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Product listing: ERC1 (P85) Antibody, UniProt ID Q8IUD2 #2884 to VANGL1 (D1J7X) Rabbit mAb, UniProt ID Q8TAA9 #14783

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: ERC1, an acronym named for previous protein names ELKS (1), RAB6IP2 (2) and CAST (3), is a RIM-binding protein that plays a role in neurotransmitter release and general membrane trafficking in other cell types (2-5). Interaction with the GTP-binding protein Rab6 suggests that it contributes to membrane traffic at the Golgi (2). In addition to its association with membrane trafficking, ERC1 has also been found as an essential part of the IκB kinase (IKK) complex required for the activation of NF-κB, perhaps by recruiting IκBα to the IKK complex (6). Alternative splicing of ERC1 generates 2 proteins with a divergent carboxy terminus, a long and a short form termed ERC1α and ERC1β, respectively. ERC1α is widely expressed, whereas ERC1β and a related family member ERC2 are expressed in the brain (4). Papillary thyroid carcinomas have been identified with the translocation t(10;12)(p11;p13) resulting in a fusion between ERC1 and the receptor tyrosine kinase Ret (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Fes/Fps and Fer are the only two members of a unique family of cytoplasmic protein tyrosine kinases (1,2). Fes and Fer contain a central Src homology-2 (SH2) domain and a carboxy-terminal tyrosine kinase catalytic domain. They are structurally distinguished from other members of cytoplasmic protein tyrosine kinase subfamilies by the presence of amino-terminal Fer/CIP4 homology and coiled-coil domains (3). Fes/Fps was originally identified as an oncogene from avian (Fps) and feline (Fes) retroviruses. Human c-Fes has been implicated in myeloid, vascular endothelial and neuronal cell differentiation. Mutations may activate the Fps kinase and thereby contribute to cancer (4). However, recent data strongly suggests that the c-Fes protein-tyrosine kinase is a tumor suppressor rather than a dominant oncogene in colorectal cancer (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Class 3 secreted semaphorin (Sema3A) is a chemorepellent that acts upon a wide variety of axons. As such, it induces a dramatic redistribution and depolymerization of actin filaments that results in growth cone collapse. Plexins are single membrane-spanning signaling proteins encompassing Plexin A1, A2, A3, and A4. Plexins form a complex with neuropilin-1 and -2 and the cell adhesion protein L1 to form a functional semaphorin receptor (1,2). The GTPase Rnd1 binds to the cytoplasmic domain of Plexin A1 to trigger cytoskeletal collapse. In contrast, the GTPase RhoD blocks Rnd1-mediated Plexin A1 activation and repulsion of sympathetic axons by Sema3A (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Spastic paraplegia 20 (spartin) is encoded by the SPG20 gene in humans, which is altered in some individuals with an autosomal recessive form of hereditary spastic paraplegia known as Troyer syndrome (1,2). While Troyer syndrome research studies have yet to clearly describe the subcellular localization or function of spartin, additional work implicates spartin in endosomal trafficking, microtubule dynamics, and lipid homoeostasis (3-5). This multifunctional protein is ubiquitously expressed within the nervous system and in non-neuronal tissues, and displays a diverse pattern of cellular localization (6). The SPG20 gene promoter is hypermethylated in many cases of colorectal cancer, which results in decreased spartin expression and cytokinesis arrest. This suggests that spartin expression and methylation state could be a promising biomarker for colorectal tumors (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Chimerins are a family of GTPase-activating proteins (GAPS) that facilitate GTP hydrolysis by the small GTPase Rac, rendering it inactive and regulating cell shape, spreading and motility. Regulation of chimerin proteins occurs in response to growth factor receptor or G-protein coupled receptor activation followed by phospholipase C activation. Chimerins are among the growing number of phorbol ester and diacylglycerol (DAG) effector molecules that do not belong to the PKC family of isoenzymes (reviewed in 1,2). β2-chimerin is highly expressed in brain and pancreas, and its expression is down-regulated in malignant gliomas (3). β2-chimerin is also down-regulated in breast cancer, and its expression causes GAP activity-dependent cell cycle arrest in MCF-7 breast cancer cells (4). Signaling from the epidermal growth factor receptor (EGFR) activates β2-chimerin and allows its association with Rac1 at the plasma membrane (5). Also in response to EGF, diacylglycerol kinase (DGK) γ interacts with β2-chimerin, promotes its translocation to the plasma membrane, and regulate its GAP activity (6).

