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Product listing: DDR1 Antibody, UniProt ID Q08345 #3917 to LRP5 (D5G4) Rabbit mAb, UniProt ID O75197 #5440

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The discoidin domain receptors (DDRs) are receptor tyrosine kinases with a discoidin homology repeat in their extracellular domains, activated by binding to extracellular matrix collagens. So far, two mammalian DDRs have been identified: DDR1 and DDR2 (1). They are widely expressed in human tissues and may have roles in smooth muscle cell-mediated collagen remodeling (2). Research studies have implicated aberrant expression and signaling of DDRs in human diseases related to increased matrix degradation and remodeling, such as cardiovascular disease, liver fibrosis, and tumor invasion (1).

PTMScan® Technology employs a proprietary methodology from Cell Signaling Technology (CST) for peptide enrichment by immunoprecipitation using a specific bead-conjugated antibody in conjunction with liquid chromatography (LC) tandem mass spectrometry (MS/MS) for quantitative profiling of post-translational modification (PTM) sites in cellular proteins. These include phosphorylation (PhosphoScan®), ubiquitination (UbiScan®), acetylation (AcetylScan®), and methylation (MethylScan®), among others. PTMScan® Technology enables researchers to isolate, identify, and quantitate large numbers of post-translationally modified cellular peptides with a high degree of specificity and sensitivity, providing a global overview of PTMs in cell and tissue samples without preconceived biases about where these modified sites occur (1). For more information on PTMScan® Proteomics Services, please visit www.cellsignal.com/common/content/content.jsp?id=ptmscan-services.
$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Ubiquitinating enzymes (UBEs) catalyze protein ubiquitination, a reversible process countered by deubiquitinating enzyme (DUB) action (1,2). Five DUB subfamilies are recognized, including the USP, UCH, OTU, MJD, and JAMM enzymes. The deubiquitinating enzyme ubiquitin-specific protease 8 (USP8/UBPy) is a cysteine protease belonging to the USP/UBP subfamily. Research studies have shown that USP8 is an essential growth-regulated enzyme indespensible for cell proliferation and survival (3,4). Indeed, conditional knock-out of murine USP8 was shown to promote a dramatic loss in expression of receptor tyrosine kinases, including EGFR, ErbB3, and c-Met (4). In agreement with these findings, USP8 inactivation leads to enhanced ubiquitination of ligand-activated EGFR (5,6). Furthermore, phosphorylation of USP8 at Ser680 results in its binding of 14-3-3, catalytic inactivation, and reduced EGFR deubiquitination (7). It appears as though USP8, in conjunction with components of the ESCRT-0 complex, plays an integral role in the early endosomal sorting machinery that functions to protect EGFR from lysosomal degradation (8,9).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 594 fluorescent dye and tested in-house for direct immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Nanog (D73G4) XP® Rabbit mAb #4903.
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry)

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: Western Blotting

Background: Tyrosine kinase non-receptor 1 (TNK1) is related to the Ack1 (TNK2) non-receptor kinase that binds cdc42 and inhibits GTPase activity of this cell cycle regulator. TNK1 is broadly expressed in embryogenic tissues and leukemia cell lines, but is restricted to select adult tissues (1). TNK1 is a putative 72 kDa protein comprised of an N-terminal kinase domain, a central SH3 domain and a proline-rich tail. Interaction with PLCγ in vitro indicates a possible role in phospholipid signal transduction pathways (2). Though the exact mechanism is currently unclear, active TNK1 may play a role in regulating cell death by preventing TNF-α-induced NF-κB transactivation (3).

$39
50 ml
This blocking reagent is designed to reduce noise originating from nonspecific protein-protein interactions in immunofluorescence assays. The core formulation includes goat serum as a protein blocker mixed with a mild detergent to facilitate permeabilization of cellular membranes.Cell Signaling Technology recommends using the buffer in accordance with our protocols for cultured cells (IF-IC) and frozen tissue sections (IF-F) to ensure accurate and reproducible results.The product is supplied as a 1X working solution and contains enough material for 500 assays based on a 100 μl assay volume.
APPLICATIONS

Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry)

