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Product listing: Integrin αV (D2N5H) Rabbit mAb, UniProt ID P06756 #60896 to Aiolos (D1C1E) Rabbit mAb (Alexa Fluor® 700 Conjugate), UniProt ID Q9UKT9 #59612

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

Application Methods: Western Blotting

Background: Integrins are α/β heterodimeric cell surface receptors that play a pivotal role in cell adhesion and migration, as well as in growth and survival (1,2). The integrin family contains at least 18 α and 8 β subunits that form 24 known integrins with distinct tissue distribution and overlaping ligand specificities (3). Integrins not only transmit signals to cells in response to the extracellular environment (outside-in signaling), but also sense intracellular cues to alter their interaction with the extracellular environment (inside-out signaling) (1,2).Several αV subfamily members, including αVβ3, αVβ5, αVβ1, are highly expressed in active endothelial cells and cancer cells (3-6) where they play a critical role in angiogenesis and tumor metastasis (7-9). Therefore, interest has focused on αV integrin as a key therapeutic target in the treatment of cancer (10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Importins belong to the karyopherin family of nuclear transport proteins (1) and are divided into two subgroups: importin α and importin β. Importins mainly function in nuclear protein import and export (2,3). Importin β1 (also known as karyopherin β1, Kpnβ1, Kpnb1, or p97) plays a key role in the nuclear import process (1-3). Nuclear import via importin β1 association with adaptor importin α (also known as karyopherin α, or Kpnα) is an essential component of the classical nuclear localization signal (NLS) pathway (4). Importin α directly recognizes the NLS present in the cargo target, prompting complex formation with importin β1. The cargo:importin α:importin β1 complex is transported across the nuclear pore complex (NPC) into the nucleus, where it is dissociated by the binding of RanGTP (1-4). Nuclear import directly via importin β1 can also occur by importin β1 recognition of the cargo protein, bypassing importin α involvement. In both cases, the importin β1/target protein interaction is mediated through the binding of importin β1 HEAT repeats with the target protein sequences (either the cargo protein itself or importin α) (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Tropomodulin-1 (TMOD1) belongs to a conserved family of cytoskeletal proteins (TMOD1-4) that play an important role in modulating actin cytoskeleton dynamics. TMOD proteins function as actin capping proteins, which stabilize actin filaments by inhibiting both elongation and depolymerization (1). While many proteins have been identified that cap the rapidly growing barbed end of actin filaments, TMODs are the only proteins thus far identified that cap the slowly growing pointed end (2). A research study in triple-negative breast cancer cells identified TMOD1 as a target of NF-κB signaling, and showed that increased TMOD1 expression was associated with enhanced tumor growth in a mouse xenograft model (3). Molecular expression of TMOD1 was also identified as part of a unique gene expression signature that could discriminate ALK-negative anaplastic large-cell lymphoma from other malignancy subtypes (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Nutrient-deprivation autophagy factor-1 (NAF-1) (also known as CISD2, CDGSH iron-sulfur domain-containing protein 2) is a member of NEET family of 2Fe-2S proteins, characterized by a unique CDGSH sequence at their Fe-S-cluster-binding domain (1). NAF-1/CISD2 is a multifunctional protein. In addition to its role in iron and ROS homeostasis, it has been shown to play a role in autophagy, neurodegenerative diseases, and aging (2-7). Enhanced expression of NAF-1/CISD2 is associated with many types of cancer. Silencing of NAF-1/CISD2 expression in cancer cells significantly inhibited proliferation and tumorigenicity; while overexpression of NAF-1/CISD2 significantly enhanced proliferation (2, 8, 9).

