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Product listing: VIMP (D1D1M) Rabbit mAb, UniProt ID Q9BQE4 #15160 to Phospho-PDGF Receptor β (Tyr740) (32A9) Rabbit mAb, UniProt ID P09619 #3168

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: VCP-interacting membrane protein (VIMP, selenoprotein S) is a putative reductase and endoplasmic reticulum (ER)-resident protein involved in the ER-associated degradation (ERAD) pathway (1,2). Research studies indicate that VIMP may play a protective role against inflammation and reduce ER-stress (3). The VIMP protein is a single-pass, transmembrane protein that recruits the cytosolic p97/VCP AAA-ATPase and its cofactors, UFD1 and NPL4, to the ER membrane (4). An ER membrane complex containing Derlin-1 and VIMP forms a critical node in the ERAD machinery and links substrate recognition in the ER lumen with the retrotranslocation function of the p97/VCP AAA-ATPase in the cytosol (1,4). Polymorphisms in the corresponding VIMP gene are associated with spontaneous preterm births and cardiovascular disease risk (5,6) while other studies do not support a correspondence between VIMP polymorphisms and inflammatory disorders (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The gene encoding metastasis-associated in colon cancer-1 (MACC1) was identified based on its overexpression in metastatic colon carcinoma (1), and was later shown to be overexpressed in multiple human cancers, including hepatocellular carcinoma, gastric cancer, head and neck cancer, and breast cancer (2-5). MACC1 regulates HGF/MET and β-catenin signaling, resulting in increased proliferation, migration and invasion, and initiation of the epithelial-mesenchymal transition (EMT) (2). Researchers have shown that MACC1 can be used as a prognostic indicator in solid tumors, and that it has potential as a therapeutic target (6).

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

Application Methods: Western Blotting

Background: The initiation of DNA replication in mammalian cells is a highly coordinated process that ensures duplication of the genome only once per cell division cycle. Origins of replication are dispersed throughout the genome and their activities are regulated via the sequential binding of pre-replication and replication factors. The origin recognition complex (ORC) is thought to bind to chromatin throughout the cell cycle (1,2). The pre-replication complex (Pre-RC) forms in late mitosis/early G1 phase with the binding of CDT1 and cdc6 to the origin, which allows binding of the heterohexameric MCM2-7 complex. The MCM complex is thought to be the replicative helicase and formation of the Pre-RC is referred to as chromatin licensing. Subsequent initiation of DNA replication requires the activation of the S-phase promoting kinases cdk2 and cdc7. Cdc7 phosphorylates MCM proteins bound to chromatin and, in conjunction with CDT1, recruits the replication factor cdc45 (3-5). Cdc45 is required for formation of pre-initiation complexes at the G1/S transition and for activation of replication origins. The level of cdc45 protein expression is associated with the proliferative status of the cell or tissue. Terminally differentiated and senescent cells lack cdc45 and highly proliferative cell lines express high levels of cdc45 (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Brain-specific kinase 1 (BRSK1; SAD-B) and Brain-specific kinase 2 (BRSK2; SAD-A) are serine/threonine kinases closely related to AMPK. LKB1 phosphorylates Thr189 in the T-loop of BRSK1 and Thr174 in the T-loop of BRSK2, resulting in activation of the kinases (1). BRSK1 localizes to synaptic vesicles in the hippocampus and cerebellum, together with the active zone proteins Bassoon and CAST, and BRSK1 phoshorylates the active zone protein RIM1 (2). An alternatively spliced from of BRSK1 displays unique activity during the cell cycle, phosphorylating Ser131 of γ-tubulin and controling centrosome duplication (3). Neuronal polarization, including axon formation, is fundamental for normal brain development. BRSK1 -/- and BRSK2 -/- mice have defects in neuronal polarity and impaired corticogenesis (4). Knockdown of BRSK1 and BRSK2 in vitro diminishes axonal growth (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Interferons (IFNs) appear both locally and systematically early after viral infection and participate in limiting the spread of infection. They also affect cell differentiation, growth, surface antigen expression and immunoregulation (1). There are three naturally occurring interferons: α, β and γ. IFN-α is derived from lymphoblastic tissue and has a number of therapeutic applications in the treatment of various human cancers and diseases of viral origin. Recombinant IFN-α from both natural and synthetic genes binds to a common cell surface receptor and induces antiviral activity in a variety of cell lines. When binding to discrete cell surface receptors on target cells, IFN-α induces rapid changes in Jak/Stat phosphorylation, which initiates the Jak/Stat signaling pathway (2). IFN-α signaling also involves production of DAG without an increased intracellular free calcium concentration and the subsequent activation of calcium-independent isoforms of PKC (β and ε) (3). All IFN-α signaling pathways lead to final alterations of gene expression, which mediate their pleiotropic biologic activities.

