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Product listing: CD11c (D1V9Y) Rabbit mAb, UniProt ID Q9QXH4 #97585 to RIF1 (D2F2M) Rabbit mAb, UniProt ID Q5UIP0 #95558

$269
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: IHC-Leica® Bond™, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: CD11c (integrin αX, ITGAX) is a transmembrane glycoprotein that forms an α/β heterodimer with CD18 (integrin β2), which interacts with a variety of extracellular matrix molecules and cell surface proteins (1). CD11c is primarily used as a dendritic cell marker. Dendritic cells can be classified into two major types: CD11c+ conventional dendritic cells that specialize in antigen presentation, and CD11c- plasmacytoid dendritic cells that specialize in type I interferon production (2, 3). CD11c expression has also been observed on activated NK cells, subsets of B cells, monocytes, granulocytes, and some B cell malignancies including hairy cell leukemia (4-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: ABHD6 (α/β-Hydrolase domain-containing 6) is a monoacylglycerol lipase, ubiquitously expressed with the highest expression in brown adipose tissue, small intestine, and brain (1). A high-fat diet upregulates ABHD6 mRNA expression in small intestine and liver, and ABHD6 knockdown protects against high-fat diet-induced obesity, hepatic steatosis, and systemic insulin resistance (2). In addition, it has been shown that ABHD6 is a negative modulator of glucose-stimulated insulin secretion (3). In the central nervous system, ABHD6 is expressed postsynptically and degrades the endocannabinoid 2-arachidonoylglycerol (2-AG), an endogenous activator of cannabinoid receptors (4,5). Inhibitors of α/β-hydrolase domain 6 (ABHD6) have been actively pursued as a promising approach to treat inflammation, metabolic disorders, and epilepsy (2,6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The Golgi-associated protein golgin A1 (GOLGA1, golgin-97) was first isolated as a Golgi complex autoantigen associated with the autoimmune disorder Sjogren's syndrome (1). The golgin-97 protein contains a carboxy-terminal GRIP domain and is a commonly used trans-Golgi network (TGN) marker. All four known mammalian GRIP domain-containing proteins (golgin-97, golgin-245, GCC88 and GCC185) are found in the TGN, share extensive alpha-helical structure, and form homodimers (2). While all four golgin proteins localize to the TGN, they exhibit different membrane-binding abilities and are found in distinct TGN regions (3). Golgin-97 and golgin-245 are targeted to the trans-Golgi network through an interaction between their GRIP domains and the Arl1 protein switch II region (4). Overexpression studies and siRNA assays with GRIP domain-containing proteins suggest that these proteins help to maintain trans-Golgi network integrity and function by controlling localization of TGN resident proteins (5). By using a Shiga toxin B fragment (STxB)-based in vitro transport assay and an E-cadherin transport model system, golgin-97 and its effector Arl1-GTP were shown to play a role in trans-Golgi endosomal trafficking (6,7). Research studies also suggest that golgin-97 may play a role in poxvirus morphogenesis and maturation (8,9).

$285
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to violetFluor™ 450 and tested in-house for direct flow cytometry analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: CD11c (integrin αX, ITGAX) is a transmembrane glycoprotein that forms an α/β heterodimer with CD18 (integrin β2), which interacts with a variety of extracellular matrix molecules and cell surface proteins (1). CD11c is primarily used as a dendritic cell marker. Dendritic cells can be classified into two major types: CD11c+ conventional dendritic cells that specialize in antigen presentation, and CD11c- plasmacytoid dendritic cells that specialize in type I interferon production (2, 3). CD11c expression has also been observed on activated NK cells, subsets of B cells, monocytes, granulocytes, and some B cell malignancies including hairy cell leukemia (4-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry, Western Blotting

Background: The type I interferon (IFN) family includes IFN-β1 and IFN-α1 through IFN-α13 in humans and IFN-α1 through IFN-α14 in mice. Type I IFN is produced following detection of pathogen-associated molecular patterns (PAMPs) and is important for induction of antiviral genes, activation of dendritic cells, and initiation of adaptive immunity (1, 2). Type I IFNs signal through the IFN alpha receptor (IFNAR), which is a heterodimer composed of IFNAR1 and IFNAR2. Activation of IFNAR leads to formation of the nuclear complex IFN-stimulated gene factor 3 (ISGF3), which consists of STAT1, STAT2, and IRF-9 (3, 4). ISGF3 binds to IFN-stimulated response elements (ISREs) to initiate transcription of interferon-stimulated genes (3).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Western Blotting

