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Product listing: SQSTM1/p62 (D5L7G) Mouse mAb, UniProt ID Q13501 #88588 to CNOT7 (D3M6O) Rabbit mAb, UniProt ID Q9UIV1 #86665

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, 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.

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

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

Background: Stat2 (113-kDa), originally purified from the nuclei of alpha-interferon-treated cells, is critical to the transcriptional responses induced by type I interferons, IFN-alpha/beta (1,2). Knockout mice with a targeted disruption of Stat2 have higher susceptibility to viral infection and altered responses to type I interferons (3). Stat2 is rapidly activated by phosphorylation at Tyr690 in response to stimulation by IFN-alpha/beta via associations with receptor-bound Jak kinases (4). Unlike other Stat proteins, Stat2 does not form homodimers. Instead, activated Stat2 forms a heterodimer with Stat1 and translocates to the nucleus. There, it associates with the DNA-binding protein p48 and forms the transcriptional activator complex, interferon-stimulated gene factor 3 (ISGF3), promoting transcription from the ISRE (5).

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

Application Methods: Chromatin IP, 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
Mouse

Application Methods: Western Blotting

Background: Integrin α5β8 facilitates activation and release of TGF-β, which has immunosuppressive effects (1). Deletion of integrin β8 from dendritic cells led to development of inflammatory bowl disease and autoimmunity in mice, as well as failure to induce regulatory T cells that require TGF-β for development (2). TGF-β is also involved in Th17 cell differentiation. Mice lacking expression of integrin β8 on dendritic cells fail to develop Th17 cells and are protected from Th17-mediated autoimmune disease (3). Regulatory T cells express high levels of integrin α5β8, which enables them to suppress pathogenic T cell activation by activating latent TGF-β (4). Integrin β8 is also essential for vascular morphogenesis as integrin β8-deficient mice are embryonic or perinatal lethal and exhibit insufficient and abnormal vascular morphogenesis (5).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Synapsins, a group of at least five related members (synapsins Ia, Ib, IIa, IIb, and IIIa), are abundant brain proteins essential for regulating neurotransmitter release (1,2). All synapsins contain a short amino-terminal domain that is highly conserved and phosphorylated by PKA or CaM kinase I (1). Phosphorylation of the synapsin amino-terminal domain at Ser9 inhibits its binding to phospholipids and dissociates synapsins from synaptic vesicles (2).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: B cell maturation antigen (BCMA/TNFRSF17/CD269) is a transmembrane glycoprotein and member of the TNFR superfamily (1). BCMA expression is largely restricted to the B-cell lineage. Pro-survival signaling through this receptor plays a pivotal role in humoral immunity by regulating B-cell maturation and plasma cell differentiation upon binding its ligands, BAFF and APRIL (2-6). BCMA is expressed in a number B-cell malignancies and has garnered much attention as a novel therapeutic target for the treatment of multiple myeloma due to its selective and elevated expression on the cell surface of malignant plasma cells (7-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein ubiquitination and deubiquitination are reversible processes catalyzed by ubiquitinating enzymes and deubiquitinating enzymes, respectively (1,2). Deubiquitinating enzymes (DUBs) are categorized into five subfamilies based on catalytic domain structure: USP, OTU, MJD, and JAMM. The valosin-containing protein p97/p47 complex-interacting protein 1 (VCIP135, VCPIP1) is a deubiquitinating enzyme that belongs to the A20-like subfamily of ovarian tumor (OTU) DUBs (3). VCIP135 serves as a cofactor for the p97/p47 complex in regulating Golgi membrane fusion and reassembly at the end of mitosis (4-6). Research studies suggest that the phosphorylation status of VCIP135 provides a mechanism to fine-tune the kinetics of Golgi disassembly and reassembly during the cell cycle. For example, these studies demonstrate that VCIP135 undergoes phosphorylation early in mitosis, which blocks its association with the Golgi membrane and p97/VCP, thus inhibiting p97/VCP-mediated Golgi membrane fusion (7,8).

