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Product listing: Cyclin B1 Antibody, UniProt ID P14635 #4138 to Dexras1 Antibody, UniProt ID Q9Y272 #4229

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Cyclins are a family of proteins that activate specific cyclin-dependent kinases required for progression through the cell cycle. The entry of all eukaryotic cells into mitosis is regulated by activation of cdc2/cdk1 at the G2/M transition. This activation is a multi-step process that begins with the binding of the regulatory subunit, cyclin B1, to cdc2/cdk1 to form the mitosis-promoting factor (MPF). MPF remains in the inactive state until phosphorylation of cdc2/cdk1 at Thr161 by cdk activating kinase (CAK) (1,2) and dephosphorylation of cdc2/cdk1 at Thr14/Tyr15 by cdc25C (3-5). Five cyclin B1 phosphorylation sites (Ser116, 126, 128, 133, and 147) are located in the cytoplasmic retention signal (CRS) domain and are thought to regulate the translocation of cyclin B1 to the nucleus at the G2/M checkpoint, promoting nuclear accumulation and initiation of mitosis (6-9). While MPF itself can phosphorylate Ser126 and Ser128, polo-like kinase 1 (PLK1) phosphorylates cyclin B1 preferentially at Ser133 and possibly at Ser147 (6,10). At the end of mitosis, cyclin B1 is targeted for degradation by the anaphase-promoting complex (APC), allowing for cell cycle progression (11). Research studies have shown that cyclin B1 is overexpressed in breast, prostate, and non-small cell lung cancers (12-14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Activity of the cyclin-dependent kinases CDK4 and CDK6 is regulated by T-loop phosphorylation, by the abundance of their cyclin partners (the D-type cyclins), and by association with CDK inhibitors of the Cip/Kip or INK family of proteins (1). The inactive ternary complex of cyclin D/CDK4 and p27 Kip1 requires extracellular mitogenic stimuli for the release and degradation of p27 concomitant with a rise in cyclin D levels to affect progression through the restriction point and Rb-dependent entry into S-phase (2). The active complex of cyclin D/CDK4 targets the retinoblastoma protein for phosphorylation, allowing the release of E2F transcription factors that activate G1/S-phase gene expression (3). Levels of cyclin D protein drop upon withdrawal of growth factors through downregulation of protein expression and phosphorylation-dependent degradation (4).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Cyclin E1 and cyclin E2 can associate with and activate CDK2 (1). Upon DNA damage, upregulation/activation of the CDK inhibitors p21 Waf1/Cip1 and p27 Kip1 prevent cyclin E/CDK2 activation, resulting in G1/S arrest. When conditions are favorable for cell cycle progression, cyclin D/CDK4/6 phosphorylates Rb and is thought to reduce the activity of p21 Waf1/Cip1 and p27 Kip1, allowing subsequent activation of cyclin E/CDK2 (1,2). Cyclin E/CDK2 further phosphorylates Rb to allow progression into S-phase, where cyclin E/CDK2 is thought to phosphorylate and activate multiple proteins involved in DNA synthesis (2,3). Turnover of cyclin E is largely controlled by phosphorylation that results in SCFFbw7-mediated ubiquitination and proteasome-dependent degradation (4,5). Cyclin E1 is phosphorylated at multiple sites in vivo including Thr62, Ser88, Ser72, Thr380 and Ser384, and is controlled by at least two kinases, CDK2 and GSK-3 (6,7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Cyclin H belongs to a conserved cyclin family that plays a critical role in the regulation of cell cycle dependent kinases (CDKs) necessary for cell cycle progression (1,2). In general, the activity of CDKs requires the binding of appropriate cyclins as well as phosphorylation driven by Cdk-activating kinase (CAK). Cyclin H is part of the CAK complex that includes the kinase CDK7, and an assembly factor p36/Mat1, which enhances binding between cyclin H and CDK7 and increases activity (3,4). CAK regulates progression through the cell cycle by activating cdc2, CDK2, and CDK4 kinases through phosphorylation of a critical threonine residue in the T-loop of the CDK-cyclin complexes (5,6). The CAK complex can exist either in its free form or in association with transcription factor IIH (TFIIH) which can affect its substrate specificity (7,8,9). When bound to TFIIH, CAK preferentially phosphorylates the carboxy-terminal domain of RNA polymerase II (9), providing a link between cell cycle control, transcriptional regulation, and DNA repair.

