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Product listing: AsCpf1 (Strain BV3L6) (E1U7C) Rabbit mAb #19984 to Perilipin-1 (K117) Antibody, UniProt ID O60240 #3467

$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).

$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).

$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).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: WIF1 (Wnt inhibitory factor 1) is a secreted protein that binds to Wnt proteins and inhibits their activity (1). It contains an N-terminal WIF domain and five EGF-like repeats (2). The WIF1 ortholog in Drosophila, Shifted, is required for Hedgehog stability and diffusion (3,4). It has been reported that WIF1 expression is downregulated in many types of cancers (5-8).

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

Application Methods: Western Blotting

Background: DNA methyltransferase 1 (DNMT1)-associated protein 1 (DMAP1) is a nuclear protein that functions in transcriptional repression and DNA repair. DMAP1 was first identified as an activator of DNMT1 methyltransferase activity (1). Both DMAP1 and DNMT1 are targeted to replication foci during S phase and function to transfer proper methylation patterns to newly synthesized DNA during replication (1). In late S phase, DMAP1-DNMT1 co-operate with a p33ING1-Sin3-HDAC2 complex to maintain pericentric heterochromatin by deacetylating histones, methylating histone H3 at Lys9, and methylating DNA (1,2). The DMAP1 protein is also part of the TIP60-p400 complex, a histone acetyltransferases (HAT) and chromatin-remodeling complex that functions in DNA repair (3,4). Upon DNA damage, the TIP60-p400 complex acetylates histone H4 at Lys16 to induce chromatin relaxation and activation of the ATM kinase. DMAP1 is required for DNA-damage induced TIP60-p400-mediated histone acetylation, and deletion of DMAP1 impairs AMT function (5). DMAP1-DNMT1 may also methylate DNA at sites of DNA damage during homologous recombination, which results in gene silencing (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Host cell factor C1 (HCFC1) was first identified as the host cell factor for human herpes simplex virus infection. HCFC1 and the viral protein VP16 belong to a multi-protein complex that promotes transcription of viral immediate early genes (1). The relatively large HCFC1 protein contains 6 centrally located 26 amino acid repeats that can be O-GlcNAcylated and subjected to O-linked beta-N-acetylglucosamine transferase (OGT) cleavage (2-4). The resulting amino-terminal (HCFC1-N) and carboxy-terminal (HCFC1-C) fragments are non-covalently associated and play important roles in cell cycle regulation. The HCFC1-N peptide facilitates progression through the G1 phase of the cell cycle while HCFC1-C enables proper mitosis and cytokinesis during the M phase (5-7). As HCFC1 plays an important role in neurodevelopment, mutations in the corresponding gene are associated with neurodevelopmental disorders (e.g., intellectual disability) in humans (8).

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

Application Methods: Western Blotting

Background: Fragile X syndrome, a frequent cause of inherited mental retardation, often results from expansion of the CGG trinucleotide repeat in the gene that encodes the fragile X mental retardation protein (FMRP) (1). FMRP (also known as FMR1) and its two autosomal homologs (FXR1 and FXR2) all bind RNA and play a role in the pathogenesis of fragile X syndrome (1-3). Each of these related proteins can associate with one another as well as form homodimers (3). FMRP can act as a translation regulator and is a component of RNAi effector complexes (RISC), suggesting a role in gene silencing (4). In Drosophila, dFMRP associates with Argonaute 2 (Ago2) and Dicer and coimmunoprecipitates with miRNA and siRNA. These results suggest that fragile X syndrome is related to abnormal translation caused by a defect in RNAi-related pathways (5). In addition, FMRP, FXR1, and FXR2 are components of stress granules (SG) and have been implicated in the translational regulation of mRNAs (6).