$262
3 nmol
300 µl
SignalSilence® hnRNP A1 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit hnRNP A1 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: Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is a member of the hnRNP A/B family of related RNA binding proteins that bind pre-mRNA and are involved in the processing, metabolism, and transport of nuclear pre-mRNA transcripts (1). hnRNP A1 regulates the alternative splicing of c-Src and c-H-Ras (2,3) and modifies initiation of translation of the fibroblast growth factor 2 mRNA (4). hnRNP A1 expression level is elevated in many cancers; knockdown of hnRNP A1 leads to apoptosis in various cancer cells (5). Although predominantly nuclear, hnRNP A1 is continually transported from the nucleus to the cytoplasm where it disassociates from mRNA and is rapidly re-imported into the nucleus (6,7). hnRNP A1 binds to cis-acting repressive sequences (CRS) of HIV-1 to influence HIV-1 production (8,9). HIV-1 enhances hnRNP A1 expression and promotes the relocalization of hnRNP A1 to the cytoplasm (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Human progesterone receptor (PR) is expressed as two forms: the full length PR-B and the short form PR-A. PR-A lacks the first 164 amino acid residues of PR-B (1,2). Both PR-A and PR-B are ligand activated, but differ in their relative ability to activate target gene transcription (3,4). The activity of PR is regulated by phosphorylation; at least seven serine residues are phosphorylated in its amino-terminal domain. Three sites (Ser81, Ser102, and Ser162) are unique to full length PR-B, while other sites (Ser190, Ser294, Ser345, and Ser400) are shared by both isoforms (5). Phosphorylation of PR-B at Ser190 (equivalent to Ser26 of PR-A) is catalyzed by CDK2 (6). Mutation of Ser190 results in decreased activity of PR (7), suggesting that the phosphorylation at Ser190 may be critical to its biological function.

$364
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 Phospho-GSK-3β (Ser9) (D85E12) XP® Rabbit mAb #5558.
APPLICATIONS
REACTIVITY
Hamster, Human, Mouse, Rat

Application Methods: Flow Cytometry

Background: Glycogen synthase kinase-3 (GSK-3) was initially identified as an enzyme that regulates glycogen synthesis in response to insulin (1). GSK-3 is a ubiquitously expressed serine/threonine protein kinase that phosphorylates and inactivates glycogen synthase. GSK-3 is a critical downstream element of the PI3K/Akt cell survival pathway whose activity can be inhibited by Akt-mediated phosphorylation at Ser21 of GSK-3α and Ser9 of GSK-3β (2,3). GSK-3 has been implicated in the regulation of cell fate in Dictyostelium and is a component of the Wnt signaling pathway required for Drosophila, Xenopus, and mammalian development (4). GSK-3 has been shown to regulate cyclin D1 proteolysis and subcellular localization (5).

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

Application Methods: Western Blotting

Background: The 20S proteasome is the major proteolytic enzyme complex involved in intracellular protein degradation. PA700, PA28, and PA200 are three major protein complexes that function as activators of the 20S proteasome. There are three evolutionarily conserved subunits of PA28: PA28α (PSME1), PA28β (PSME2), and PA28γ (PSME3) (1,2). PA28α and PA28β form a heteroheptameric complex and function by binding to the 20S complex at its opening site(s). The PA28α/β complex is present throughout the cell and participates in MHC class I antigen presentation by promoting the generation of antigenic peptides from foreign proteins (2). PA28γ exists in the form of a homoheptamer and is mainly located in the nucleus. The PA28γ complex exerts its function by binding and guiding specific nuclear target proteins to the 20S proteasome for further degradation (3,4).