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

Application Methods: Western Blotting

Background: Cyclophilins are a highly conserved family of peptidylprolyl cis-trans-isomerases (PPIA) that are targets of the immunosuppressant drug cyclosporin A (CsA) (1,2). The complex of cyclophilin and CsA can bind to and inhibit calcineurin which leads to inhibition of the transcription factor NFAT and decreased production of cytokines (3,4). As isomerases, cyclophilins have been proposed to aid in protein folding. Cyclophilin A can bind to the p55 Gag protein of HIV and appears necessary for HIV infection (5,6). There is also some evidence that cyclophilins have nuclease activity and play a role in apoptosis (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Cytoplasmic FMR1-interacting protein 1 (CYFIP1) is a component of the CYFIP1/EIF4E/FMR1 complex which mediates translational repression by binding to the mRNA cap (1). CYFIP1 also plays a role in neuronal axonal growth dynamics by binging to the WAVE complex to regulate remodeling of actin filaments (2). Mutations in the gene encoding CYFIP1 has been linked to multiple neural development and psychiatric disorders, including autism spectrum disorder and schizophrenia (3-6). The specific mechanism by which CYFIP1, which is enriched in synapses, contributes to these neurological diseases is unknown, but may involve regulating the balance of synaptic excitation and inhibition to maintain neuronal circuit homeostasis during development and in mature brains (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: CYLD is a cytoplasmic deubiquitinating enzyme encoded by a tumor suppressor gene altered in individuals diagnosed with cylindromatosis, a genetic condition characterized by benign tumors of skin appendages (1,2). Functional CYLD deubiquitinase regulates inflammation and cell proliferation by down regulating NF-κB signaling through removal of ubiquitin chains from several NF-κB pathway proteins (3,4). CYLD is a negative regulator of proximal events in Wnt/β-catenin signaling and is a critical regulator of natural killer T cell development (5,6). The transcription factor Snail can inhibit CYLD expression, resulting in melanoma cell proliferation (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CYP17A1, also known as cytochrome P450C17, is a steroidogenic enzyme belonging to the P450 cytochrome superfamily of monooxygenases (1, 2). In humans, CYP17A1 expression is abundantly expressed in the adrenal cortex, where it plays a central role in the androgen synthesis pathway (2). CYP17A1 is the primary target of abiraterone, a synthetic steroid used in the treatment of castration-resistant prostate cancer (CRPC) (3, 4). Abiraterone is converted to the more active form D4A, which antagonizes androgen receptor signaling by inhibiting CYP17A1 and other steroidogenic enzymes (3, 4). This suppresses the synthesis of 5α-dihydrotestosterone (DHT), which is a driver of castration-resistant prostate cancer cell growth (3, 4).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Cytochrome c is a well conserved electron-transport protein and is part of the respiratory chain localized to mitochondrial intermembrane space (1). Upon apoptotic stimulation, cytochrome c released from mitochondria associates with procaspase-9 (47 kDa)/Apaf 1. This complex processes caspase-9 from inactive proenzyme to its active form (2). This event further triggers caspase-3 activation and eventually leads to apoptosis (3).

