteins 46 and 48 (RBAP46 and RBAP48; also known as RBBP7 and RBBP4) were first characterized in human cells as proteins that bind to the retinoblastoma (Rb) tumor suppressor protein (1). Since then, these proteins have been shown to be components of many protein complexes involved in chromatin regulation, including the chromatin assembly factor 1 (CAF-1) complex and type B histone acetyltransferase complex HAT1, both of which function in chromatin assembly during DNA replication (2,3). RBAP46 and RBAP48 are also found in the nucleosome remodeling factor complex NURF, the nucleosome remodeling and histone de-acetylation complex NuRD, and the Sin3/HDAC histone de-acetylation complex (4-7). More recently, RBAP46 and RBAP48 were identified as components of the polycomb repressor complex PRC2, which also contains EED and Ezh2 (8). RBAP46 and RBAP48 bind to the histone fold region of histone H4 and are believed to target these chromatin remodeling, histone acetylation, and histone de-acetylation complexes to their histone substrates (3).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The Set1 histone methyltransferase protein was first identified in yeast as part of the Set1/COMPASS histone methyltransferase complex, which methylates histone H3 at Lys4 and functions as a transcriptional co-activator (1). While yeast contain only one known Set1 protein, six Set1-related proteins exist in mammals: SET1A, SET1B, MLL1, MLL2, MLL3, and MLL4, all of which assemble into COMPASS-like complexes and methylate histone H3 at Lys4 (2,3). These Set1-related proteins are each found in distinct protein complexes, all of which share the common subunits WDR5, RBBP5, ASH2L, CXXC1 and DPY30. These subunits are required for proper complex assembly and modulation of histone methyltransferase activity (2-6). MLL1 and MLL2 complexes contain the additional protein subunit, menin (6). Like yeast Set1, all six Set1-related mammalian proteins methylate histone H3 at Lys4 (2-6). MLL translocations are found in a large number of hematological malignancies, suggesting that Set1/COMPASS histone methyltransferase complexes play a critical role in leukemogenesis (6).

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

Application Methods: Western Blotting

Background: The Set1 histone methyltransferase protein was first identified in yeast as part of the Set1/COMPASS histone methyltransferase complex, which methylates histone H3 at Lys4 and functions as a transcriptional co-activator (1). While yeast contain only one known Set1 protein, six Set1-related proteins exist in mammals: SET1A, SET1B, MLL1, MLL2, MLL3, and MLL4, all of which assemble into COMPASS-like complexes and methylate histone H3 at Lys4 (2,3). These Set1-related proteins are each found in distinct protein complexes, all of which share the common subunits WDR5, RBBP5, ASH2L, CXXC1 and DPY30. These subunits are required for proper complex assembly and modulation of histone methyltransferase activity (2-6). MLL1 and MLL2 complexes contain the additional protein subunit, menin (6). Like yeast Set1, all six Set1-related mammalian proteins methylate histone H3 at Lys4 (2-6). MLL translocations are found in a large number of hematological malignancies, suggesting that Set1/COMPASS histone methyltransferase complexes play a critical role in leukemogenesis (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The retinoblastoma (Rb) tumor suppressor family includes the retinoblastoma protein Rb (p105), retinoblastoma-like protein 1 (RBL1, p107), and retinoblastoma-like protein 2 (RBL2, p130). These Rb family proteins are referred to as "pocket proteins" because they contain a conserved binding pocket region that interacts with critical regulatory proteins, including E2F family transcription factors, c-Abl tyrosine kinase, and proteins containing a conserved LXCXE motif (1,2). In quiescent G0 phase cells, active Rb proteins hypophosphorylate and bind to E2F transcription factors to repress transcription and inhibit cell cycle progression (1,2). Upon growth factor induction of quiescent cells, Rb proteins become hyperphosphorylated and inactivated by G1-phase cyclinD-cdk4/6, G1/S-phase cyclin E-cdk2, and G1/S-phase cyclin A-cdk2 complexes (1,2). Hyperphosphorylation of Rb proteins results in a loss of E2F binding and allows for transcriptional activation and cell cycle progression (1,2). In addition to regulating the cell cycle, Rb proteins regulate chromosome stability, induction, and maintenance of senescence, apoptosis, cellular differentiation, and angiogenesis (3).Retinoblastoma-like protein 1 (RBL1, p107) interacts with E2F4 and E2F5 to recruit the DP, RB-like, E2F, and MuvB protein (DREAM) complex to E2F target genes to repress transcription of multiple genes required for progression into S phase and mitosis (4-6). Hypophosphorylation of RBL1 during cellular senescence is required for maintenance of senescent cells (7,8).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: The retinoblastoma (Rb) tumor suppressor family includes the retinoblastoma protein Rb (p105), retinoblastoma-like protein 1 (RBL1, p107), and retinoblastoma-like protein 2 (RBL2, p130). These Rb family proteins are referred to as ‘pocket proteins’ because they contain a conserved binding pocket region that interacts with critical regulatory proteins, including E2F family transcription factors, c-Abl tyrosine kinase, and proteins containing a conserved LXCXE motif (1,2). In quiescent G0 phase cells, active Rb proteins are hypophosphorylated and bind to E2F transcription factors to repress transcription and inhibit cell cycle progression (1,2). Upon growth factor induction of quiescent cells, Rb proteins become hyperphosphorylated and inactivated by G1-phase cyclinD-cdk4/6, G1/S-phase cyclin E-cdk2, and G1/S-phase cyclin A-cdk2 complexes (1,2). Hyperphosphorylation of Rb proteins results in a loss of E2F binding and allows for transcriptional activation and cell cycle progression (1,2). In addition to regulating the cell cycle, Rb proteins regulate chromosome stability, induction, and maintenance of senescence, apoptosis, cellular differentiation, and angiogenesis (3).Retinoblastoma-like protein 2 (RBL2, p130) is the most predominant and active Rb family member found in quiescent cells. In these cells, RBL2 interacts with E2F4 and E2F5 to recruit the DP, RB-like, E2F, and MuvB protein (DREAM) complex to E2F target genes to repress transcription of multiple genes required for progression into S phase and mitosis (4-6). Hypophosphorylation of RBL2 during cellular senescence is required for maintenance of senescent cells (7,8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The X-linked RNA binding motif protein (RBMX, hnRNP G) is a multi-functional protein that is part of a heterogeneous nuclear ribonucleoprotein complex (1,2). This widely expressed protein is involved in the control of pre-mRNA splicing as part of the spliceosome. RBMX is important for the alternative splicing of many pre-mRNAs, including those that encode for dystrophin, tropomyosin, and survival motor neuron protein (SMN) in skeletal muscle and cardiac muscle (3,4). The RBMX protein is essential for the maintenance of proper sister chromatid cohesion prior to sister chromosome segregation during mitosis (5). Research studies show that RBMX accumulates at sites of DNA damage and that the presence of RBMX is required for homologous recombination repair (6).