$262
3 nmol
300 µl
SignalSilence® p38α MAPK siRNA I (Mouse Specific) from Cell Signaling Technology (CST) allows the researcher to specifically inhibit p38α MAPK 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
Mouse

Background: p38 MAP kinase (MAPK), also called RK (1) or CSBP (2), is the mammalian orthologue of the yeast HOG kinase that participates in a signaling cascade controlling cellular responses to cytokines and stress (1-4). Four isoforms of p38 MAPK, p38α, β, γ (also known as Erk6 or SAPK3), and δ (also known as SAPK4) have been identified. Similar to the SAPK/JNK pathway, p38 MAPK is activated by a variety of cellular stresses including osmotic shock, inflammatory cytokines, lipopolysaccharide (LPS), UV light, and growth factors (1-5). MKK3, MKK6, and SEK activate p38 MAPK by phosphorylation at Thr180 and Tyr182. Activated p38 MAPK has been shown to phosphorylate and activate MAPKAP kinase 2 (3) and to phosphorylate the transcription factors ATF-2 (5), Max (6), and MEF2 (5-8). SB203580 (4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)-imidazole) is a selective inhibitor of p38 MAPK. This compound inhibits the activation of MAPKAPK-2 by p38 MAPK and subsequent phosphorylation of HSP27 (9). SB203580 inhibits p38 MAPK catalytic activity by binding to the ATP-binding pocket, but does not inhibit phosphorylation of p38 MAPK by upstream kinases (10).

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

Application Methods: Western Blotting

Background: Cellular levels of mRNAs are controlled by mRNA stability, the rate of synthesis and the rate of degradation. The presence and length of the poly(A) tail has been associated with mRNA stability (1). Exonucleolytic shortening of the poly(A) tail is the process that initiates the decay of many eukaryotic mRNAs (2). Poly(A)-specific ribonuclease (PARN) is the enzyme responsible for initiation of deadenylation and exonucleolytic shortening of mRNA transcripts. Through an evolutionarily conserved mechanism, PARN also translationally silences selective mRNAs during early embryonic development (3). PARN is constitutively expressed in most mammalian tissues and plays a critical role in the post-transcriptional control of gene expression (4).

$262
3 nmol
300 µl
SignalSilence® PI3 Kinase p110α siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit PI3 Kinase p110α 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 CST™ SignalSilence® siRNA products are rigorously tested in-house and have been shown to reduce protein expression by western analysis.
REACTIVITY
Human