Background: Tissue Factor (TF)/CD142 (Coagulation factor III/Thromboplastin) is a type-I transmembrane glycoprotein that serves as the cell surface receptor and cofactor for blood coagulation factors VII and VIIa, and thus plays a central role in hemostasis and thrombosis (1). The TF:VIIa receptor-ligand complex is widely recognized as the initiator of the extrinsic blood coagulation protease cascade, which ultimately leads to the generation of fibrin and thrombin (1). A member of the type-II cytokine receptor superfamily, TF has also been shown to engage the PI3K (2) and MAPK (3) signaling cascades upon binding to factor VIIa in order to drive cellular responses such as cell migration, growth, and proliferation. Although the function of TF under physiologic conditions is to coordinate blood clotting in response to tissue damage, TF is implicated in pathologic conditions such as tumorigenesis. Indeed, TF is aberrantly expressed in colorectal cancer, breast cancer, pancreatic cancer, and glioblastoma multiforme (4). It has been shown to promote tumor angiogenesis, tumor growth, metastasis, and venous thrombosis (5). Given that TF overexpression is associated with numerous types of solid tumors, it has garnered much attention as a potential therapeutic target.

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

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

Background: ETS-related gene (ERG) is a member of the E-26 transformation-specific (ETS) family of sequence-specific DNA-binding transcription factors (1). ERG plays important and highly conserved roles in vertebrate development. Early in embryonic development, ERG is highly expressed in the embryonic mesoderm and endothelium, where it plays a critical role in the formation of the vascular system, urogenital tract and bone development (2,3). Later in embryonic development, ERG functions to regulate the pluripotency of hematopoietic stem cells, endothelial cell homeostasis and angiogenesis (2,4-7). ERG expression is not restricted to development. In adult mouse, ERG is normally expressed in endothelial tissues, including adrenal, cartilage, heart, spleen, lymphatic endothelial and eosinophil cells (8). However, deregulation of ERG activity, often resulting from chromosomal rearrangements, has been implicated and linked to poor prognosis in a number of different cancers. Chromosomal translocations generating EWS/ERG chimeric proteins comprised of the amino-terminal transactivation domain of Ewing’s sarcoma breakpoint region 1 (EWS) and the carboxy-terminal ETS domain of ERG have been identified in 5-10% of Ewing’s sarcoma, an aggressive bone and soft tissue tumor (9). Chromosomal translocations between ERG and TLS/FUS or ERG and ELF4 have been implicated in acute myeloid leukemia (10, 11). Over-expression of ERG, resulting from gene fusion with the androgen-driven promoter of the TMPRSS2 gene, has been identified as a key driver of metastasis and marker for poor prognosis in prostate cancer (12).

$106
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

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

$131
200 µl
This Cell Signaling Technology antibody is conjugated to FITC 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.

$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 HEXIM1 (D5Y5K) Rabbit mAb #12604.
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry

Background: Hexamethylene bis-acetamide-inducible protein 1 (HEXIM1) was originally identified in vascular smooth muscle cells as a protein that is upregulated upon treatment with the differentiating agent hexamethylene bisacetamide (1). HEXIM1 binds 7SK RNA, a highly abundant non-coding RNA, and together they act as a potent inhibitor of positive transcription elongation factor b (P-TEFb) (2,3). P-TEFb phosphorylates the C-terminal domain of the largest subunit of RNA polymerase II and is an important regulator of transcription elongation (4-8). 7SK RNA-bound HEXIM1 interacts with the cyclin T1 subunit of P-TEFb, sequestering P-TEFb in an inactive form leading to transcription inhibition (2,3). The regulation of the relative ratio of inactive to active P-TEFb in the cell by HEXIM1/7SK RNA is thought to play a critical role in regulation of a wide range of cellular gene expression programs such as estrogen and glucocorticoid receptor regulated genes (9-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Uncoupling protein 3 (UCP3), a mitochondrial inner membrane transport protein, is highly expressed in skeletal muscle and activates glucose transport in muscle cells (2). UCP3 lowers the production of reactive oxygen species in mitochondria by reducing the mitochondrial inner membrane potential (3). UCP3 has been implicated in the protection against fat-induced insulin resistance in skeletal muscle (4) and fat gain induced by high-fat feeding (1).