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

Application Methods: Western Blotting

Background: PATL1/PAT1b is the human homolog of the evolutionarily conserved Pat1/Mrt1 protein, which was first identified in Saccharomyces cerevisiae (1,2). This protein is a critical component of the RNA decay machinery in the cytoplasmic processing bodies (P-bodies), localized foci of mRNA silencing and degradation (3). PATL1/PAT1b interacts with many key components of the RNA decay machinery. These include the 5’ decapping proteins DDX6/RCK, DCP1, DCP2, EDC4, and the LSm1–7 ring (3,4) as well as the 3’ deadenylation complex of CAF1-CCR4-NOT1 (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Epithelial Protein Lost in Neoplasm (EPLIN) is an actin-binding protein that regulates actin filament dynamics and cross-linking (1). Alpha and beta isoforms are generated from alternate promoters, with the EPLIN-β isoform representing the full-length protein and the EPLIN-α isoform lacking the amino-terminal 160 amino acids (2). Increased expression of EPLIN protein results in more abundant and larger actin stress fibers due to stabilizing of cross-links and inhibition of actin depolymerization. EPLIN protein inhibits Rac1-promoted membrane ruffling and Arp2/3-associated actin filament branching (1).Research studies demonstrate reduced EPLIN-α expression in tumor tissues, and correlate this reduction with increased invasiveness and poor clinical outcomes (3). The EPLIN protein is an important negative regulator of the epithelial-mesenchymal transition (EMT)(4). While EMT is a critical process during normal embryonic development, dysregulation in transformed cells is a key step in the transition to metastasis (5).

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

Application Methods: Western Blotting

Background: Oligophrenin-1 is a RhoGTPase-activating protein encoded by the gene OPHN1 (1). Oligophrenin-1 is composed of an N-terminal BAR domain, a pleckstrin homology domain, a central RhoGAP domain, and three putative C-terminal SH3-binding sites. Oligophrenin-1 plays a role in membrane signaling through interaction of its BAR domain with curved membranes, binding of its pleckstrin homology domain with membrane phosphoinositides, and interaction of the SH3-binding sites with adaptor proteins (1-3). Oligophrenin-1 regulates synaptic vesicle endocytosis (3) and plays an important role in dendritic spine morphogenesis (4). Furthermore, by interacting with the transcription factor Rev-erbα and protecting it from degradation, Oligophrenin-1 participates in the regulation of the circadian rhythm in the hippocampus (5). Research studies have demonstrated an involvement of Oligophrenin-1 in X-linked mental retardation (1).

$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. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated TRAIL (C92B9) Rabbit mAb #3219.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL), also referred to as Apo2 ligand, first identified based on its sequence homology to TNF and Fas/Apo ligand is a member of the TNF family of cytokines and either exists as a type II membrane or soluble protein (1,2). TRAIL induces apoptosis in a variety of transformed cell lines and plays a role in anti-tumor and anti-viral immune surveillance (3). TRAIL signals via binding with death receptors DR4 (TRAIL-R1) (4) and DR5 (TRAIL-R2) (5-8) which can trigger apoptosis as well as NF-κB activation (7,9). Death domains on these receptors leads to the recruitment of a death-induced signaling complex (DISC) leading to caspase-8 and subsequent caspase-3 activation. In addition, TRAIL binds with decoy receptors DcR1 (TRAIL-R3) (10-13) and DcR2 (TRAIL-R4, TRUNDD) (14-15) which lack the functional cytoplasmic death domain antagonizing TRAIL-induced apoptosis. Osteoprotegerin (OPG) has also been identified as receptor capable of inhibiting TRAIL-induced apoptosis (16). The selectivity of soluble TRAIL at triggering apoptosis in transformed cells as compared to normal cells has led to its investigation as a potential cancer therapeutic (17-18).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein Phosphatase 2A subunit isoform R5-δ (PPP2R5D) belongs to the R5/B'/B56 family of the regulatory subunit B of serine/threonine phosphatase 2A (1). PPP2R5D (B-δ) is structurally related to the other components of subunit B, B-α. PPP2R5D lacks the WD-40 repeats that are important for protein-protein interaction (1-2). Structural differences may contribute to distinct down stream effects (3) and directing PP2A nuclear localization (4). Current evidence suggests that in contrast to B-α, PPP2R5D modulates the TGF-β/Actividin/Nodal signaling pathways by restricting the downstream activities of the type I TGF-β receptors, ALK4, and ALK5 (3)