Background: Phosphoinositide 3-kinase (PI3K) catalyzes the production of phosphatidylinositol-3,4,5-triphosphate by phosphorylating phosphatidylinositol (PI), phosphatidylinositol-4-phosphate (PIP), and phosphatidylinositol-4,5-bisphosphate (PIP2). Growth factors and hormones trigger this phosphorylation event, which in turn coordinates cell growth, cell cycle entry, cell migration, and cell survival (1). PTEN reverses this process, and research studies have shown that the PI3K signaling pathway is constitutively activated in human cancers that have loss of function of PTEN (2). PI3Ks are composed of a catalytic subunit (p110) and a regulatory subunit. Various isoforms of the catalytic subunit (p110α, p110β, p110γ, and p110δ) have been isolated, and the regulatory subunits that associate with p110α, p110β, and p110δ are p85α and p85β (3). In contrast, p110γ associates with a p101 regulatory subunit that is unrelated to p85. Furthermore, p110γ is activated by βγ subunits of heterotrimeric G proteins (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Mortality factor 4-like protein 1 (MORF4L1/MRG15) is a chromo domain-containing protein that is part of several histone modifying complexes, including the Tip60 histone acetyltransferase (HAT) complex, histone deacetylase (HDAC) complexes, and the JARID1A and JARID1B histone demethylase complexes (1-6). MORF4L1/MRG15 recognizes di- or trimethylated Lys36 of histone H3 through its chromo domain. This interaction recruits and anchors MORF4L1/MRG15-associated chromatin modifying complexes to target genes for transcriptional regulation (7,8). MORF4L1/MRG15 plays a role in DNA repair as part of the Tip60 HAT complex (9,10). MORF4L1/MRG15 regulates alternative splicing during co-transcriptional splicing of mRNA as a part of the JARID1A complex (11). MORF4L1/MRG15 recruitment of the JARID1B complex to embryonic stem cell renewal-associated genes is important for repression of cryptic transcription and maintenance of proper transcriptional elongation (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: Myelinated axons contain un-myelinated gaps called nodes of Ranvier. These regularly spaced gaps are critical for the proper propagation and rapid conduction of nerve impulses in the central and peripheral nervous system (1). The structure and organization of the nodes of Ranvier is dictated by interaction between the axon and glial cells (2). Voltage-gated sodium channels concentrated at the nodes and potassium channels clustered at the paranodes are responsible for propagation of the action potentials (3,4). Other proteins that contribute to the architecture and function of the nodes of Ranvier include βIV spectrin (5), ankyrin-G (6), and the L1 cell adhesion molecules, neurofascin and NrCAM (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: THEMIS is a recently identified protein found to be critical for T cell development (1-5). It contains two amino-terminal globular domains, a nuclear localization signal, and a carboxy-terminal proline-rich sequence with homology to SH3 binding domains (2,3). THEMIS is detected in both the cytoplasm and the nucleus (2). It is expressed at low levels in mature T cells and during thymocyte development, with expression peaking in CD4+CD8+ double positive cells (1-5). THEMIS is tyrosine phosphorylated downstream of TCR signaling and associates with the adaptor GRB2 and possibly other SH3 domain-containing proximal TCR signaling molecules (1-5). Mice lacking THEMIS have a defect in positive selection that results in decreased numbers of both single positive thymocytes and mature T cells (1-5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Protein ubiquitination requires the concerted action of the E1, E2, and E3 ubiquitin-conjugating enzymes. Ubiquitin is first activated through ATP-dependent formation of a thiol ester with ubiquitin-activating enzyme E1. The activated ubiquitin is then transferred to a thiol group of ubiquitin-carrier enzyme E2. The final step is the transfer of ubiquitin from E2 to an ε-amino group of the target protein lysine residue, which is mediated by ubiquitin-ligase enzyme E3 (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: SH2-containing inositol phosphatase 1 (SHIP1) is a hematopoietic phosphatase that hydrolyzes phosphatidylinositol-3,4,5-triphosphate to phosphatidylinositol-3,4-bisphosphate (1). SHIP1 is a cytosolic phosphatase with an SH2 domain in its amino terminus and two NPXY Shc binding motifs in its carboxy terminus (1,2). Upon receptor cross-linking, SHIP is first recruited to the membrane junction through binding of its SH2 domain to the phospho-tyrosine in the ITIM motif (2), followed by tyrosine phosphorylation on the NPXY motif (2). The membrane relocalization and phosphorylation on the NPXY motif is essential for the regulatory function of SHIP1 (3-5). Its effect on calcium flux, cell survival, growth, cell cycle arrest, and apoptosis is mediated through the PI3K and Akt pathways (3-5). Tyr1021 is located in one of the NPXY motifs in SHIP1, and its phosphorylation is important for SHIP1 function (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Rat

Application Methods: Immunoprecipitation, Western Blotting

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: SynGAP is a synaptic GTPase-activating protein selectively expressed in the brain and found at higher concentrations specifically at excitatory synapses in the mammalian forebrain. SynGAP has a PH domain, a C2 domain, and a highly conserved RasGAP domain, which negatively regulates both Ras activity and its downstream signaling pathways. SynGAP interacts with the PDZ domains of SAP102, as well as PSD95, a postsynaptic scaffolding protein that couples SynGAP to NMDA receptors (1). SynGAP is phosphorylated by Ca2+/calmodulin-dependent protein kinase II (CaMKII) at Ser765 and Ser1123, among other sites (2,3). Phosphorylation of SynGAP results in stimulation of the GTPase activity of Ras, and PSD95 dependent CaMKII phosphorylation of SynGAP increases after transient brain ischemia (1,4). SynGAP is implicated in NMDAR- and CaMKII-dependent regulation of AMPAR trafficking and plays an important role in synaptic plasticity (3,5). SynGAP is critical during neuronal development as mice lacking SynGAP protein die postnatally. Furthermore, SynGAP mutant mice have reduced long-term potentiation (LTP) and perform poorly in spatial memory tasks (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The type II receptor for Müllerian inhibiting substance (MIS), also known as the anti-Müllerian hormone receptor 2 (AMHR2), binds a hormone-ligand that directs the incomplete development of Müllerian ducts in male embryos (1,2). MIS-R2 is a single transmembrane serine/threonine kinase receptor of the TGF-β receptor family involved in the phosphorylation of shared type 1 receptors and Smad transcriptional regulators (3,4). MIS produced by the fetal testis promotes the regression of Müllerian ducts that would otherwise differentiate into the uterus and fallopian tubes in the male fetus (5). Corresponding MIS-R2 gene mutations can cause persistent Müllerian duct syndrome type 2 (PMDS-2), a form of male pseudohermaphroditism characterized by a failure of Müllerian duct regression (6). The presence of MIS-R2 is observed in ovarian cancer cell lines that respond positively to treatment with recombinant MIS, suggesting that both receptor and ligand may be important therapeutic tools (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, Mouse