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

Application Methods: Western Blotting

Background: The common beta-chain (beta-c) of the granulocyte macrophage colony-stimulating factor (GM-CSF), interleukin-3 (IL-3) and IL-5 receptors is the major signaling subunit of these receptors, coupling ligand binding to multiple biological activities (1-3). Tyrosine phosphorylation of cytokine receptor common beta-chain is one of the first events in GM-CSF, IL-3 and IL-5 receptor activation and in signaling initiation (4). Serine phosphorylation within the 14-3-3 binding sequence of the common beta-chain is also involved in GM-CSF, IL-3 and IL-5 receptor-specific functions (5,6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The Reelin signaling pathway plays a critical role in neuronal development. Reelin is a secreted glycoprotein that binds to the lipoprotein receptors VLDLR and ApoER2 or alpha3beta1 integrin on the surface of neurons (1,2). Activation of these receptors induces tyrosine phosphorylation of Disabled 1 (Dab1), an intracellular adaptor. It is generally believed that tyrosine phosphorylation of Dab1 by Src family tyrosine kinases is the most critical downstream event in Reelin signaling. The phosphotyrosine-binding (PTB) domain within its amino terminus enables Dab1 to recognize and bind to a conserved sequence motif within the cytoplasmic tail of the receptors. In addition, the PTB contains a Pleckstrin Homology-like subdomain that binds to phosphoinositides. The phosphoinositide-binding region within the Dab1 PTB domain is required for membrane localization and basal tyrosine phosphorylation of Dab1 independent of VLDLR and ApoER2 (3). It has been demonstrated that Src, CrkII, CrkL and Dock1 associate with tyrosine-phosphorylated Dab. The CrkII-Dab1 interaction requires tyrosine phosphorylation of Dab1 at residues 220 or 232 (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Decay-accelerating factor (DAF/CD55) is a GPI-linked plasma membrane glycoprotein normally expressed on the surface of vascular endothelial and hematopoietic cells, which are continuously exposed to autologous complement components. In conjunction with other membrane complement regulatory proteins (CD35, CD46, and CD59), DAF/CD55 protects healthy cells from inappropriate complement-mediated lysis (1). DAF/CD55 inhibits activation of the complement cascade by promoting membrane dissociation and inactivation of C3 convertase, which inhibits amplification of the classical and alternative complement cascades (2). Research studies have demonstrated that DAF/CD55 is overexpressed in a variety of solid and liquid tumors, which functions to protect tumor cells from complement-mediated attack (3,4). Given its ability to disable the complement cascade and facilitate immune evasion by tumor cells, DAF/CD55 has received attention as a potential therapeutic target for the treatment of human malignancies. CD55 deficiency is also linked to human disease. The inability to express CD55 on the surface of erythrocytes renders them highly susceptible to complement-mediated lysis, which contributes to the development of paroxymal noctural hemoglobinuria (PNH). PNH is characterized by hemolytic anaemia, pancytopenia, and venous thrombosis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Death associated protein 1 (DAP1) is a 15 kDa protein that functions as a positive mediator of cell death initiated by interferon-gamma (1, 2). The DAP1 protein is proline rich and possesses one SH3 binding motif, as well as several consensus protein kinase phosphorylation sites (1). The protein is localized in the cytoplasm, but the detailed mechanism of its proapoptotic function is unclear. Death associated protein 3 (DAP3) is widely expressed, and the expression is upregulated during membrane receptor-mediated apoptosis. In interferon-gamma- and Fas-induced apoptosis, DAP3 acts as a positive mediator, functioning downstream of the receptor signaling complex and upstream of the effector caspases (3,4). Death associated protein 5 (DAP5) is a 97 kDa protein with a high degree of amino acid sequence homology to eukaryotic translation initiation factor 4G (Elf4G) (1,5). Compared with elF4G, DAP5 lacks the amino-terminal region necessary for cap-dependent translation, and has a unique carboxy-terminal region that functions as a regulator of