$364
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin in combination with cyanine 7 (PE-Cy®7) 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 Phospho-Akt (Ser473) (D9E) XP® Rabbit mAb #4060.
APPLICATIONS
REACTIVITY
Bovine, D. melanogaster, Hamster, Human, Monkey, Mouse, Rat, Zebrafish

Application Methods: Flow Cytometry

Background: Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis (1-3). This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin-sensitive pathway involving PI3 kinase (2,3). Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 (4) and by phosphorylation within the carboxy terminus at Ser473. The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin (mTOR) in a rapamycin-insensitive complex with rictor and Sin1 (5,6). Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad (7), forkhead transcription factors (8), c-Raf (9), and caspase-9. PTEN phosphatase is a major negative regulator of the PI3 kinase/Akt signaling pathway (10). LY294002 is a specific PI3 kinase inhibitor (11). Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK-3α and β (12,13). Akt may also play a role in insulin stimulation of glucose transport (12). In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation by preventing GSK-3β-mediated phosphorylation and degradation of cyclin D1 (14) and by negatively regulating the cyclin dependent kinase inhibitors p27 Kip1 (15) and p21 Waf1/Cip1 (16). Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor (17). More importantly, Akt phosphorylates and inactivates tuberin (TSC2), an inhibitor of mTOR within the mTOR-raptor complex (18,19).

$327
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 647 fluorescent dye and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated Phospho-IRAK4 (Thr345/Ser346) (D6D7) Rabbit mAb #11927.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Interleukin-1 (IL-1) receptor-associated kinase (IRAK) is a serine/threonine-specific kinase that can be coprecipitated in an IL-1-inducible manner with the IL-1 receptor (1). The mammalian family of IRAK molecules contains four members (IRAK1, IRAK2, IRAK3/IRAK-M, and IRAK4). The binding of IL-1 to IL-1 receptor type I (IL-1RI) initiates the formation of a complex that includes IL-1RI, AcP, MyD88, and IRAKs (2). IRAK undergoes autophosphorylation shortly after IL-1 stimulation. The subsequent events involve IRAK dissociation from the IL-1RI complex, its ubiquitination, and its association with two membrane-bound proteins: TAB2 and TRAF6. The resulting IRAK-TRAF6-TAB2 complex is then released into the cytoplasm where it activates protein kinase cascades, including TAK1, IKKs, and the stress-activated kinases (3).

$293
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Galectins are a family of β-galactose binding proteins that are characterized by an affinity for poly-N-acetyllactosamine-enriched glycoconjugates and a carbohydrate-binding site (1,2). Members of the galectin family have been implicated in a variety of biological functions including cell adhesion (3), growth regulation (4), cytokine production (5), T-cell apoptosis (6), and immune responses (7).Galectin-3/LGALS3 is involved in several diverse biological functions. Galectin-3/LGALS3 binds IgE (8). Galectin-3/LGALS3 is an unusual protein in that can be found both extracellularly and intracellularly. Intracellularly, galectin-3/LGALS3 can localize to the cytoplasm, nucleus, or both, depending on cell type and experimental conditions. Nuclear galectin-3/LGALS3 has been identified as a pre-mRNA splicing factor (9). Galectin-3/LGALS3 production has been shown to increase during inflammation and in obesity, and the protein itself can have an inflammatory effect under certain conditions (10). Galectin-3/LGALS3 forms a complex with α3, β1 integrin to act as a surface receptor on endothelial cells for the NG2 proteoglycan, which triggers cell motility and angiogenesis (11). In addition to these functions, galectin-3/LGALS3 is also a required factor for the terminal differentiation of epithelial cells (12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The matrix metalloproteinases (MMPs) are a family of proteases that target many extracellular proteins including other proteases, growth factors, cell surface receptors, and adhesion molecules (1). Among the family members, MMP-2, MMP-3, MMP-7, and MMP-9 have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis, and apoptosis (2-4). Research studies have shown that MMP activity correlates with cancer development (2). One mechanism of MMP regulation is transcriptional (5). Once synthesized, MMP exists as a latent proenzyme. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full length protein (5).

$327
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) 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 Phospho-SAMHD1 (Thr592) (D7O2M) Rabbit mAb #89930.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: SAM domain and HD domain-containing protein 1 (SAMHD1) is a negative regulator of the cell-intrinsic innate immune response (1). Research studies have identified mutations in SAMHD1 as a cause of Aicardi-Goutieres syndrome, an autoimmune disease characterized by elevated production of interferon-α and symptoms resembling congenital viral infection (1). SAMHD1 was identified as the restriction factor that renders most myeloid cells refractory to human immunodeficiency virus (HIV) infection (2-4). Expression of the viral protein Vpx in refractory cells targets SAMHD1 for ubiquitin-mediated degradation and relieves HIV restriction. SAMHD1 prevents autoimmunity and HIV infection by hydrolyzing intracellular deoxynucleoside triphosphates (dNTPs), thereby limiting inappropriate immune activation by self nucleic acid and inhibiting reverse transcription of the HIV genome (4-6).