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: Antigen receptors found on the surface of B cells contain a heterodimeric signaling component composed of CD79A and CD79B, also known as Ig α and Ig β, respectively (1,2). Presence of this receptor complex is essential for B-cell development and function (3). Together these two proteins and the associated B cell receptor initiate intracellular signaling following antigen binding (4,5). An immunoreceptor tyrosine-based activation motif (ITAM) found in the CD79A intracellular region appears to be important for its function (6). Antigen binding precedes formation of the CD79A and CD79B heterodimer and subsequent activation of receptor associated kinases (7). Research has shown that CD79A is a marker for B-lineage lymphoblastic leukemia (8). Additionally, investigators have found that mutations in the CD79A (MB1) gene are associated with abnormally low levels of functional B cell receptors in some cases of chronic B cell lymphocytic leukemia (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Ectonucleotide pyrophosphatase-phosphodiesterase 1 (ENPP1) is a single-pass, type II transmembrane protein primarily involved in ATP hydrolysis at the plasma membrane. Targeting of ENPP1 to the basolateral cell surface relies on the presence of a carboxy-terminal di-leucine-based signal (1). ENPP1 plays important roles in bone mineralization and soft tissue calcification (2-5). Mutations in the corresponding ENPP1 gene cause generalized arterial calcification in infancy (GACI) and idiopathic infantile arterial calcification (IIAC) (6,7). ENPP1 inhibits insulin receptor function and overexpression of this enzyme causes insulin resistance and glucose intolerance in mice (8,9). Genetic variants of ENPP1 have been associated with obesity and type 2 diabetes (10-12).

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

Application Methods: Western Blotting

Background: Fragile X syndrome is a genetic disorder characterized by a spectrum of physical and behavioral features and is a frequent form of inherited mental retardation (1). X-linked FMRP (FMR-1) and its two autosomal homologs, FXR1 and FXR2, are polyribosome-associated RNA-binding proteins that are involved in the pathogenesis of fragile X syndrome (1-3). Each of the fragile X proteins can self-associate, as well as form heteromers with the other two related proteins (3). FMRP can act as a translation regulator and is a component of RNAi effector complexes (RISC), suggesting a role in gene silencing (4). The Drosophila homolog of FMRP (dFMRP) associates with Argonaute 2 (Ago2) and Dicer and can coimmunoprecipitate with miRNA and siRNA (5). These results suggest that fragile X syndrome is related to abnormal translation caused by defects in RNAi-related pathways. In addition, FMRP, FXR1, and FXR2 are components of stress granules (SG) and have been implicated in the translational regulation of mRNAs (6).

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

Application Methods: Immunoprecipitation, Western Blotting

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated p21 Waf1/Cip1 (12D1) Rabbit mAb #2947.
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry

Background: The tumor suppressor protein p21 Waf1/Cip1 acts as an inhibitor of cell cycle progression. It functions in stoichiometric relationships forming heterotrimeric complexes with cyclins and cyclin-dependent kinases. In association with CDK2 complexes, it serves to inhibit kinase activity and block progression through G1/S (1). However, p21 may also enhance assembly and activity in complexes of CDK4 or CDK6 and cyclin D (2). The carboxy-terminal region of p21 is sufficient to bind and inhibit PCNA, a subunit of DNA polymerase, and may coordinate DNA replication with cell cycle progression (3). Upon UV damage or during cell cycle stages when cdc2/cyclin B or CDK2/cyclin A are active, p53 is phosphorylated and upregulates p21 transcription via a p53-responsive element (4). Protein levels of p21 are downregulated through ubiquitination and proteasomal degradation (5).