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

Application Methods: Chromatin IP, Immunohistochemistry (Paraffin), Western Blotting

Background: RBPSUH (Recombining Binding Protein, SUppressor of Hairless), also termed RBP-J or CSL, is the DNA-binding component of the transcription complex regulated by canonical Notch signaling. In the absence of Notch activation, RBPSUH suppresses target gene expression through interactions with a co-repressor complex containing histone deacetylase. Upon activation of Notch receptors, the Notch intracellular domain (NICD) translocates to the nucleus and binds to RBPSUH. This displaces the co-repressor complex and replaces it with a transcription activation complex that includes Mastermind-like (MAML) proteins and histone acetylase p300, leading to transcriptional activation of Notch target genes (1-3). RBPSUH is also the DNA-binding partner for Epstein-Barr virus (EBV) nuclear antigen 2 (EBNA2), a protein critical for latent viral transcription and immortalization of EBV-infected B cells (4,5).

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

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

Background: RING-box protein 1 (RBX1 or ROC1) is an essential component of two distinct but structurally related E3 ubiquitin ligase complexes, the SCF complex and the CBC (VHL) complex (1). RBX1 mediates the neddylation of CUL1, which activates SCF E3 ligase by facilitating the ubiquitin transfer from E2 to substrates (2-4). The RING finger domain of RBX1 is required for ubiquitin ligation (5). Two evolutionarily conserved mammalian RBX family members, RBX1/ROC1 and RBX2/ROC2/SAG, have been identified (5). RBX1 is constitutively expressed and binds to CUL2/VHL, while stress-inducible RBX2 binds to CUL5/SOCS (6).

$348
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 RCAS1 (D2B6N) XP® Rabbit mAb #12290.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Receptor binding cancer antigen expressed on SiSo cells (RCAS1) is also known as estrogen receptor-binding fragment-associated gene 9 (EBAG9). Originally identified as an estrogen-inducible gene (1), RCAS1 was recently found to play a novel role in the adaptive immune response by negatively regulating the cytolytic activity of cytotoxic T lymphocytes (CTLs) (2). RCAS1 is conserved in phylogeny and is ubiquitously expressed in most human tissues and cells (3,4). There is evidence that tissue expression of RCAS1 is increased in a variety of malignancies, including cancers of the gastrointestinal tract, liver, lung, breast, ovary, endometrium, and cervix. Research studies have shown that levels of RCAS1 tissue expression are negatively correlated with the prognosis of patients harboring the aforementioned malignancies (4). It is also noteworthy that research studies have detected elevated levels of RCAS1 in the sera of cancer patients (4). Initial studies indicated that RCAS1 was secreted from cancer cells and functioned as a ligand for a putative receptor expressed on NK cells, as well as T and B lymphocytes, inducing their apoptosis, which enabled cancer cells to evade immune surveillance (5,6). Subsequent studies have identified RCAS1 as a type III transmembrane Golgi protein with the ability to regulate vesicle formation, secretion, and protein glycosylation (2,7-9). Indeed, it has been shown that RCAS1 overexpression negatively regulates the cytolytic function of CTLs by negatively regulating protein trafficking from the trans-Golgi to secretory lysosomes (2). Furthermore, RCAS1 overexpression delays vesicle transport from the ER to Golgi and causes components of the ER quality control and glycosylation machinery to mislocalize. As a consequence, RCAS1 induces the deposition of tumor-associated glycan antigens on the cell surface, which are thought to contribute to tumor pathogenesis through the mediation of adhesion, invasion, and metastasis (8,9).