Jurkat cells are treated with 100 nM calyculin A and 1 mM pervanadate to inhibit multiple serine/threonine and tyrosine phosphatases, respectively and upregulate protein phosphorylation. Treated Jurkat cells were lysed in 1X cell lysis buffer and lysates were lyophilized.
$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: Sarcoplasmic and endoplasmic reticulum Ca2+ ATPases (SERCA) are members of a highly conserved family of Ca2+ pumps (1). SERCA pumps transport Ca2+ from the cytosol to the sarcoplasmic and endoplasmic reticulum lumen against a large concentration gradient (1). ATP2A1 (SERCA1) is a fast-twitch, skeletal muscle sarcoplasmic reticulum Ca2+ ATPase (2). Research studies have shown that mutations in the ATP2A1 gene cause an autosomal recessive muscle disorder known as Brody myopathy, which is characterized by muscle cramping and impaired muscle relaxation associated with exercise (1-3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Secretory proteins translocate into the endoplasmic reticulum (ER) after their synthesis where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Disulfide isomerase (PDI) has two thioredoxin homology domains and catalyzes the formation and isomerization of these disulfide bonds (2). Other ER resident proteins that possess the thioredoxin homology domains, including endoplasmic reticulum stress protein 57 (ERp57), constitute the PDI family (2). ERp57 interacts with calnexin and calreticulin (3) and is suggested to play a role in the isomerization of disulfide bonds on certain glycoproteins (3).

$262
3 nmol
300 µl
SignalSilence® p16 INK4A siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit p16 INK4A 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: Cyclin-dependent kinases (CDKs) are activated in part by forming complexes with cyclins. For example, CDK4 and CDK6 associate with the D-type cyclins and phosphorylate the retinoblastoma protein. This phosphorylation is a necessary event for cells to enter S-phase (1). The inhibitors of CDK4 (INK4) family include p15 INK4B, p16 INK4A, p18 INK4C and p19 INK4D. p18 has been shown to function as a haploinsufficient tumor suppressor in vivo (2). All INK4 proteins are composed of 32 amino acid ankyrin motifs and selectively inhibit CDK4/6 activity. Mutational analyses of p18 implicate the third and the amino-terminal portion of the fourth ankyrin repeat in mediating binding to CDK4/6 (3). The interaction of INK4 family members can be a binary complex with CDK4/6 or ternary complex with cyclin D-bound CDK4/6 and ultimately results in the inhibition of cell cycle progression (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: LASP1 is a cytoskeletal scaffold protein belonging to the LIM protein subfamily (1,2). LASP1 consists of an N-terminal LIM domain, followed by two nebulin repeats, and a C-terminal SH3 domain (1,3). The nebulin repeats interact with actin, while the SH3 domain interacts with palladin (4,5), suggesting LASP1 functions as an actin-binding protein, possibly in cytoskeletal organization. LASP1 has been shown to localize to focal adhesions, lamellipodia, and membrane ruffles (6-8) and might be involved in membrane migration. Overexpression of LASP1 has been associated with metastatic cancers, such as breast and ovarian cancer (2). In these cases, membrane, cytoplasmic, and nuclear localization of LASP1 in the tumor cell has been reported, suggesting LASP1 involvement in membrane and nuclear signaling (9,10).

$114
10 blots
Nonphosphorylated Rb-C Fusion Protein (5 µg/ml): Rb-C is expressed as a recombinant fusion protein of Rb residues 701–928 and maltose binding protein serves as a negative control. Supplied in SDS Sample Buffer.Phosphorylated Rb-C Fusion Protein (5 µg/ml): Rb-C is expressed as a recombinant fusion protein of Rb residues 701–928 and maltose binding protein prepared by in vitro kinase reaction with cdc2 serves as a positive control. Supplied in SDS Sample Buffer.Note: This truncated Rb recombinant protein is not recognized by Phospho-Rb (Ser608) Antibody #2181 or Rb (D20) Rabbit mAb #9313.
APPLICATIONS