$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 Rab7 (D95F2) XP® Rabbit mAb #9367.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Rab7 and Rab9 are members of the Ras superfamily of small Rab GTPases (1). Both proteins are located in late endosomes, but exert different functions. Rab7 associates with the RIPL effector protein to control membrane trafficking from early to late endosome and to lysosomes (2,3). Rab7 also helps to regulate growth receptor endocytic trafficking and degradation (3,4), and maturation of phagosome and autophagic vacuoles (4-6). Rab9 interacts with its effector proteins p40 and TIP47 (7,8) to promote the MPR (mannose 6-phosphate receptor)-associated lysosomal enzyme transport between late endosomes and the trans Golgi network (9,10).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Galectins are a family of β-galactose binding proteins that are characterized by their affinity for poly-N-acetyllactosamine-enriched glycoconjugates and their 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-1/LGALS1 has been shown to be expressed in a wide range of tissues and cell types. The level and pattern of expression of galectin-1 have been shown to change during development (8). In addition to a role in developmental processes, galectin-1 has been shown to be involved in central immune tolerance and may function in tumorigenesis by modulating the immune response to the tumor (9,10). Research studies have shown that galectin-1 expression is increased in several human cancers, suggesting a correlation with metastatic potential (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The kindlin family of focal adhesion proteins is involved in multiple biological processes, including integrin signaling, adhesion, migration, angiogenesis, differentiation, and mitotic spindle formation (1,2). Kindlin family members 1, 2, and 3 (FERM1, FERM2, and URP2) are differentially expressed in tissues. Kindlin-1 is primarily expressed in epithelial cells, kindlin-2 is ubiquitously expressed, and kindlin-3 expression is restricted to the hematopoietic system (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Notch proteins (Notch1-4) are a family of transmembrane receptors that play important roles in development and the determination of cell fate (1). Mature Notch receptors are processed and assembled as heterodimeric proteins, with each dimer comprised of a large extracellular ligand-binding domain, a single-pass transmembrane domain, and a smaller cytoplasmic subunit (Notch intracellular domain, NICD) (2). Binding of Notch receptors to ligands of the Delta-Serrate-Lag2 (DSL) family triggers heterodimer dissociation, exposing the receptors to proteolytic cleavages; these result in release of the NICD, which translocates to the nucleus and activates transcription of downstream target genes (3,4).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Prdx1 belongs to a family of non-seleno peroxidases that function as H2O2 scavengers. All 6 Prdx isoforms share a conserved N-terminal cysteine (Cys51) that is oxidized by H2O2 to form cysteine-sulfenic acid (Cys51-SOH) and, in turn, reacts with Cys172-SH of another Prdx protein, forming a disulfide dimer and protecting it from degradation (1-3). Abnormally high levels of H2O2 cause Prdx1 to form an oligomeric chaperone that loses its peroxidase activity (4). Prdx family members have been reported to bind to JNK and c-Abl and regulate their kinase activity (5,6). Prdx1 was shown to bind to PTEN and regulate its phosphatase activity in conditions of mild or no cellular stress, hence preventing Akt-driven transformation by protecting PTEN from oxidation-induced inactivation (7).

$327
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 Cleaved Caspase-7 (Asp198) (D6H1) Rabbit mab #8438.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Caspase-7 (CMH-1, Mch3, ICE-LAP3) has been identified as a major contributor to the execution of apoptosis (1-4). Caspase-7, like caspase-3, is an effector caspase that is responsible for cleaving downstream substrates such as (ADP-ribose) polymerase and PARP (1,3). During apoptosis, caspase-7 is activated through proteolytic processing by upstream caspases at Asp23, Asp198, and Asp206 to produce the mature subunits (1,3). Similar to caspase-2 and -3, caspase-7 preferentially cleaves substrates following the recognition sequence DEVD (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Guanine monophosphate synthase (GMPS) catalyzes the conversion of xanthosine 5’-monophosphate (XMP) into GMP during the final step of de novo guanine nucleotide synthesis. In addition to comprising the building blocks for DNA and RNA, guanine nucleotides also provide GTP for many signaling pathways that are important for multiple cellular processes (1). Chromosomal translocations involving MLL and GMPS is reported in some patients diagnosed with acute myeloid leukemia (2). Research studies indicate that genotoxic stress or nucleotide deprivation prompts translocation of GMPS to the nucleus where it complexes with USP7 and p53 to promote p53 stabilization (3). Additional studies show that the nuclear GMPS-USP7 protein complex deubiquitinates histone H2B in Drosophila (4).

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

Application Methods: Western Blotting

Background: Enolase is an important glycolytic enzyme involved in the interconversion of 2-phosphoglycerate to phosphoenolpyruvate. Mammalian enolase exists as three subunits: enolase-1 (α-enolase), enolase-2 (γ-enolase) and enolase-3 (β-enolase) that can form both homo- and heterodimers. Expression of the enolase isoforms differs in a tissue specific manner (1). Enolase-1 plays a key role in anaerobic metabolism under hypoxic conditions and may act as a cell surface plasminogen receptor during tissue invasion (2,3). Abnormal expression of enolase-1 is associated with tumor progression in some cases of breast and lung cancer (4-7). Alternatively, an enolase-1 splice variant (MBP-1) binds the c-myc promoter p2 and may function as a tumor suppressor. For this reason enolase-1 is considered as a potential therapeutic target in the treatment of some forms of cancer (8).