$263
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to PE and tested in-house for direct flow cytometry analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: CD19 is a 95 kDa coreceptor, which amplifies the signaling cascade in B cells (1). On the B cell surface, CD19 associates with CD21, CD81 and Leu-13 to exert its function. The cytoplasmic tail of CD19 has nine conserved tyrosine residues playing critical roles in CD19 mediated function by coupling signaling molecules to the receptor (1). After B cell receptor or CD19 ligation, Tyr531 and Tyr500 of CD19 are progressively phosphorylated. This phosphorylation enables the coupling of PI3 kinase and Src family tyrosine kinase to CD19 and activates the PI3K and Src signaling pathways (2,3). Coligation of B cell receptor and CD19 also promotes Tyr409 phosphorylation in CD19. The phosphorylation at these sites enables its binding to Vav and mediates elevated intracellular calcium response, as well as the JNK pathway (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: The coronin family of actin-binding proteins regulates a variety of cellular functions, including migration, phagocytosis, and cytokinesis. Coronin 1A is highly expressed in lymphocytes, and is required for appropriate immune regulation in mice and humans. Researchers are investigating coronin 1A as a potential therapeutic target for autoimmune diseases and lymphoid cancers (1,2). Coronin 1A affects bone resorption through its regulation of lysosome fusion and secretion of cathepsin K in osteoclasts (3). In the nervous system, coronin 1A has been shown to regulate GPCR signaling and neurite outgrowth (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: CD133, also known as Prominin, was first described as a cell surface marker recognized by monoclonal antibody AC133 on putative hematopoietic stem cells (1). Subsequent cDNA cloning indicated that CD133 is a five-transmembrane protein with a predicated molecular weight of 97 kDa. Due to heavy glycosylation, its apparent molecular weight is 130 kDa as determined by SDS-PAGE analysis (2). Besides blood stem cells, CD133 is expressed on and used to isolate other stem cells, including cancer stem cells (3-7). A deletion mutation in CD133 produces aberrant protein localization and may result in retinal degeneration in humans (8).

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

Application Methods: Western Blotting

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

$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 Sox2 (D9B8N) Rabbit mAb #23064.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: Embryonic stem cells (ESC) derived from the inner cell mass of the blastocyst are unique in their pluripotent capacity and potential for self-renewal (1). Research studies demonstrate that a set of transcription factors that includes Oct-4, Sox2, and Nanog forms a transcriptional network that maintains cells in a pluripotent state (2,3). Chromatin immunoprecipitation experiments show that Sox2 and Oct-4 bind to thousands of gene regulatory sites, many of which regulate cell pluripotency and early embryonic development (4,5). siRNA knockdown of either Sox2 or Oct-4 results in loss of pluripotency (6). Induced overexpression of Oct-4 and Sox2, along with additional transcription factors Klf4 and c-Myc, can reprogram both mouse and human somatic cells to a pluripotent state (7,8). Additional evidence demonstrates that Sox2 is also present in adult multipotent progenitors that give rise to some adult epithelial tissues, including several glands, the glandular stomach, testes, and cervix. Sox2 is thought to regulate target gene expression important for survival and regeneration of these tissues (9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Paired box (PAX) proteins are a family of transcription factors that play important and diverse roles in animal development (1). Nine PAX proteins (PAX1-9) have been described in humans and other mammals. They are defined by the presence of an amino-terminal "paired" domain, consisting of two helix-turn-helix motifs, with DNA binding activity (2). PAX proteins are classified into four structurally distinct subgroups (I-IV) based on the absence or presence of a carboxy-terminal homeodomain and a central octapeptide region. Subgroup I (PAX1 and 9) contains the octapeptide but lacks the homeodomain; subgroup II (PAX2, 5, and 8) contains the octapeptide and a truncated homeodomain; subgroup III (PAX3 and 7) contains the octapeptide and a complete homeodomain; and subgroup IV (PAX4 and 6) contains a complete homeodomain but lacks the octapeptide region (2). PAX proteins play critically important roles in development by regulating transcriptional networks responsible for embryonic patterning and organogenesis (3); a subset of PAX proteins also maintain functional importance during postnatal development (4). Research studies have implicated genetic mutations that result in aberrant expression of PAX genes in a number of cancer subtypes (1-3), with members of subgroups II and III identified as potential mediators of tumor progression (2).