Application Methods: Western Blotting

Background: The retinoblastoma tumor suppressor protein Rb regulates cell proliferation by controlling progression through the restriction point within the G1-phase of the cell cycle (1). Rb has three functionally distinct binding domains and interacts with critical regulatory proteins including the E2F family of transcription factors, c-Abl tyrosine kinase, and proteins with a conserved LXCXE motif (2-4). Cell cycle-dependent phosphorylation by a CDK inhibits Rb target binding and allows cell cycle progression (5). Rb inactivation and subsequent cell cycle progression likely requires an initial phosphorylation by cyclin D-CDK4/6 followed by cyclin E-CDK2 phosphorylation (6). Specificity of different CDK/cyclin complexes has been observed in vitro (6-8) and cyclin D1 is required for Ser780 phosphorylation in vivo (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TCL1 (T cell leukemia 1), MTCP1 and TCL1b belong to the TCL1 proto-oncogene family, and their products are involved in Akt activation during embryonic development, T cell leukemias, prolymphocytic leukemias and B cell lymphomas (1-3). The Akt association domain of TCL1 binds with the PH domain of Akt. The formation of an oligomeric TCL-Akt complex is required for TCL1 coactivator function and results in phosphorylation and activation of Akt . Furthermore, functional analysis indicates that the interaction between TCL1 and Akt promotes translocation of Akt to the nucleus (4-6). These findings are supported by the crystal structure of TCL1, which suggests that TCL1 may participate in molecular transport (7).

$260
100 µl
APPLICATIONS

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

Background: CRISPR-Cas (clustered regularly interspaced short palindromic repeats and CRISPR-associated proteins) are RNA-guided nuclease effectors that are utilized for precise genome editing in mammalian systems (1). Cpf1 (CRISPR from Prevotella and Francisella) are members of the Class 2 CRISPR system (2). Class 2 CRISPR systems, such as the well characterized Cas9, rely on single-component effector proteins to mediate DNA interference (3). Cpf1 endonucleases, compared to Cas9 systems, have several unique features that increase the utility of CRISPR-based genome editing techniques: 1) Cpf1-mediated cleavage relies on a single and short CRISPR RNA (crRNA) without the requirement of a trans-activating crRNA (tracrRNA), 2) Cpf1 utilizes T-Rich protospacer adjacent motif (PAM) sequences rather than a G-Rich PAM, and 3) Cpf1 generates a staggered, rather than a blunt-ended, DNA double-stranded break (2). These features broaden the utility of using CRISPR-Cas systems for specific gene regulation and therapeutic applications. Several Cpf1 bacterial orthologs have been characterized for CRISPR-mediated mammalian genome editing (2, 4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Frizzled (Fzd) belongs to the seven transmembrane-spanning G-protein-coupled receptor (GPCR) superfamily (1). Fzds have a large extracellular N-terminal region containing a cysteine-rich domain (CRD), which is involved in binding to Wnt proteins (1,2). The intracellular C-terminus binds to the PDZ domain of Dvl proteins, a major signaling component downstream of Fzd (3). Wnt proteins bind to Fzd and the co-receptors LRP5 or LPR6, and activate Wnt/β-catenin pathway through inhibiting phosphorylation of β-catenin by GSK3-β (4,5). In addition to this canonical Wnt/β-catenin pathway, some Wnt proteins can also activate the Fzd/Ca2+ pathway and Fzd/PCP (planar cell polarity) pathway (6,7). The mammalian Fzd subfamily has 10 members (Fzd1 to Fzd10) and they may mediate signaling through different pathways (8). Some Fzds can also bind to other secreted proteins, like Norrin and R-Spondin (9-11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Patched1 and 2 (PTCH1 and PTCH2) are twelve-pass transmembrane proteins that function as the receiving receptors for members of the Hedgehog family of proteins (1-4). In the absence of Hedgehog proteins, PTCH suppresses the otherwise constitutively active signaling receptor Smoothened (Smo) so that the Hedgehog signaling pathway is in the off state (5,6). Deactivating mutations that impair the ability of PTCH1 to suppress Smo are frequently found in patients with nevoid basal cell carcinoma syndrome (7,8). PTCH proteins have a sterol-sensing domain (SSD) also found in several proteins that function in cholesterol homeostasis, such as HMGCR (3-hydroxy-3-methylglutaryl coenzyme A-reductase) and SCAP (sterol regulatory element-binding protein-cleavage activating protein). However, the role of the SSD in Patched proteins is not clear (9,10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Cell growth is a fundamental biological process whereby cells accumulate mass and increase in size. The mammalian Target of Rapamycin (mTOR) pathway regulates growth by coordinating energy and nutrient signals with growth factor-derived signals (1). mTOR is a large protein kinase with two different complexes. One complex contains mTOR, GβL, and raptor, which is a target of rapamycin. The other complex, insensitive to rapamycin, includes mTOR, GβL, and rictor (1). GβL associates with the kinase domain of mTOR and stimulates mTOR kinase activity (2). A reduction in GβL expression has been shown to decrease in vivo phosphorylation of S6K1 (2).