$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 cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Smac/Diablo (D5S3R) Rabbit mAb #15108.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Smac/Diablo is a 21 kDa mammalian mitochondrial protein that functions as a regulatory component during apoptosis (1,2). Upon mitochondrial stress, Smac/Diablo is released from mitochondria and competes with caspases for binding of IAPs (inhibitor of apoptosis proteins) (1,2). The interaction of Smac/Diablo with IAPs relieves the inhibitory effect of the IAPs on caspases (3,4). This interaction involves mainly the amino-terminal residues of Smac/Diablo with the BIR3 region of XIAP, supplemented with several other hydrophobic interactions between the helical structures of Smac/Diablo and other areas of BIR3 (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: The transcription factor proline, glutamic acid, and leucine rich protein 1 (PELP1, MNAR) mediates cell signaling through direct interaction with hormone nuclear receptors to regulate target gene transcription. This versatile protein also regulates gene expression by participating in chromatin remodeling, and acts as a cytoplasmic scaffold protein to mediate growth factor and hormone signaling (1). Following its original description as an estrogen receptor α (ERα) coactivator (2), additional research showed that PELP1 corepresses multiple nuclear hormone receptors and transcriptional regulators, including progesterone receptor, glucocorticoid receptor, AP1, and Stat3 (3). PELP1 also acts cooperatively with the secondary coactivator CARM1 at ERα target gene promoters to increase ERα-mediated transactivation (4). The PELP1 protein contains several leucine-rich repeats, important for interaction with nuclear receptors, and a carboxy-terminal glutamic acid-rich domain responsible for histone protein interaction (2). The glutamic acid-rich region of PELP1 binds to hypoacetylated histones H3 and H4 to block interaction between histone proteins and acetyltransferases. This interaction maintains histones in a hypoacetylated state and suppresses serum-response gene activation. Interaction between PELP1 and ERα relieves this repression and promotes acetylation of histone proteins (3).Research studies demonstrate altered regulation of PELP1 in several distinct hormone-dependent cancers, such as ovarian, breast, and prostate cancers (5-7). As a result, PELP1 may be a promising prognostic marker for hormone-dependent cancers, and inhibiting PELP1 expression or activity may prove beneficial in disrupting hormonal cancer initiation, progression, and metastasis (8).

$348
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated UCHL1 (D3T2E) XP® Rabbit mAb #13179.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Protein ubiquitination and deubiquitination are reversible processes catalyzed by ubiquitinating enzymes (UBEs) and deubiquitinating enzymes (DUBs) (1,2). DUBs are categorized into 5 subfamilies: USP, UCH, OTU, MJD, and JAMM. UCHL1, UCHL3, UCHL5/UCH37, and BRCA-1-associated protein-1 (BAP1) belong to the ubiquitin carboxy-terminal hydrolase (UCH) family of DUBs, which all possess a conserved catalytic UCH domain of about 230 amino acids. UCHL5 and BAP1 have unique, extended carboxy-terminal tails. UCHL1 is abundantly expressed in neuronal tissues and testes, while UCHL3 expression is more widely distributed (3,4). Although UCHL1 and UCHL3 are the most closely related UCH family members with about 53% identity, their biochemical properties differ in that UCHL1 binds monoubiquitin and UCHL3 shows dual specificity toward both ubiquitin (Ub) and NEDD8, a Ub-like molecule.UCHL1 (PGP 9.5/PARK5) functions as a deubiquitinating enzyme and monoubiquitin stabilizer. In vitro studies have demonstrated that UCHL1 can hydrolyze isopeptide bonds between the carboxy-terminal glycine of Ub and the ε-amino group of lysine on target proteins. UCHL1 is also involved in the cotranslational processing of pro-ubiquitin and ribosomal proteins translated as ubiquitin fusions (5-7). Mice deficient in UCHL1 experience spasticity, suggesting that UCHL1 activity is required for the normal neuromuscular junction structure and function (5-7). Research studies have described loss of UCHL1 expression in numerous human malignancies, such as prostate, colorectal, renal, and breast carcinomas. Investigators have shown that loss of UCHL1 expression in breast carcinomas can be attributed to hyper-methylation of the UCHL1 gene promoter (8). While loss of UCHL1 expression is implicated in human carcinogenesis, mutation of UCHL1 has been implicated in neurodegenerative diseases such as Parkinson's and Alzheimer's (6,7).