$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 HER2/ErbB2 (29D8) Rabbit mAb #2165.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: The ErbB2 (HER2) proto-oncogene encodes a 185 kDa transmembrane, receptor-like glycoprotein with intrinsic tyrosine kinase activity (1). While ErbB2 lacks an identified ligand, ErbB2 kinase activity can be activated in the absence of a ligand when overexpressed and through heteromeric associations with other ErbB family members (2). Amplification of the ErbB2 gene and overexpression of its product are detected in almost 40% of human breast cancers (3). Binding of the c-Cbl ubiquitin ligase to ErbB2 at Tyr1112 leads to ErbB2 poly-ubiquitination and enhances degradation of this kinase (4). ErbB2 is a key therapeutic target in the treatment of breast cancer and other carcinomas and targeting the regulation of ErbB2 degradation by the c-Cbl-regulated proteolytic pathway is one potential therapeutic strategy. Phosphorylation of the kinase domain residue Tyr877 of ErbB2 (homologous to Tyr416 of pp60c-Src) may be involved in regulating ErbB2 biological activity. The major autophosphorylation sites in ErbB2 are Tyr1248 and Tyr1221/1222; phosphorylation of these sites couples ErbB2 to the Ras-Raf-MAP kinase signal transduction pathway (1,5).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in mouse cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Nanog (D2A3) XP® Rabbit mAb (Mouse Specific) #8822.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry

Background: Nanog is a homeodomain-containing transcription factor that is essential for the maintenance of pluripotency and self renewal in embryonic stem cells (1). Nanog expression is controlled by a network of factors including Sox2 and the key pluripotency regulator Oct-4 (1). Recent advances in somatic cell reprogramming have utilized viral expression of combinations of transcription factors including nanog, Oct-4, Sox2, KLF4, c-Myc, and LIN28 (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Dectin-1 is a C-type lectin receptor expressed by macrophages, monocytes, dendrtic cells, neutrophils, and a subset of γδ T cells (1,2). Dectin-1 is a glycoprotein with eight different isoforms, generated through alternative splicing (3-5). It plays an important role in anti-fungal immunity by acting as a pattern recognition receptor for β-glucans found on the cell wall of fungi and some bacteria (5,6). Dectin-1 is composed of a short amino-terminal cytoplasmic domain containing an ITAM-like motif, a transmembrane domain, and an extracellular carboxy-terminal C-type lectin domain (5). Dectin-1 recognizes β-glucans through its C-type lectin domain and transduces signals through its ITAM-like motif by recruiting and activating Syk (7,8). Dendritic cells activated through Dectin-1 promote differentiation of Th17 cells by producing IL-6 and IL-23 (9).

$305
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 B-Raf (D9T6S) Rabbit mAb #14814.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: A-Raf, B-Raf, and c-Raf (Raf-1) are the main effectors recruited by GTP-bound Ras to activate the MEK-MAP kinase pathway (1). Activation of c-Raf is the best understood and involves phosphorylation at multiple activating sites including Ser338, Tyr341, Thr491, Ser494, Ser497, and Ser499 (2). p21-activated protein kinase (PAK) has been shown to phosphorylate c-Raf at Ser338, and the Src family phosphorylates Tyr341 to induce c-Raf activity (3,4). Ser338 of c-Raf corresponds to similar sites in A-Raf (Ser299) and B-Raf (Ser445), although this site is constitutively phosphorylated in B-Raf (5). Inhibitory 14-3-3 binding sites on c-Raf (Ser259 and Ser621) can be phosphorylated by Akt and AMPK, respectively (6,7). While A-Raf, B-Raf, and c-Raf are similar in sequence and function, differential regulation has been observed (8). Of particular interest, B-Raf contains three consensus Akt phosphorylation sites (Ser364, Ser428, and Thr439) and lacks a site equivalent to Tyr341 of c-Raf (8,9). Research studies have shown that the B-Raf mutation V600E results in elevated kinase activity and is commonly found in malignant melanoma (10). Six residues of c-Raf (Ser29, Ser43, Ser289, Ser296, Ser301, and Ser642) become hyperphosphorylated in a manner consistent with c-Raf inactivation. The hyperphosphorylation of these six sites is dependent on downstream MEK signaling and renders c-Raf unresponsive to subsequent activation events (11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Killer cell immunoglobulin-like receptors (KIRs) are type 1 transmembrane glycoproteins expressed by natural killer cells and subsets of CD4, CD8, and γδ T cells (1-5). Analogous to the diversity of their human leucocyte antigen class I (HLA Class I) ligands, the KIR genes are polymorphic and the content of the KIR gene cluster varies among haplotypes, although several "framework" genes are found in all haplotypes (6-7). The KIR proteins are characterized by the number of extracellular immunoglobulin-superfamily domains (2D or 3D) and by whether they have a long (L) or short (S) cytoplasmic domain (8-10). KIR proteins with the long cytoplasmic domain transduce inhibitory signals upon ligand binding via an immune tyrosine-based inhibitory motif (ITIM) (10), while KIR proteins with the short cytoplasmic domain lack an ITIM and instead transduce activating signals (11,12). KIR proteins play an important role in the regulation of the immune response. Combinations of KIR and HLA class I variants influence susceptibility to autoimmunity and infectious disease, as well as outcomes of haematopoietic stem cell transplantation (12-14).