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

Application Methods: Immunoprecipitation, 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).

$132
100 µl
This Cell Signaling Technology antibody was conjugated to Alexa Fluor® 700 fluorescent dye and tested in-house for direct flow cytometric analysis of human cells.
APPLICATIONS

Application Methods: Flow Cytometry

Background: Isotype control antibodies are used to estimate the nonspecific binding of target primary antibodies due to Fc receptor binding or other protein-protein interactions. An isotype control antibody should have the same immunoglobulin type and be used at the same concentration as the test antibody.

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: In response to genomic stress, the ATR interacting protein (ATRIP) binds and is phosphorylated by the DNA damage-and checkpoint-activated kinase ATR (ataxia-telangiectasia mutated and rad3-related). Both ATR and ATRIP are integral for checkpoint signaling and are critical in the DNA repair response (1-3). Direct interaction between ATRIP and replication protein A (RPA) at RPA-coated, single-stranded DNA results in the recruitment of phosphorylated ATR/ATRIP to stalled replication forks and sites of DNA damage (3). ATR/ATRIP coordinate DNA repair and cell cycle progression in conjunction with key regulatory proteins, such as Rad17 and the 9-1-1 complex (4). ATR associated with ATRIP can also be stimulated by topoisomerase II binding protein (TOPBP1), suggesting that ATRIP may regulate both ATR localization and activity (5).

$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-EGF Receptor (Tyr1068) (D7A5) XP® Rabbit mAb #3777.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: The epidermal growth factor (EGF) receptor is a transmembrane tyrosine kinase that belongs to the HER/ErbB protein family. Ligand binding results in receptor dimerization, autophosphorylation, activation of downstream signaling, internalization, and lysosomal degradation (1,2). Phosphorylation of EGF receptor (EGFR) at Tyr845 in the kinase domain is implicated in stabilizing the activation loop, maintaining the active state enzyme, and providing a binding surface for substrate proteins (3,4). c-Src is involved in phosphorylation of EGFR at Tyr845 (5). The SH2 domain of PLCγ binds at phospho-Tyr992, resulting in activation of PLCγ-mediated downstream signaling (6). Phosphorylation of EGFR at Tyr1045 creates a major docking site for the adaptor protein c-Cbl, leading to receptor ubiquitination and degradation following EGFR activation (7,8). The GRB2 adaptor protein binds activated EGFR at phospho-Tyr1068 (9). A pair of phosphorylated EGFR residues (Tyr1148 and Tyr1173) provide a docking site for the Shc scaffold protein, with both sites involved in MAP kinase signaling activation (2). Phosphorylation of EGFR at specific serine and threonine residues attenuates EGFR kinase activity. EGFR carboxy-terminal residues Ser1046 and Ser1047 are phosphorylated by CaM kinase II; mutation of either of these serines results in upregulated EGFR tyrosine autophosphorylation (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Leupaxin is a member of the paxillin family of scaffold proteins whose functions include regulation of cell adhesion, migration and metastasis (1). Leupaxin suppresses integrin-dependent tyrosine phosphorylation of paxillin and affects the regulation of cell-matrix adhesion (2). Researchers have implicated leupaxin in the progression of human hepatocellular carcinoma through its regulation of beta-catenin-mediated transcription (3). Researchers have also shown that leupaxin regulates actin dynamics and migration of prostate cancer cells through its interaction with caldesmon (4) and down-regulation of p120-catenin (5). Studies in breast cancer implicate leupaxin in the regulation of ER-alpha transcription and invasiveness (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: MATK/CHK (CTK, NTK and HYL) is a non-receptor tyrosine kinase structually and functionally homologous to Csk kinase. The kinase was identified through molecular cloning from multiple tissues by different research groups. Like Csk, MATK/CHK has a N-terminal SH3 domain, followed by an SH2 domain and a C-terminal catalytic kinase domain (1-4). MATK/CHK inhibits Src family members in several different ways. First, it directly phosphorylates the inhibitory C-terminal tyrosine of Src (as well as other Src family members). This induces a Src protein conformational change from the active to inactive state (2,4). Second, it binds directly to activated Src and induces a conformational change to the inactive state (5,6). The SH2 domain of MATK/CHK directly interacts with the phosphorylated tyrosine of activated receptor tyrosine kinases, such as ErbB-2 and c-Kit, to inhibit receptor function (7-9). MATK/CHK negatively regulates tumor cell growth, migration and invasion (10-13). Decreased expression of the protein has been correlated with brain tumors as well as colon cancers in research studies (14-15).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: YAP (Yes-associated protein, YAP65) was identified based on its ability to associate with the SH3 domain of Yes. It also binds to other SH3 domain-containing proteins such as Nck, Crk, Src, and Abl (1). In addition to the SH3 binding motif, YAP contains a PDZ interaction motif, a coiled-coil domain, and WW domains (2-4). While initial studies of YAP all pointed towards a role in anchoring and targeting to specific subcellular compartments, subsequent studies showed that YAP is a transcriptional co-activator by virtue of its WW domain interacting with the PY motif (PPxY) of the transcription factor PEBP2 and other transcription factors (5). In its capacity as a transcriptional co-activator, YAP is now widely recognized as a central mediator of the Hippo Pathway, which plays a fundamental and widely conserved role in regulating tissue growth and organ size. Phosphorylation at multiple sites (e.g., Ser109, Ser127) by LATS kinases promotes YAP translocation from the nucleus to the cytoplasm, where it is sequestered through association with 14-3-3 proteins (6-8). These LATS-driven phosphorylation events serve to prime YAP for subsequent phosphorylation by CK1δ/ε in an adjacent phosphodegron, triggering proteosomal degradation of YAP (9).