Application Methods: Western Blotting

Background: SH2D1A and SH2D1B are small, adaptor proteins with a single SH2-domain that play important signal transduction roles mediated by the signaling lymphocytic activation molecule (SLAM) family receptors (1). SH2D1A (also called SAP or SLAM-associated protein) is frequently mutated in patients with X-linked lymphoproliferative disease (Duncan’s disease), which is characterized by extreme susceptibility to Epstein-Barr virus; approximately 50 different SH2D1A mutations have been reported to date (2-4). The single SH2D1B gene in humans (also called EAT-2 or Ewing's sarcoma's/FLI1-activated transcript 2) is present as a pair of duplicated EAT-2A and EAT-2B genes with identical genomic organization in mouse and rat (5,6).

$262
3 nmol
300 µl
SignalSilence® Skp2 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit Skp2 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: Members of the F-box family of proteins are characterized by the approximate 40 amino acid F-box motif named after cyclin F (1,2). F-box proteins constitute one of the four subunits of the Skp1-Cullin-F-box (SCF) ubiquitin ligase complex. The substrate specificity of SCF complexes is determined by the interchangeable F-box proteins, which act as adaptors by associating with phosphorylated substrate proteins and recruiting them to the SCF core. F-box proteins contain two fundamental domains: the F-box motif mediates binding to Skp1 and a leucine rich repeat (LRR) domain mediates substrate interactions.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Myotubularin-related protein 14 (MTMR14), also known as Jumpy, is a myotubularin-related phosphoinositol-3-phosphate (PI3P) phosphatase (1). Mutations in the MTMR14 gene have been associated with centronuclear myopathy (1). MTMR14 deficiency in mice leads to altered calcium homeostasis and muscle disorders (2). MTMR14 has also been shown to play a role in autophagy, a process that is highly regulated by phosphatidylinositides through the type III PI3K, Vps34 (3). MTMR14 was localized to autophagic isolation membranes and early autophagosomes (3). In these studies, MTMR14 inhibited autophagy and mutations of MTMR14 associated with centronuclear myopathy were also defective in autophagy inhibition. In zebrafish, MTMR14 knockdown was shown to increase the number of autophagosomes, suggesting that its activity is associated with an inhibition of autophagy (4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Mesoderm development candidate genes 1 (MESDC1) and 2 (MESDC2) were identified from the mesoderm development (MESD) deletion interval located on mouse chromosome 7 (1). MESD acts as a chaperone for low-density lipoprotein receptor (LDLR) proteins in the ER, and particularly associates with Wnt signaling pathway coreceptors LRP5 and LPR6 (2). MESD is required for proper LRP5/6 folding and maturation to the cell surface, which plays a major role in Wnt signaling (3-5). The interaction between MESD and LRP5 is disrupted by a G171V mutation in LRP5 that is found in individuals with a familial phenotype characterized by high bone mass (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Triacylglycerol is stored in lipid droplets as a primary energy reserve. Perilipin is localized at the periphery of lipid droplets and serves as a protective coating against lipases (1-3). Evidence suggests that PKA regulates lipolysis by phosphorylating perilipin (1,2,4,5). Phosphorylation of perilipin results in the conformational change that exposes lipid droplets to endogenous lipases, such as hormone-sensitive lipases (2). Hence, perilipin plays a pivotal role in lipid storage (2,5).