$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 Nur77 (D63C5) XP® Rabbit mAb #3960.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Nur77, also known as TR3 and NGFI-B, is an immediate-early response gene and an orphan member of the steroid/thyroid/retinoid receptor superfamily (1-3). Nur77 is composed of an amino-terminal transactivation domain, a central DNA-binding domain and a carboxy-terminal ligand-binding domain. Expression of Nur77 is rapidly induced by a variety of stimuli, including apoptotic, mitogenic and stress signals (1-6). It has been proposed to have many functions related to cell proliferation, differentiation and apoptosis. Nur77 has been extensively studied in T cells where it has been implicated in the process of negative selection and TCR-mediated apoptosis (5,6). Nur77 binds to specific DNA elements leading to the regulation of target genes (7). As a possible mechanism for regulating apoptosis, Nur77 can induce the expression of apoptotic genes such as FasL and TRAIL (8,9). Nur77 is heavily phosphorylated by multiple kinases, which may affect its transactivation activity as well as its subcellular localization (4,10,11). Translocation of Nur77 from the nucleus to the mitochondria can regulate its association with Bcl-2 and control the release of cytochrome c, thereby triggering apoptosis (12,13).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: c-Myb is a transcriptional activator that specifically recognizes the sequence 5'-YAAC[GT]G-3'. It is expressed in hematopoietic progenitor cells where it plays an important role in the control of proliferation and differentiation (1-3). c-Myb is required for transcription of genes involved in self-renewal of intestinal stem cells. Importantly, c-Myb regulates expression of Lgr5, a protein expressed in putative intestinal stem cells that give rise to all cell lineages of small intestinal crypts (4). c-Myb is reported to be expressed in colon crypt cells and in human colorectal cancer lines (5,6). Research has shown that c-Myb gene translocations and copy number alterations are found in several leukemias, breast cancer, and other solid tumors (7,8).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: TAZ is a transcriptional co-activator with a PDZ-binding motif that is regulated by its interaction with 14-3-3 proteins (1). TAZ shares homology with the WW domain of Yes-associated protein (YAP) (1). TAZ is proposed to modulate the switch between proliferation and differentiation of mesenchymal stem cells (MSC) via interaction with transcription factors Runx2 and PPARγ. This process is critical to normal tissue development and the prevention of tumor formation. Due to its role in determination of MSC fate, TAZ may have clinical relevance to several human diseases caused by an imbalance of MSC differentiation (2,3). TAZ is negatively regulated via phosphorylation by LATS1/2, core kinases in the Hippo signaling pathway that controls stem cell development, tissue growth and tumor development (4).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 594 fluorescent dye and tested in-house for immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated PD-L1 (Extracellular Domain Specific) (D8T4X) Rabbit mAb #86744.
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: Programmed cell death 1 ligand 1 (PD-L1, B7-H1, CD274) is a member of the B7 family of cell surface ligands that regulate T cell activation and immune responses. The PD-L1 ligand binds the PD-1 transmembrane receptor and inhibits T cell activation. PD-L1 was discovered following a search for novel B7 protein homologs and was later shown to be expressed by antigen presenting cells, activated T cells, and tissues including placenta, heart, and lung (1-3). Similar in structure to related B7 family members, PD-L1 protein contains extracellular IgV and IgC domains and a short, cytoplasmic region. Research studies demonstrate that PD-L1 is expressed in several tumor types, including melanoma, ovary, colon, lung, breast, and renal cell carcinomas (4-6). Expression of PD-L1 in cancer is associated with tumor infiltrating lymphocytes, which mediate PD-L1 expression through the release of interferon gamma (7). Additional research links PD-L1 expression to cancers associated with viral infections (8,9).