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

Application Methods: Western Blotting

Background: The E3 ubiquitin-protein ligase ARIH2 (TRIAD1) is an Ariadne subfamily ligase involved in the polyubiquitination of proteins designated for proteasomal degradation. The TRIAD1 nuclear protein contains an amino-terminal acidic region, a pair of RING fingers, two carboxyl-terminal coiled coil domains and a novel C6HC DRIL/IBR domain located between the RING fingers. Together, the paired RING fingers and DRIL/IBR domain form a highly conserved TRIAD (two RING fingers and DRIL) domain (1). Research studies suggest that TRIAD1 mediates both Lys48 and Lys63 protein polyubiquitination and acts as a negative regulator of myelopoiesis. TRIAD1 ubiquitin ligase inhibits myeloid cell proliferation by mediating protein ubiquitination through the ubiquitin-conjugating enzymes UbcH7 and UbcH13 (2,3). Experimental deletion of TRIAD1 in mice has a lethal effect, leading to death at the embryonic stage or later due to a severe, multi-organ inflammatory response. Results indicate that TRIAD1 binds IκBβ in dendritic cells and promotes the degradation of the NF-κB inhibitor (4).

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

Application Methods: Western Blotting

Background: Van Gogh-like proteins (VANGL1, VANGL2) are human orthologs of Drosophila Van Gogh (Vang/Stbm), a multi-pass transmembrane protein that is required to establish cell polarity in embryonic eyes, legs, and bristles (1,2). As in Drosophila, mammalian VANGL proteins are core components of the planar cell polarity (PCP) pathway that promotes asymmetric orientation of cells across a planar surface, and drives convergence-extension movements that are critical for tissue morphogenesis (3). Mutations in the human VANGL1 gene have been identified in patients diagnosed with neural tube defects (e.g., spina bifida), providing evidence that VANGL1 plays a role in human embryonic morphogenesis (4,5). These findings are supported by genetic studies in mice, where mutations in both Vangl1 and Vangl2 result in neural tube defects (6,7). A possible role for VANGL in tumor progression is suggested by an increased expression of VANGL1 mRNA in breast cancer patients with an elevated risk of relapse (8).