$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 Ezh2 (D2C9) XP® Rabbit mAb #5246.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The polycomb group (PcG) proteins are involved in maintaining the silenced state of several developmentally regulated genes and contribute to the maintenance of cell identity, cell cycle regulation, and oncogenesis (1,2). Enhancer of zeste homolog 2 (Ezh2), a member of this large protein family, contains four conserved regions including domain I, domain II, and a cysteine-rich amino acid stretch that precedes the carboxy-terminal SET domain (3). The SET domain has been linked with histone methyltransferase (HMTase) activity. Moreover, mammalian Ezh2 is a member of a histone deacetylase complex that functions in gene silencing, acting at the level of chromatin structure (4). Ezh2 complexes methylate histone H3 at Lys9 and 27 in vitro, which is thought to be involved in targeting transcriptional regulators to specific loci (5). Ezh2 is deregulated in various tumor types, and its role, both as a primary effector and as a mediator of tumorigenesis, has become a subject of increased interest (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

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 is also associated with a number of physiological processes including development, differentiation, neurodegeneration, infection and cancer (3). The molecular machinery of autophagy was largely discovered in yeast and is directed by a number of autophagy-related (Atg) genes. These proteins are involved in the formation of autophagosomes, cytoplasmic vacuoles that are delivered to lysosomes for degradation. The class III type phosphoinositide 3-kinase (PI3K) Vps34 regulates vacuolar trafficking and autophagy (4,5). Multiple proteins associate with Vsp34, including p105/Vsp15, Beclin-1, UVRAG, Atg14, and Rubicon, to determine Vsp34 function (6-12). Atg14 and Rubicon were identified based on their ability to bind to Beclin-1 and participate in unique complexes with opposing functions (9-12). Rubicon, which localizes to the endosome and lysosome, inhibits Vps34 lipid kinase activity; knockdown of Rubicon enhances autophagy and endocytic trafficking (11,12). In contrast, Atg14 localizes to autophagosomes, isolation membranes and ER, and can enhance Vps34 activity. Knockdown of Atg14 inhibits starvation-induced autophagy (11,12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: There are three members of the steroid receptor co-activator (SRC) family of proteins: SRC-1 (NCoA-1), SRC-2 (TIF2/GRIP1/NCoA-2), and SRC-3 (ACTR/pCIP/RAC3/TRAM-1/AIB1). All SRC family members share significant structural homology and function to stimulate transcription mediated by nuclear hormone receptors and other transcriptional activators such as Stat3, NF-κB, E2F1, and p53 (1-4). Two SRC proteins, SRC-1 and SRC-3, function as histone acetyltransferases (5,6). In addition, all three family members can recruit other histone acetyltransferases (CBP/p300, PCAF) and histone methyltransferases (PRMT1, CARM1) to target promoters and cooperate to enhance expression of many genes (5-8). The SRC proteins play important roles in multiple physiological processes including cell proliferation, cell survival, somatic cell growth, mammary gland development, female reproductive function, and vasoprotection (9). SRC-1 and SRC-3 are conduits for kinase-mediated growth factor signaling to the estrogen receptor and other transcriptional activators. Seven SRC-1 phosphorylation sites and six SRC-3 phosphorylation sites have been identified, which are induced by steroids, cytokines, and growth factors and involve multiple kinase signaling pathways (9-11). Research has shown that all three SRC family members are associated with increased activity of nuclear receptors in breast, prostate, and ovarian carcinomas. According to the literature, SRC-3 is frequently amplified or overexpressed in a number of cancers (12), and SRC-1/PAX3 and SRC-2/MYST3 translocations are found associated with rhabdomyosarcoma and acute myeloid leukemia, respectively (13,14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Gasdermin D (GSDMD), a member