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

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

Application Methods: Western Blotting

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The membrane protein syntaxin 5 (STX5) is a key component of soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) receptor (SNARE) complexes that regulate cellular protein transport, vesicle docking, and membrane fusion (1). Syntaxin 5 protein is found as a 42 kDa ("long") protein localized to the Golgi complex and endoplasmic reticulum, and a “short” 35 kDa isoform localized primarily to the Golgi (2,3). Formation of the syntaxin 5 SNARE complex, which also includes proteins Sec22B, Bet1, GOSR1, GOSR2, and Ykt6, allows for regulation of ER-to-Golgi transport, intra-Golgi transport, and endosome-to-Golgi retrograde transport (4-6). Research studies indicate that the syntaxin 5 SNARE complex also plays an essential role in autophagy following autophagosome formation. Intracellular protein transport mediated by the syntaxin 5 complex is required for transport and localized activity of lysosomal proteases. The experimental reduction or deletion of syntaxin 5 complex components results in non-functional lysosomes and accumulation of autophagosomes (7).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Eukaryotic translation initiation factor 1 (eIF1) was first purified as a factor stimulating binding of Met-tRNA and mRNA to the ribosome (1,2). eIF1 is essential for growth in yeast and two classes of mutations in yeast eIF1 indicate a role for this protein in ensuring accurate translation initiation site selection (3). It has been demonstrated that eIF1 expression is stress-inducible, suggesting that modulation of translation initiation occurs during cellular stress (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: The sodium-dependent phosphate transport protein 2B (NaPi-2b, SLC34A2) is a sodium dependent inorganic phosphate (Pi) transporter that regulates phosphate homeostasis in various organs, including the small intestine, lung, liver, and testis (1). In the small intestine, NaPi-2b localizes to the intestinal brush border membrane to mediate Pi reabsorption (2). In the lung, NaPi-2b is expressed in the apical membrane of type II alveolar cells and is involved in the synthesis of surfactant (3). Mutations in the corresponding SLC34A2 gene causes pulmonary alveolar microlithiasis, a rare autosomal recessive disorder characterized by the deposition of calcium phosphate microliths throughout the lungs (4). Research studies show aberrant expression of NaPi-2b in various type of cancer, including ovarian, breast, and lung cancer (5). Chromosomal rearrangements involving SLC34A2-ROS1 are seen in gastric carcinoma and non-small cell lung cancer and result in the formation of a SLC34A2-ROS1 chimeric protein that retains a constitutive kinase activity (6,7).

$269
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: CD64 (FcgammaRI), CD32 (FcgammaRII) and CD16 (FcgammaRIII) are three classes of the immunoglobulin superfamily. CD64 has a high affinity for IgG with three Ig-like domains while CD32 and CD16 have low affinities with two Ig-like domains. Two genes encode CD16-A and CD16-B resulting only in a 6 amino acid difference in their ectodomains. However, CD16-A has a transmembrane anchor versus CD16-B, which has a glycosylphosphatidylinositol (1). CD64, CD32 and CD16 are membrane glycoproteins that are expressed by all immunologically active cells and trigger various immune functions (activate B cells, phagocytosis, antibody-dependent cellular cytotoxicity, immune complex clearance and enhancement of antigen presentation) (2). CD16 cross-linking induces tyrosine phosphorylation (Tyr394) of Lck in NK cells (3). CD32 has tyrosine-based activation motifs in the cytoplasmic domain in contrast to CD16, which associates with molecules possessing these motifs (1).

$262
3 nmol
300 µl
SignalSilence® Bmi1 siRNA I from Cell Signaling Technology (CST) allows the researcher to specifically inhibit Bmi1 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: The polycomb group (PcG) of proteins contributes to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation, and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death, and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, EED-EZH2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. This histone methyl-transferase activity requires the Ezh2, Eed, and Suz12 subunits of the complex (5). Histone H3 methylation at Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinylates histone H2A on Lys119 (6). Bmi1 is a component of the PRC1 complex, which together with Ring1 strongly enhances the E3 ubiquitin ligase activity of the Ring2 catalytic subunit (7). Bmi1 plays an important role in the regulation of cell proliferation and senescence through repression of the p16 INK4A and p19 ARF genes and is required for maintenance of adult hematopoietic and neural stem cells (3,4,8-10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Tissue Factor (TF)/CD142 (Coagulation factor III/Thromboplastin) is a type-I transmembrane glycoprotein that serves as the cell surface receptor and cofactor for blood coagulation factors VII and VIIa, and thus plays a central role in hemostasis and thrombosis (1). The TF:VIIa receptor-ligand complex is widely recognized as the initiator of the extrinsic blood coagulation protease cascade, which ultimately leads to the generation of fibrin and thrombin (1). A member of the type-II cytokine receptor superfamily, TF has also been shown to engage the PI3K (2) and MAPK (3) signaling cascades upon binding to factor VIIa in order to drive cellular responses such as cell migration, growth, and proliferation. Although the function of TF under physiologic conditions is to coordinate blood clotting in response to tissue damage, TF is implicated in pathologic conditions such as tumorigenesis. Indeed, TF is aberrantly expressed in colorectal cancer, breast cancer, pancreatic cancer, and glioblastoma multiforme (4). It has been shown to promote tumor angiogenesis, tumor growth, metastasis, and venous thrombosis (5). Given that TF overexpression is associated with numerous types of solid tumors, it has garnered much attention as a potential therapeutic target.