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

Application Methods: Western Blotting

Background: MAP kinases are inactivated by dual-specificity protein phosphatases (DUSPs) that differ in their substrate specificity, tissue distribution, inducibility by extracellular stimuli, and cellular localization. DUSPs, also known as MAPK phosphatases (MKP), specifically dephosphorylate both threonine and tyrosine residues in MAPK P-loops and have been shown to play important roles in regulating the function of the MAPK family (1,2). At least 13 members of the family (DUSP1-10, DUSP14, DUSP16, and DUSP22) display unique substrate specificities for various MAP kinases (3). MAPK phosphatases typically contain an amino-terminal rhodanese-fold responsible for DUSP docking to MAPK family members and a carboxy-terminal catalytic domain (4). These phosphatases can play important roles in development, immune system function, stress responses, and metabolic homeostasis (5). In addition, research studies have implicated DUSPs in the development of cancer and the response of cancer cells to chemotherapy (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Macrophage-colony stimulating factor (M-CSF, CSF-1) receptor is an integral membrane tyrosine kinase encoded by the c-fms proto-oncogene. M-CSF receptor is expressed in monocytes (macrophages and their progenitors) and drives growth and development of this blood cell lineage. (1-3). Binding of M-CSF to its receptor induces receptor dimerization, activation, and autophosphorylation of cytoplasmic tyrosine residues used as docking sites for SH2-containing signaling proteins (4). There are at least five major tyrosine autophosphorylation sites. Tyr723 (Tyr721 in mouse) is located in the kinase insert (KI) region. Phosphorylated Tyr723 binds the p85 subunit of PI3 kinase as well as PLCγ2 (5). Phosphorylation of Tyr809 provides a docking site for Shc (5). Overactivation of this receptor can lead to a malignant phenotype in various cell systems (6). The activated M-CSF receptor has been shown to be a predictor of poor outcome in advanced epithelial ovarian carcinoma (7) and breast cancer (8).

$489
96 assays
1 Kit
The PathScan® Total Neurofilament-L Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of neurofilament-L protein. A neurofilament-L mouse mAb has been coated onto the microwells. After incubation with cell lysates, the neurofilament-L proteins are captured by the coated antibody. Following extensive washing, an neurofilament-L rabbit detection mAb is added to detect captured neurofilament-L proteins. Anti-rabbit IgG, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of absorbance for the developed color is proportional to the quantity of neurofilament-L protein.Antibodies in the kit are custom formulations specific to the kit.
REACTIVITY
Mouse, Rat

Background: The cytoskeleton consists of three types of cytosolic fibers: actin microfilaments, intermediate filaments, and microtubules. Neurofilaments are the major intermediate filaments found in neurons and consist of light (NFL), medium (NFM), and heavy (NFH) subunits (1). Similar in structure to other intermediate filament proteins, neurofilaments have a globular amino-terminal head, a central α-helical rod domain, and a carboxy-terminal tail. A heterotetrameric unit (NFL-NFM and NFL-NFH) forms a protofilament, with eight protofilaments comprising the typical 10 nm intermediate filament (2). While neurofilaments are critical for radial axon growth and determine axon caliber, microtubules are involved in axon elongation. PKA phosphorylates the head domain of NFL and NFM to inhibit neurofilament assembly (3,4). Research studies have shown neurofilament accumulations in many human neurological disorders including Parkinson's disease (in Lewy bodies along with α-synuclein), Alzheimer's disease, Charcot-Marie-Tooth disease, and Amyotrophic Lateral Sclerosis (ALS) (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Catechol-O-methyltransferase (COMT) is an intracellular enzyme that catalyzes the O-methylation and inactivation of catecholamine neurotransmitters and hormones, including dopamine, epinephrine, and norepinephrine (1). Two distinct COMT proteins are generated from separate promoters in cells, including a 28 kDa, membrane-bound protein (mb-COMT), and a soluble protein (s-COMT) of 24 kDa (2,3). The soluble s-COMT is the predominant form of COMT found in peripheral organs, while the mb-COMT protein is more abundant in the central nervous system (4,5).In addition to inactivating endogenous catecholamines, COMT can also inhibit catechol-based drugs used to treat a number of disorders, including Parkinson's disease and schizophrenia. Research studies using COMT inhibitors indicate that these reagents can prolong the bioavailability of psychoactive drugs such as levodopa by preventing O-methylation and subsequent degradation (6). A Val158Met polymorphism in the corresponding COMT gene reduces COMT enzymatic activity and leads to increased cortical dopamine levels (7). Several research studies suggest that this reduced COMT activity is associated with a large number of mental disorders, including schizophrenia, bipolar disorder, attention deficit hyperactivity disorder, obsessive-compulsive disorder, and anorexia nervosa (reviewed in 8).