of the gasdermin family that includes GSDMA, GSDMB, and GSMDC, has been reported to have a critical role as a downstream effector of pyroptosis (1,2). Pyroptosis is a lytic type of cell death triggered by inflammasomes, multiprotein complexes assembled in response to pathogen-associated molecular patterns (PAMPs) or danger-associated molecular patterns (DAMPs) that result in the activation of caspase-1 and subsequent cleavage of pro-inflammatory cytokines IL-1β and IL-18 (3). Gasdermin D was identified by two independent groups as a substrate of inflammatory caspases, caspase-1 and caspase-11/4/5, producing two fragments: GSDMD-N and GSDMD-C. Cleavage results in release of an intramolecular inhibitory interaction between the N- and C-terminal domains, allowing the N-terminal fragment GSMDM-N to initiate pyroptosis through the formation of pores on the plasma membrane (4-7).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry, IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: FcγRIIB (CD32B) is a low affinity, IgG Fc-binding receptor expressed on B cells, monocytes, macrophages, and dendritic cells (DCs) (1-3). It is the inhibitory Fc receptor and signals through an immunoreceptor tyrosine-based inhibitory motif (ITIM) within its carboxy-terminal cytoplasmic tail (2). Binding of immune complexes to FcγRIIB results in tyrosine phosphorylation of the ITIM motif at Tyr292 and recruitment of the phosphatase SHIP, which mediates inhibitory effects on immune cell activation (2,4). In this way, FcγRIIB suppresses the effects of activating Fc-binding receptors (3). For example, mice deficient for FcγRIIB have greater T cell and DC responses following injection of immune complexes (5, 6). In addition, FcγRIIB plays a role in B cell affinity maturation (7). Signaling through FcγRIIB in the absence of signaling through the B cell receptor (BCR) is proapoptotic, while signaling through FcγRIIB and the BCR simultaneously attenuates the apoptotic signal and results in selection of B cells with higher antigen affinity (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Methyltransferase-like protein 3 (METTL3) and methytransferase-like protein 14 (METTL14) are the two catalytic subunits of an N6-methyltransferase complex that methylates adenosine residues in RNA (1). Methylation of adenosine residues regulates mRNA splicing, processing, translation efficiency, editing and stability, in addition to regulating primary miRNA processing, and is critical for proper regulation of the circadian clock, embryonic stem cell self-renewal, immune tolerance, response to various stimuli, meiosis and mouse fertility (2,3). In this complex, METTL3 functions as the catalytic methyltransferase subunit and METTL14 functions as the target recognition subunit by binding to RNA (4). In addition, the Wilms tumor 1-associated protein (WTAP) functions as a regulatory subunit and is required for accumulation of the complex to nuclear speckles, which are sites of RNA processing (5). Several studies suggest a role for this complex in cancer. METTL3 expression is elevated in lung adenocarcinoma where it promotes growth, survival and invasion of human lung cancer cells (6). In addition, WTAP is over-expressed in a number of different cancers and positively regulates cell migration and invasion in glioblastoma and cholangiocarcinoma (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Western Blotting

Background: Tripartite motif containing protein 37 (TRIM37, also known as MUL1) is a member of the tripartite motif (TRIM) family whose members contain a RING domain, a B-box, and a coiled-coil region (together called RBCC). TRIM37 was initially described as the defining truncation mutation in mulibrey nanism (1). An E3 ubiquitin ligase, TRIM37 is responsible for the monoubiquitination of histone H2A at Lys119, and is amplified in over 40% of breast cancers (2,3). TRIM37 interacts with polycomb group proteins EZH2 and SUZ12, and contributes to histone H3K27 lysine tri-methylation and subsequent silencing of tumor suppressor genes (3). Oncogenic activity of TRIM37 has also been reported in pancreatic, hepatic, and colorectal cancers (4-7).