$327
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) 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 Phospho-Stat3 (Ser727) (D4X3C) Rabbit mAb #34911.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: The Stat3 transcription factor is an important signaling molecule for many cytokines and growth factor receptors (1) and is required for murine fetal development (2). Research studies have shown that Stat3 is constitutively activated in a number of human tumors (3,4) and possesses oncogenic potential (5) and anti-apoptotic activities (3). Stat3 is activated by phosphorylation at Tyr705, which induces dimerization, nuclear translocation, and DNA binding (6,7). Transcriptional activation seems to be regulated by phosphorylation at Ser727 through the MAPK or mTOR pathways (8,9). Stat3 isoform expression appears to reflect biological function as the relative expression levels of Stat3α (86 kDa) and Stat3β (79 kDa) depend on cell type, ligand exposure, or cell maturation stage (10). It is notable that Stat3β lacks the serine phosphorylation site within the carboxy-terminal transcriptional activation domain (8).

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

Application Methods: Western Blotting

Background: YTH domain-containing protein 1 (YTHDC1) and YTH domain-containing protein 2 (YTHDC2) both belong to a family of proteins that bind to RNA. YTHDC1 and YTHDC2 both recognize and bind to N6-methyladenosine(m6A)-containing RNAs; binding is mediated through the YTH domains (1-3). m6A is a modification that is present at internal sites of mRNAs and some non-coding RNAs and plays a role in regulating mRNA splicing, processing, and stability. YTHDC1, also known as splicing factor YT521, regulates alternative splicing by functioning as a key regulator of exon-inclusion or exon-skipping. YTHDC1 promotes exon-inclusion by recruiting pre-mRNA splicing factor SRSF3 to regions containing m6A, while repressing exon-skipping by blocking SRSF10 binding to these same regions (2). Increased expression of YTHDC1 promotes malignant endometrial carcinoma (EC) through alternative splicing of vascular endothelial growth factor A (VEGF-A), resulting in an increase in VEGF-165 isoform and increased EC cell invasion (4). YTHDC2 functions to enhance the translation efficiency of target mRNAs and may play a role in spermatogenesis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Frozen)

Background: The Na-K-2Cl cotransporter (NKCC2) is a sodium-potassium-chloride cotransporter. It is mainly expressed on the luminal membrane of renal epithelial cells of the thick ascending limb of Henle's loop (TALH) and mediates the majority of NaCl resorption and concentration of urine (1,2). NKCC2 is the target for several diuretic drugs, such as bumetanide, and is involved in the pathogenesis of hypertension (3,4). Mutations in the NKCC2-encoding gene, SLC12A1, causes Bartter’s syndrome, which is featured by impaired salt reabsorption in the TALH, hypokalemic metabolic alkalosis, and hypercalciuria (5,6). Recently, NKCC2 was reported to be expressed in the brain hypothalamo-neurohypophyseal system (HNS) and upregulated upon osmotic stress (7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Bruton's tyrosine kinase (Btk) is a member of the Btk/Tec family of cytoplasmic tyrosine kinases. Like other Btk family members, it contains a pleckstrin homology (PH) domain and Src homology SH3 and SH2 domains. Btk plays an important role in B cell development (1,2). Activation of B cells by various ligands is accompanied by Btk membrane translocation mediated by its PH domain binding to phosphatidylinositol-3,4,5-trisphosphate (3-5). The membrane-localized Btk is active and associated with transient phosphorylation of two tyrosine residues, Tyr551 and Tyr223. Tyr551 in the activation loop is transphosphorylated by the Src family tyrosine kinases, leading to autophosphorylation at Tyr223 within the SH3 domain, which is necessary for full activation (6,7). The activation of Btk is negatively regulated by PKCβ through phosphorylation of Btk at Ser180, which results in reduced membrane recruitment, transphosphorylation, and subsequent activation (8). The PKC inhibitory signal is likely to be a key determinant of the B cell receptor signaling threshold to maintain optimal Btk activity (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Iron-sulfur (Fe-S) clusters (ISC) are cofactors for many proteins that display a wide range of biological functions, such as DNA maintenance, transcription, translation, cellular metabolism, electron transport, and oxidative phosphorylation (1). While structurally simple, the synthesis and insertion of ISC into Fe-S proteins are complex processes that involve many different proteins. The cytosolic iron-sulfur assembly component 1 (CIAO1) protein is a key component of the cytosolic ISC assembly machinery that incorporates ISC into cytoplasmic and nuclear Fe-S proteins in eukaryotic cells (1,2). CIAO1, along with MMS19, XPD, FAM96B, and ANT2, comprise a complex that localizes to the mitotic spindle during mitosis, which suggests a role in chromosome segregation (3-6). The CIAO1 protein interacts with Wilms' tumor suppressor protein (WT1) and may affect its transactivation activity (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: CD68 (macrosialin) is a heavily glycosylated transmembrane protein that is expressed by and commonly used as a marker for monocytes and macrophages (1, 2). It is found on the plasma membrane, as well as endosomal and lysosomal membranes (1-3). It is proposed to bind OxLDL and has been observed as a homodimer (3, 4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: MDM2, a ubiquitin ligase for p53, plays a central role in regulation of the stability of p53 (1). Akt-mediated phosphorylation of MDM2 at Ser166 and Ser186 increases its interaction with p300, allowing MDM2-mediated ubiquitination and degradation of p53 (2-4). Phosphorylation of MDM2 also blocks its binding to p19ARF, increasing the degradation of p53 (3).