interferon-gamma-induced cell death (5,6). During induction of apoptosis, DAP5 is cleaved at aspartic acid 790. The carboxy-terminal truncated form of DAP5 functions as a cap-independent translation initiation factor responsible for the mediation of its own translation during apoptosis (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Death-associated protein kinase (DAPK1) is a Ca2+/calmodulin-regulated serine/threonine kinase that participates in a wide range of apoptotic signals including interferon-γ, tumor necrosis factor α, Fas, activated c-Myc, and detachment from the extracellular matrix. In addition to the kinase domain and calmodulin regulatory segment, DAPK1 also has eight ankyrin repeats, a cytoskeleton binding region, and a conserved death domain (1-3). Deletion of the calmodulin-regulatory domain generates a constitutively active mutant kinase. Ectopic expression of wild-type DAPK1 induced cell death in HeLa cells. Conversely, expression of a catalytically inactive mutant protected cells from interferon-γ-induced cell death (4). The catalytic domain of DAPK1 has very high sequence similarity to vertebrate myosin light chain kinase (MLCK) and a RXX(S/T)X motif derived from myosin light chain protein was shown to be phosphorylated in vitro by DAPK1 (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Death-associated protein kinase (DAPK1) is a Ca2+/calmodulin-regulated serine/threonine kinase that participates in a wide range of apoptotic signals including interferon-γ, tumor necrosis factor α, Fas, activated c-Myc, and detachment from the extracellular matrix. In addition to the kinase domain and calmodulin regulatory segment, DAPK1 also has eight ankyrin repeats, a cytoskeleton binding region, and a conserved death domain (1-3). Deletion of the calmodulin-regulatory domain generates a constitutively active mutant kinase. Ectopic expression of wild-type DAPK1 induced cell death in HeLa cells. Conversely, expression of a catalytically inactive mutant protected cells from interferon-γ-induced cell death (4). The catalytic domain of DAPK1 has very high sequence similarity to vertebrate myosin light chain kinase (MLCK) and a RXX(S/T)X motif derived from myosin light chain protein was shown to be phosphorylated in vitro by DAPK1 (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: DARPP-32 (dopamine and cyclic AMP-regulated phosphoprotein, relative molecular mass 32,000) is a cytosolic protein highly enriched in medium-sized spiny neurons of the neostriatum (1). It is a bifunctional signaling molecule that controls serine/threonine kinase and serine/threonine phosphatase activity (2). Dopamine stimulates phosphorylation of DARPP-32 through D1 receptors and activation of PKA. PKA phosphorylation of DARPP-32 at Thr34 converts it into an inhibitor of protein phosphatase 1 (1). DARPP-32 is converted into an inhibitor of PKA when phosphorylated at Thr75 by cyclin-dependent kinase 5 (CDK5) (2). Mice containing a targeted deletion of the DARPP-32 gene exhibit an altered biochemical, electrophysiological, and behavioral phenotype (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The human Deleted in AZoospermia (DAZ) genes encode a family of RNA-binding proteins that are expressed exclusively in the germ cells and play a role in the regulation of mRNA translation (1). Members of the family include DAZ, DAZL, and BOULE. The essential role of DAZL and BOULE in spermatogenesis has been established (2-4), but the role of DAZ remains unclear. Men with deletions in the DAZ1 gene can produce sperm, although in lower numbers, and are capable of reproduction and transmission of the genetic lesions (5-7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: The human DAZ (Deleted in Azoospermia) gene family contains at least three members that encode RNA-binding proteins with a common RNA-recognition motif (1). An autosomal homolog of DAZ, DAZL (DAZ-like), is specifically expressed in germ cells and is essential for the specification of the germ cell lineage during embryogenesis and during gametogenesis in adults of both sexes (2,3). DAZL may function by directly recruiting poly(A)-binding proteins (PABPs) in order to activate silent mRNAs during germ cell development (2). Deletions encompassing the Y chromosomal DAZ genes are the most common molecularly defined cause of infertility in humans (4,5).