$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 cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Acetyl-Histone H2AZ (Lys4/Lys7) Rabbit mAb #75336.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Modulation of chromatin structure plays a critical role in the regulation of transcription in eukaryotes. The nucleosome, made up of four core histone proteins (H2A, H2B, H3 and H4), is the primary building block of chromatin. In addition to the growing number of post-translational histone modifications regulating chromatin structure, cells can also exchange canonical histones with variant histones that can directly or indirectly modulate chromatin structure (1). There are five major variants of histone H2A: canonical H2A (most abundant), H2A.X, MacroH2A, H2ABbd and H2A.Z (2). Histone H2A.Z, the most conserved variant across species, functions as both a positive and negative regulator of transcription and is important for chromosome stability (2). Several homologous protein complexes, such as SWR-C (S. cerevisiae), TIP60 (D. melanogaster) and SRCAP (mammals), have been shown to catalyze the ATP-dependent exchange of H2A.Z for H2A in the nucleosome (3,4,5). This exchange of histone H2A variants changes histone-histone interactions in the nucleosome core and alters an acidic patch on the surface of the nucleosome, resulting in changes in nucleosome stability and binding of non-histone proteins such as HP1α (6,7).

$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 Na,K-ATPase α1 (D4Y7E) Rabbit mAb #23565.
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Na,K-ATPase is an integral membrane heterodimer belonging to the P-type ATPase family. This ion channel uses the energy derived from ATP hydrolysis to maintain membrane potential by driving sodium export and potassium import across the plasma membrane against their electrochemical gradients. It is composed of a catalytic α subunit and a β subunit (reviewed in 1). Several phosphorylation sites have been identified for the α1 subunit. Tyr10 is phosphorylated by an as yet undetermined kinase (2), Ser16 and Ser23 are phosphorylated by PKC, and Ser943 is phosphorylated by PKA (3-5). All of these sites have been implicated in the regulation of enzyme activity in response to hormones and neurotransmitters, altering trafficking and kinetic properties of Na,K-ATPase. Altered phosphorylation in response to angiotensin II stimulates activity in the rat proximal tubule (6). Na,K-ATPase is also involved in other signal transduction pathways. Insulin regulates its localization in differentiated primary human skeletal muscle cells, and this regulation is dependent on ERK1/2 phosphorylation of the α subunit (7). Na,K-ATPase and Src form a signaling receptor complex that affects regulation of Src kinase activity and, subsequently, its downstream effectors (8,9).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: IHC-Leica® Bond™, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: The B cell antigen receptor (BCR) is composed of membrane immunoglobulin molecules non-covalently associated with the heterodimeric signaling component, CD79A and CD79B (also known as Igα and Igβ, respectively) (1,2). The presence of this receptor complex is essential for B cell development and function (3). Following antigen binding, CD79A/CD79B heterodimers are phosphorylated and initiate intracellular signaling through Src family kinases, Lyn, Blk, and Fyn, as well as Syk and Btk tyrosine kinases (4,5). The complexity of BCR signaling results in a variety of distinct cellular functions, such as proliferation, tolerance, apoptosis, and differentiation (6). BCR-antigen ligation also leads to internalization of the complex, trafficking to late endosomes, and antigen presentation in major histocompatibility molecules on the B cell surface (7,8). CD79B enhances the phosphorylation of CD79A (9). Alternatively spliced transcript variants encoding different isoforms of CD79B have been identified (10). CD79B is widely expressed on B cell malignancies and may serve as a target for therapeutic intervention (11,12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Insulin receptor substrate 1 (IRS-1) is one of the major substrates of the insulin receptor kinase (1). IRS-1 contains multiple tyrosine phosphorylation motifs that serve as docking sites for SH2-domain containing proteins that mediate the metabolic and growth-promoting functions of insulin (2-4). IRS-1 also contains over 30 potential serine/threonine phosphorylation sites. Ser307 of IRS-1 is phosphorylated by JNK (5) and IKK (6) while Ser789 is phosphorylated by SIK-2, a member of the AMPK family (7). The PKC and mTOR pathways mediate phosphorylation of IRS-1 at Ser612 and Ser636/639, respectively (8,9). Phosphorylation of IRS-1 at Ser1101 is mediated by PKCθ and results in an inhibition of insulin signaling in the cell, suggesting a potential mechanism for insulin resistance in some models of obesity (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