$116
0.5nmol
60 µl
RNA interference is a method whereby gene expression can be selectively silenced through the delivery of double-stranded RNA molecules into the cell. SignalSilence® Control siRNA (Cy5® Conjugate) from Cell Signaling Technology (CST) is an siRNA sequence that will not lead to the specific degradation of any cellular message. It is intended to serve as a negative control for experiments using targeted siRNA transfection. In addition, this siRNA is Cy5®-conjugated to allow the researcher to assess transfection efficiency by fluorescence microscopy.
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Bcl-2 family consists of a number of evolutionarily conserved proteins containing Bcl-2 homology domains (BH) that regulate apoptosis through control of mitochondrial membrane permeability and release of cytochrome c (1-3). Four BH domains have been identified (BH1-4) that mediate protein interactions. The family can be separated into three groups based upon function and sequence homology: pro-survival members include Bcl-2, Bcl-xL, Mcl-1, A1 and Bcl-w; pro-apoptotic proteins include Bax, Bak and Bok; and "BH3 only" proteins Bad, Bik, Bid, Puma, Bim, Bmf, Noxa and Hrk. Interactions between death-promoting and death-suppressing Bcl-2 family members has led to a rheostat model in which the ratio of pro-apoptotic and anti-apoptotic proteins controls cell fate (4). Thus, pro-survival members exert their behavior by binding to and antagonizing death-promoting members. In general, the "BH3-only members" can bind to and antagonize the pro-survival proteins leading to increased apoptosis (5). While some redundancy of this system likely exists, tissue specificity, transcriptional and post-translational regulation of many of these family members can account for distinct physiological roles.

$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 DYKDDDDK Tag (D6W5B) Rabbit mAb #14793.
APPLICATIONS
REACTIVITY
All Species Expected

Application Methods: Western Blotting

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

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

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

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).

$131
100 tests
500 µl
This Cell Signaling Technology antibody is conjugated to FITC and tested in-house for direct flow cytometry analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: When T cells encounter antigens via the T cell receptor (TCR), information about the quantity and quality of antigens is relayed to the intracellular signal transduction machinery (1). This activation process depends mainly on CD3 (Cluster of Differentiation 3), a multiunit protein complex that directly associates with the TCR. CD3 is composed of four polypeptides: ζ, γ, ε and δ. Each of these polypeptides contains at least one immunoreceptor tyrosine-based activation motif (ITAM) (2). Engagement of TCR complex with foreign antigens induces tyrosine phosphorylation in the ITAM motifs and phosphorylated ITAMs function as docking sites for signaling molecules such as ZAP-70 and p85 subunit of PI-3 kinase (3,4). TCR ligation also induces a conformational change in CD3ε, such that a proline region is exposed and then associates with the adaptor protein Nck (5).