$263
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to PE and tested in-house for direct flow cytometry analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: CD14 is a leucine-rich repeat-containing pattern recognition receptor with expression largely restricted to the monocyte/macrophage cell lineage (1). Research studies have shown that CD14 is a bacterial lipopolysaccharide (LPS) binding glycoprotein, expressed as either a GPI-linked membrane protein or a soluble plasma protein (2). LPS induces an upregulation of GPI-linked CD14 expression, which facilitates TLR4 signaling and macrophage activation in response to bacterial infection (3-5).

$84
100 µl
Ghost Dye™ Violet 510 Viability Dye is used to discriminate viable from non-viable mammalian cells in flow cytometry applications. Ghost Dye™ Violet 510 Viability Dye irreversibly binds free amines available on the cell surface as well as intracellular free amines exposed in cells with compromised cell membranes. Non-viable cells with loss of membrane integrity will react with significantly more Ghost Dye™ Violet 510 Viability Dye than healthy cells in the same sample. Cells that exhibit increased fluorescence intensity can be excluded from analysis.
APPLICATIONS

Application Methods: Flow Cytometry

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Catenin δ-1 (p120 catenin) has an amino-terminal coiled-coil domain followed by a regulatory domain containing multiple phosphorylation sites and a central Armadillo repeat domain of ten linked 42-amino acid repeats. The carboxy-terminal tail has no known function (1). Catenin δ-1 fulfills critical roles in the regulation of cell-cell adhesion as it regulates E-cadherin turnover at the cell surface to determine the level of E-cadherin available for cell-cell adhesion (2). Catenin δ-1 has both positive and negative effects on cadherin-mediated adhesion (3). Actin dynamics are also regulated by catenin δ-1, which modulates RhoA, Rac, and cdc42 proteins (1). Analogous to β-catenin, catenin δ-1 translocates to the nucleus, although its role at this location is unclear. Many studies show that catenin δ-1 is expressed irregularly or is absent in various types of tumor cells, suggesting that catenin δ-1 may function as a tumor suppressor (4).

$348
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 CD31 (PECAM-1) (D8V9E) XP® Rabbit mAb #77699.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: CD31 (Platelet Endothelial Cell Adhesion Molecule-1: PECAM-1), a member of the Ig superfamily of cell adhesion molecules, is expressed by circulating platelets, monocytes, neutrophils, some T cells, and endothelial cells and modulates cell adhesion, endothelial cell migration, and angiogenesis (1). CD31 is phosphorylated on Tyr686 at the cytoplasmic carboxy-terminal tail upon various stimuli (e.g. mechanical or oxidative stress), presumably by Src family members (2). The tyrosine phosphorylation mediates associations with a number of SH2 domain-containing binding partners such as PI3 kinase, SHIP, PLCγ, and SHP-2. Thus, CD31 serves as a scaffold for various signaling molecules (3).