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

Background: The receptor-interacting protein (RIP) family of serine-threonine kinases (RIP, RIP2, RIP3, and RIP4) are important regulators of cellular stress that trigger pro-survival and inflammatory responses through the activation of NF-κB, as well as pro-apoptotic pathways (1). In addition to the kinase domain, RIP contains a death domain responsible for interaction with the death domain receptor Fas and recruitment to TNF-R1 through interaction with TRADD (2,3). RIP-deficient cells show a failure in TNF-mediated NF-κB activation, making the cells more sensitive to apoptosis (4,5). RIP also interacts with TNF-receptor-associated factors (TRAFs) and can recruit IKKs to the TNF-R1 signaling complex via interaction with NEMO, leading to IκB phosphorylation and degradation (6,7). Overexpression of RIP induces both NF-κB activation and apoptosis (2,3). Caspase-8-dependent cleavage of the RIP death domain can trigger the apoptotic activity of RIP (8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Sequestosome 1 (SQSTM1, p62) is a ubiquitin binding protein involved in cell signaling, oxidative stress, and autophagy (1-4). It was first identified as a protein that binds to the SH2 domain of p56Lck (5) and independently found to interact with PKCζ (6,7). SQSTM1 was subsequently found to interact with ubiquitin, providing a scaffold for several signaling proteins and triggering degradation of proteins through the proteasome or lysosome (8). Interaction between SQSTM1 and TRAF6 leads to the K63-linked polyubiquitination of TRAF6 and subsequent activation of the NF-κB pathway (9). Protein aggregates formed by SQSTM1 can be degraded by the autophagosome (4,10,11). SQSTM1 binds autophagosomal membrane protein LC3/Atg8, bringing SQSTM1-containing protein aggregates to the autophagosome (12). Lysosomal degradation of autophagosomes leads to a decrease in SQSTM1 levels during autophagy; conversely, autophagy inhibitors stabilize SQSTM1 levels. Studies have demonstrated a link between SQSTM1 and oxidative stress. SQSTM1 interacts with KEAP1, which is a cytoplasmic inhibitor of NRF2, a key transcription factor involved in cellular responses to oxidative stress (3). Thus, accumulation of SQSTM1 can lead to an increase in NRF2 activity.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TNFRSF8/CD30 is a type-I transmembrane glycoprotein that is a member of the TNFR superfamily. CD30 is synthesized as a precursor protein that undergoes extensive posttranslational modification before becoming embedded in the plasma membrane as a 120-kDa transmembrane protein (1,2). The expression of CD30 is upregulated in activated T-cells and may trigger costimulatory signaling pathways upon its engagement (3,4). While its expression is normally restricted to subsets of activated T-cells and B-cells, CD30 expression is robustly upregulated in hematologic malignancies, such as Hodgkin’s lymphoma (HL), anaplastic large cell lymphoma (ALCL), and adult T-cell leukemia, thus making it an attractive target for therapeutic intervention (5,6). Research studies have suggested that in certain disease contexts, CD30 recruits TRAF2 and TRAF5 adaptor proteins to drive NF-kappa B activation, aberrant cell growth, and cytokine production (7-9). CD30 signaling is also regulated by TACE-dependent proteolytic cleavage of its ectodomain, which results in reduced CD30L-dependent activation of CD30+ cells (10, 11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: The Rap1 interacting factor 1 (RIF1) was originally identified as a regulator of telomere homeostasis in yeast and mammalian cells (1). Research studies show that RIF1 regulates the timing of eukaryotic DNA replication origin firing through its affect on chromatin architecture (2-4). Additional studies show that RIF1 is essential for regulating the repair of DNA double strand breaks (DSBs). RIF1 is recruited to sites of DSBs by 53BP1 in response to DNA damage, and suppresses 5' end resection to favor the non-homologous end joining (NHEJ) pathway over homologous recombination (HR) repair (5-9). Oct4 and Smad3 modulate Rif1 expression in mouse embryonic stem cells; Rif1 may regulate embryonic stem cell stability during cell proliferation (10).