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

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

Background: Deleted in breast cancer gene 1 protein (DBC1) was originally identified by its localization to a region of chromosome 8p21 that is homozygously deleted in breast cancer (1). DBC1 is a large, nuclear protein with multiple functions in cell survival. It binds directly to the estrogen receptor α (ERα) hormone-binding domain in a ligand-independent manner and may be a key determinant of ligand-independent ERα expression and survival in human breast cancer cells (2). DBC1 can promote p53-mediated apoptosis by binding to and inhibiting the deacetylase activity of SirT1, resulting in increased p53 acetylation levels and activity (3). DBC1 may be an important regulator of heterochromatin formation as it binds SUV39H1 and inhibits its histone methyltransferase activity (4). Caspase-dependent processing activates the pro-apoptotic activity of DBC1 during Tumor Necrosis Factor-α (TNF-α)-mediated cell death signaling (5). This processing of DBC1 in response to TNF-α is an early event in the onset of apoptosis and results in relocalization of DBC1 to the cytoplasm. Overexpression of the processed, cytoplasmic form of DBC1 results in mitochondrial clustering and matrix condensation and sensitizes cells to TNF-α-mediated apoptosis.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: DCBLD2 (discoidin, CUB and LCCL domain-containing 2; also known as ESDN and CLCP1) is a type I transmembrane protein that is structurally similar to neuropilin family proteins and contains the longest known amino-terminal secretory signal sequence among eukaryotic proteins (1). Highly expressed in nerve bundles, vascular smooth muscle cells and upregulated following vascular injury, DCBLD2 may be involved in a wide range of functions in the nervous and vascular systems (1,2). Studies have found DCBLD2 to be upregulated in several types of lung cancer with an especially high frequency in metastatic lesions and lymph node metastasis, implicating a role in the process of tumor progression and metastatic capability (3). DCBLD2 has also been identified as part of a complex EGF phosphotyrosine signaling network, serving as a novel tyrosine phosphorylation target of EGF signaling in human cancer cells (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The tumor necrosis factor receptor family, which includes TNF-RI, Fas, DR3, DR4, DR5, and DR6, plays an important role in the regulation of apoptosis in various physiological systems (1,2). The receptors are activated by a family of cytokines that include TNF, FasL, and TRAIL. They are characterized by a highly conserved extracellular region containing cysteine-rich repeats and a conserved intracellular region of about 80 amino acids termed the death domain (DD). The DD is important for transducing the death signal by recruiting other DD containing adaptor proteins (FADD, TRADD, RIP) to the death-inducing signaling complex (DISC), resulting in activation of caspases.

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Western Blotting

Background: The tumor necrosis factor receptor family, which includes TNF-RI, Fas, DR3, DR4, DR5, and DR6, plays an important role in the regulation of apoptosis in various physiological systems (1,2). The receptors are activated by a family of cytokines that include TNF, FasL, and TRAIL. They are characterized by a highly conserved extracellular region containing cysteine-rich repeats and a conserved intracellular region of about 80 amino acids termed the death domain (DD). The DD is important for transducing the death signal by recruiting other DD containing adaptor proteins (FADD, TRADD, RIP) to the death-inducing signaling complex (DISC), resulting in activation of caspases.

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

Application Methods: Western Blotting

Background: Damaged DNA-Binding Protein (DDB) consists of a 127 kDa subunit (DDB-1) and a 48 kDa subunit (DDB-2) that contribute to the formation of the UV-damaged DNA-binding protein complex (UV-DDB) (1-3). In conjunction with CUL4A and ROC-1, the UV-DDB complex forms an E3 ubiquitin ligase that recognizes a broad spectrum of DNA lesions such as cyclobutane pyrimidine dimers, 6-4 photoproducts, apurinic sites and short mismatches. The complex polyubiquitinates components of the nucleotide excision repair pathway (4-6). Loss of DDB activity has been identified in a subset of xeroderma pigmentosum complementation group E (XP-E) patients and has been linked to the deficient repair of cyclobutane pyrimidine dimers in cells derived from these patients (7-10).

$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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Rat

Application Methods: Immunoprecipitation, 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).

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

Application Methods: Western Blotting

Background: The DEAD box family of RNA helicases is characterized in part by a common D-E-A-D amino acid motif. The family is composed of a growing number of proteins found in a wide range of organisms from bacteria to mammals. DEAD helicases have distinct biological functions in RNA metabolism and ribonucleoprotein (RNP) processing (reviewed in 1,2).DDX3 is a DEAD box family RNA helicase with diverse cellular functions. DDX3 is required for nuclear export of HIV-1 viral transcripts, possibly in a complex with the viral Rev protein and host cofactor CRM1 (3). DDX3 is required for hepatitis C virus (HCV) RNA replication (4) and its expression is downregulated in hepatitis B virus (HBV) associated hepatocellular carcinoma (HCC) (5).Recent evidence suggests that DDX3 functions as a tumor suppressor protein. Its expression inhibits tumor cell colony formation and increases expression of the cdk inhibitor p21 Waf1/Cip1. Low DDX3 expression has been shown in HCC (5,6), and aberrant subcellular localization occurs in many squamous cell carcinomas (6). Reduced DDX3 expression in cultured cells causes a diminished dependence on serum for cell proliferation and changes in cyclin D1 and p21 Waf1/Cip1 expression (5).DDX3 is phosphorylated at Thr204 and Thr323 by the mitotic cyclin dependent kinase, cyclin B/cdc2. This phosphorylation is thought to cause a loss of DDX3 function and a concomitant repression of ribosome biogenesis and translation in mitosis (7).