$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 mouse cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated Cox2 (D5H5) XP® Rabbit mAb #12282.
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Cyclooxygenase1 (Cox1) and cyclooxygenase2 (Cox2), family members with 60% homology in humans, catalyze prostaglandin production from arachidonic acid (1,2). While Cox1 expression is constitutive in most tissues, Cox2 expression is induced by lipopolysaccharide (LPS) and peptidoglycan (PGN) (3). PGN activates Ras, leading to phosphorylation of Raf at Ser338 and Erk1/2 at Tyr204. The activation of MAP kinase signaling results in subsequent activation of IKKα/β, phosphorylation of IκBα at Ser32/36, and NF-κB activation. Finally, activation of the transcription factor NF-κB is responsible for the induction of Cox2 expression (4). Investigators have shown that LPS and PGN induce the clinical manifestations of arthritis and bacterial infections, such as inflammation, fever, and septic shock (5). Research studies have indicated that Cox1 and Cox2 may also play a role in the neuropathology of Alzheimer's disease by potentiating γ-secretase activity and β-amyloid generation (6).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Nuclear cap-binding protein subunit 1 (NCBP1), also known as cap-binding protein 80 (CBP80), plays a role in nuclear pre-mRNA splicing (1,2). It has also been shown to function in the nonsense-mediated decay (NMD) of mRNAs where translation is prematurely terminated (3). NCBP1/CBP80 increases the efficiency of NMD by promoting the interaction of two active NMD components Upf1 and Upf2 (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Amplified in Osteosarcoma 9 (OS-9) was identified as a gene that is frequently amplified in human sarcomas (1). OS-9 is an N-glycosylated ER resident protein that harbors a mannose-6-phosphate receptor homology (MRH) domain and plays a critical role in mammalian ER quality control, in part, by functioning as a lectin. There are two major isoforms of OS-9 (OS-9-1, OS-9-2) that are generated through alternative splicing of mRNA (2). The expression of both OS-9 isoforms is enhanced upon activation of the IRE1/XBP1 pathway in cells exposed to acute ER stress. It is postulated that OS-9 serves as a retention factor for glycosylated and nonglycosylated, misfolded proteins, preventing their progression through the secretory pathway (3,4). Furthermore, OS-9 promotes the removal of misfolded proteins from the ER lumen and their subsequent proteasome-dependent degradation via its association with the Hrd1-SEL1L ubiquitin ligase complex (5).

$364
100 µl
This Cell Signaling Technology (CST) antibody is conjugated to biotin under optimal conditions. The unconjugated Phospho-Stat3 (Tyr705) (D3A7) XP® Rabbit mAb #9145 reacts with human, mouse, rat and monkey phospho-Stat3 (Tyr705) protein. CST expects that Phospho-Stat3 (Tyr705) (D3A7) XP® Rabbit mAb (Biotinylated) will also recognize phospho-Stat3 (Tyr705) in these species.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

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).

$262
3 nmol
300 µl
SignalSilence® SQSTM1/p62 siRNA II from Cell Signaling Technology (CST) allows the researcher to specifically inhibit SQSTM1/p62 expression using RNA interference, a method whereby gene expression can be selectively silenced through the delivery of double stranded RNA molecules into the cell. All SignalSilence® siRNA products from CST are rigorously tested in-house and have been shown to reduce target protein expression by western analysis.
REACTIVITY
Human

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, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: LRP5 and LRP6 are single-pass transmembrane proteins belonging to the low-density lipoprotein receptor (LDLR)-related protein family. Unlike other members of the LDLR family, LRP5 and LRP6 have four EGF and three LDLR repeats in the extracellular domain, and proline-rich motifs in the cytoplasmic domain (1). They function as co-receptors for Wnt and are required for the canonical Wnt/β-catenin signaling pathway (2,3). LRP5 and LRP6 are highly homologous and have redundant roles during development (4,5). The activity of LRP5 and LRP6 can be inhibited by the binding of some members of the Dickkopf (DKK) family of proteins (6,7). Upon stimulation with Wnt, LRP6 is phosphorylated at multiple sites including Thr1479, Ser1490, and Thr1493 by kinases such as GSK-3 and CK1 (8-10). Phosphorylated LRP6 recruits axin to the membrane and presumably activates β-catenin signaling (8-10).