$61
500 ml
Ponceau S Staining Solution is supplied as ready to use. This product is recommended for rapid and reversible protein staining on nitrocellulose or PVDF membranes. This staining technique is often utilized to confirm protein electrotransfer in Western blotting assays prior to antibody-based detection.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Western Blotting

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

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

Background: Activation of protein kinase C (PKC) is one of the earliest events in a cascade that controls a variety of cellular responses, including secretion, gene expression, proliferation, and muscle contraction (1,2). PKC isoforms belong to three groups based on calcium dependency and activators. Classical PKCs are calcium-dependent via their C2 domains and are activated by phosphatidylserine (PS), diacylglycerol (DAG), and phorbol esters (TPA, PMA) through their cysteine-rich C1 domains. Both novel and atypical PKCs are calcium-independent, but only novel PKCs are activated by PS, DAG, and phorbol esters (3-5). Members of these three PKC groups contain a pseudo-substrate or autoinhibitory domain that binds to substrate-binding sites in the catalytic domain to prevent activation in the absence of cofactors or activators. Control of PKC activity is regulated through three distinct phosphorylation events. Phosphorylation occurs in vivo at Thr500 in the activation loop, at Thr641 through autophosphorylation, and at the carboxy-terminal hydrophobic site Ser660 (2). Atypical PKC isoforms lack hydrophobic region phosphorylation, which correlates with the presence of glutamic acid rather than the serine or threonine residues found in more typical PKC isoforms. The enzyme PDK1 or a close relative is responsible for PKC activation. A recent addition to the PKC superfamily is PKCμ (PKD), which is regulated by DAG and TPA through its C1 domain. PKD is distinguished by the presence of a PH domain and by its unique substrate recognition and Golgi localization (6). PKC-related kinases (PRK) lack the C1 domain and do not respond to DAG or phorbol esters. Phosphatidylinositol lipids activate PRKs, and small Rho-family GTPases bind to the homology region 1 (HR1) to regulate PRK kinase activity (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Topoisomerases are ubiquitous, conserved enzymes that remove DNA supercoils resulting from processes such as chromosome segregation, DNA replication, transcription, and repair (1). Topoisomerase inhibitors such as camptothecin and etoposide trap the enzyme as a DNA-bound intermediate, and these drugs are used to treat multiple human cancers (1,2). Tyrosyl-DNA-phosphodiesterases TDP1 and TDP2 function in the base excision repair (BER) and nonhomologous end joining (NHEJ) DNA repair pathways, respectively, and function in part in the repair of stalled topoisomerase-DNA complexes (3). Research has shown that inhibitors of tyrosyl-DNA-phosphodiesterases may act synergistically with topoisomerase inhibitors, allowing the potential for a more robust treatment of cancer (4,5). In small cell lung cancer, research suggests that TDP1 and topoisomerase 1 levels can predict sensitivity to topoisomerase 1 inhibitors (6).

$348
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 NF-κB p65 (D14E12) XP® Rabbit mAb #8242.
APPLICATIONS
REACTIVITY
Dog, Hamster, Human, Monkey, Mouse, 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).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 700 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 Aiolos (D1C1E) Rabbit mAb #15103.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: Aiolos is an Ikaros family transcription factor composed of several zinc fingers that mediate DNA binding and homodimerization or heterodimerization with other Ikaros family members (1). Multiple Aiolos isoforms are generated through alternative splicing of the portion of the transcript encoding the amino-terminal zinc fingers (2). Aiolos is expressed by lymphoid tissues, with highest expression levels seen in mature B and T cells (1). Ikaros family proteins control lymphocyte development by recruiting chromatin remodeling complexes to DNA (3). B cells from mice lacking Aiolos have a reduced threshold for activation, increased proliferation, and elevated levels of IgG and IgE. In addition, Aiolos null mice develop B cell lymphomas (4). In T cells, Aiolos contributes to Th17 cell differentiation by suppressing IL-2 expression (5). Aberrant expression of Aiolos in transformed epithelial cells promotes anchorage independence through downregulation of adhesion-related genes (6). Alterations in the Aiolos gene are observed in near haploid acute lymphoblastic leukemia, and the genetic locus containing Aiolos is linked to increased susceptibility to rheumatoid arthritis and systemic lupus erythematosus (7-9).