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

Application Methods: Western Blotting

Background: DDX5 (DEAD box polypeptide 5), also known as p68, was first identified as a 68 kDa nuclear protein with similarity to translation initiation factor eIF-4A (1). DDX5 is a member of the DEAD box family of putative RNA helicases, defined by the presence of a conserved DEAD (Asp-Glu-Ala-Asp) motif that appears to function primarily in the regulation of RNA secondary structure. DDX5 exhibits ATP-dependent RNA helicase activity (2) and has been identified as a critical subunit of the DROSHA complex that regulates miRNA and rRNA processing (3,4). DDX may also regulate mRNA splicing (5) and has been shown to interact with HDAC1, where it can regulate promoter-specific transcription (6). DDX5 interacts with a diverse group of proteins, including Runx2, p53, Smad3, CBP, and p300 (7-10), suggesting an important role for DDX5 in a multitude of developmental processes. Notably, DDX5 may be involved in growth factor-induced epithelial mesechymal transition (EMT). Phosphorylation of DDX5 at Tyr593 following PDGF stimulation was shown to displace Axin from β-catenin; this prevented phosphorylation of β-catenin by GSK-3β, leading to Wnt-independent nuclear translocation of β-catenin (11) and increased transcription of c-Myc, cyclin D1, and Snai1 (12,13).

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

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

Background: DDX6, also known as RCK and p54, was identified as a proto-oncogene product and is a member of the ATP-dependent DEAD box helicase family (1,2). This protein interacts with translation initiation factor eIF4E in the cytoplasmic P-bodies (3) and represses mRNA translation (4). DDX6 is a component of the miRNA induced silencing complex (miRISC) and interacts with Argonaute 1 (Ago1) and Argonaute 2 (Ago2) proteins in vitro and in vivo (5), functioning in miRNA-mediated translational repression (5). Depletion of DDX6 leads to the disruption of cytoplasmic P-bodies indicating that it is required for P-body formation (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Western Blotting

Background: The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments and microtubules. Major types of intermediate filaments are distinguished and expressed in particular cell types: cytokeratins (epithelial cells), glial fibrillary acidic protein or GFAP (glial cells), desmin (skeletal, visceral and certain vascular smooth muscle cells), vimentin (mesenchyme origin) and neurofilaments (neurons). GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). Vimentin is present in sarcomas, but not carcinomas, and its expression is examined relative to other markers to distinguish between the two forms of neoplasm (3). Desmin is a myogenic marker expressed in early development that forms a network of filaments that extends across the myofibril and surrounds Z discs. The desmin cytoskeleton provides a connection among myofibrils, organelles and the cytoskeleton (4). Desmin knockout mice develop cardiomyopathy, skeletal and smooth muscle defects (5). In humans, desmin related myopathies might be caused by mutations in the corresponding desmin gene or in proteins with which desmin interacts, including αB-crystallin and synemin. Disorganized desmin filaments and the accumulation of protein aggregates comprised predominantly of desmin characterize desmin-related myopathies (reviewed in 6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Dexras1 (Ras dexamethasone induced 1) belongs to the Ras superfamily of GTPases and was initially identified as a dexamethasone inducible gene (1,2). Dexras1 reportedly regulates several distinct signal transduction pathways, including MAPK signaling, NMDA receptor-nitric oxide-mediated signaling, and pathways involving adenylyl cyclases (3-5). Dexras1 can directly modulate FE65-APP-mediated transcription and regulate the photic sensitivity of the mammalian circadian clock (6,7).