$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 E-Cadherin (4A2) Mouse mAb #14472.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Cadherins are a superfamily of transmembrane glycoproteins that contain cadherin repeats of approximately 100 residues in their extracellular domain. Cadherins mediate calcium-dependent cell-cell adhesion and play critical roles in normal tissue development (1). The classic cadherin subfamily includes N-, P-, R-, B-, and E-cadherins, as well as about ten other members that are found in adherens junctions, a cellular structure near the apical surface of polarized epithelial cells. The cytoplasmic domain of classical cadherins interacts with β-catenin, γ-catenin (also called plakoglobin), and p120 catenin. β-catenin and γ-catenin associate with α-catenin, which links the cadherin-catenin complex to the actin cytoskeleton (1,2). While β- and γ-catenin play structural roles in the junctional complex, p120 regulates cadherin adhesive activity and trafficking (1-4). Investigators consider E-cadherin an active suppressor of invasion and growth of many epithelial cancers (1-3). Research studies indicate that cancer cells have upregulated N-cadherin in addition to loss of E-cadherin. This change in cadherin expression is called the "cadherin switch." N-cadherin cooperates with the FGF receptor, leading to overexpression of MMP-9 and cellular invasion (3). Research studies have shown that in endothelial cells, VE-cadherin signaling, expression, and localization correlate with vascular permeability and tumor angiogenesis (5,6). Investigators have also demonstrated that expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers (7,8).

$364
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 Phospho-Akt (Thr308) (D25E6) XP® Rabbit mAb #13038.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Akt, also referred to as PKB or Rac, plays a critical role in controlling survival and apoptosis (1-3). This protein kinase is activated by insulin and various growth and survival factors to function in a wortmannin-sensitive pathway involving PI3 kinase (2,3). Akt is activated by phospholipid binding and activation loop phosphorylation at Thr308 by PDK1 (4) and by phosphorylation within the carboxy terminus at Ser473. The previously elusive PDK2 responsible for phosphorylation of Akt at Ser473 has been identified as mammalian target of rapamycin (mTOR) in a rapamycin-insensitive complex with rictor and Sin1 (5,6). Akt promotes cell survival by inhibiting apoptosis through phosphorylation and inactivation of several targets, including Bad (7), forkhead transcription factors (8), c-Raf (9), and caspase-9. PTEN phosphatase is a major negative regulator of the PI3 kinase/Akt signaling pathway (10). LY294002 is a specific PI3 kinase inhibitor (11). Another essential Akt function is the regulation of glycogen synthesis through phosphorylation and inactivation of GSK-3α and β (12,13). Akt may also play a role in insulin stimulation of glucose transport (12). In addition to its role in survival and glycogen synthesis, Akt is involved in cell cycle regulation by preventing GSK-3β-mediated phosphorylation and degradation of cyclin D1 (14) and by negatively regulating the cyclin dependent kinase inhibitors p27 Kip1 (15) and p21 Waf1/Cip1 (16). Akt also plays a critical role in cell growth by directly phosphorylating mTOR in a rapamycin-sensitive complex containing raptor (17). More importantly, Akt phosphorylates and inactivates tuberin (TSC2), an inhibitor of mTOR within the mTOR-raptor complex (18,19).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Mitochondrial fission factor (MFF) is a tail-anchored protein that resides within the outer mitochondrial membrane and is part of the mitochondrial fission complex. MFF participates in mitochondrial fission by serving as one of multiple receptors for the GTPase dynamin-related protein 1 (Drp1) (1-4). Research studies have also shown that MFF is a peroxisomal membrane protein and participates in peroxisome fission by serving as a receptor for another GTPase, dynamin-like protein 1 (5,6).

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

Application Methods: Western Blotting

Background: The evolutionarily conserved CCR4-NOT (CNOT) complex regulates mRNA metabolism in eukaryotic cells (1). This regulation occurs at different levels of mRNA synthesis and degradation, including transcription initiation, elongation, deadenylation, and degradation (1). Multiple components, including CNOT1, CNOT2, CNOT3, CNOT4, CNOT6, CNOT6L, CNOT7, CNOT8, CNOT9, and CNOT10 have been identified in this complex (2). In addition, subunit composition of this complex has been shown to vary among different tissues (3).