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

Application Methods: Western Blotting

Background: Leucyl-tRNA Synthetase (LARS) is a leucine sensor critical for the activation of mTORC1 (1). mTORC1 kinase complex is an important component in the regulation of cell growth (2,3). Its activity is modulated by energy levels, growth factors, and amino acids (4,5). The four related GTPases, RagA, RagB, RagC, and RagD, have been shown to interact with raptor in mTORC1 (2,3). These interactions are both necessary and sufficient for mTORC1 activation in response to amino acid signals (2,3). LARS functions as a GTPase-activating protein (GAP) and interacts directly with RagD GTPase (1). The role of LARS in leucine sensing is not related to its tRNA charging activity (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Tuberin is a product of the TSC2 tumor suppressor gene and an important regulator of cell proliferation and tumor development (1). Mutations in either TSC2 or the related TSC1 (hamartin) gene cause tuberous sclerosis complex (TSC), an autosomal dominant disorder characterized by development of multiple, widespread non-malignant tumors (2). Tuberin is directly phosphorylated at Thr1462 by Akt/PKB (3). Phosphorylation at Thr1462 and Tyr1571 regulates tuberin-hamartin complexes and tuberin activity (3-5). In addition, tuberin inhibits the mammalian target of rapamycin (mTOR), which promotes inhibition of p70 S6 kinase, activation of eukaryotic initiation factor 4E binding protein 1 (4E-BP1, an inhibitor of translation initiation), and eventual inhibition of translation (3,6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Vascular endothelial growth factor receptor 3 (VEGFR3) is a 195 kDa membrane receptor tyrosine kinase. VEGF receptors are characterized by the presence of seven extracellular immunoglobulin (Ig)-like domains followed by a membrane-spanning domain and a conserved intracellular tyrosine kinase domain (1). VEGF receptor 3 expression is largely restricted to adult lymphatic endothelium and is thought to control lymphangiogenesis (1,2). Binding of VEGF-C/VEGF-D to VEGFR3 results in transphosphorylation of tyrosine residues in its intracellular domain, recruitment of signaling molecules and activation of ERK1/2 and Akt signaling cascades (1,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Chromatin IP, Chromatin IP-seq, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: The super elongation complex (SEC) plays a critical role in regulating RNA polymerase II (RNAPII) transcription elongation (1). The SEC is composed of AFF4, AFF1/AF4, MLLT3/AF9, and MLLT1/ENL proteins. The pathogenesis of mixed lineage leukemia is often associated with translocations of the SEC subunits joined to the histone H3 Lys4 methyltransferase mixed lineage leukemia (MLL) gene (1-4). The SEC has been found to contain RNAPII elongation factors eleven-nineteen lysine-rich leukemia (ELL), ELL2, and ELL3, along with the associated factors EAF1 and EAF2, which can increase the catalytic rate of RNAPII transcription in vitro, (1,2,5-7). The SEC positive transcription elongation factor b (P-TEFb) phosphorylates the carboxy-terminal domain within the largest subunit of RNAP II at Ser2 of the heptapeptide repeat. The SEC negative transcription elongation factors, DRB-induced stimulating factor (DSIF) and negative elongation factor (NELF), signal the transition from transcription initiation and pausing to productive transcription elongation (2,8-10). The chromosomal translocation of MLL with the members of the SEC leads to SEC recruitment to MLL regulated genes, such as the highly developmentally regulated Hox genes, implicating the misregulation and overexpression of these genes as underlying contributors to leukemogenesis (1,2,9,11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Autophagy is a catabolic process for the autophagosomic-lysosomal degradation of bulk cytoplasmic contents (1,2). Autophagy is generally activated by conditions of nutrient deprivation, but it has also been associated with a number of physiological processes including development, differentiation, neurodegenerative diseases, infection, and cancer (3). Autophagy marker Light Chain 3 (LC3) was originally identified as a subunit of microtubule-associated proteins 1A and 1B (termed MAP1LC3) (4) and subsequently found to contain similarity to the yeast protein Apg8/Aut7/Cvt5 critical for autophagy (5). Three human LC3 isoforms (LC3A, LC3B, and LC3C) undergo post-translational modifications during autophagy (6-9). Cleavage of LC3 at the carboxy terminus immediately following synthesis yields the cytosolic LC3-I form. During autophagy, LC3-I is converted to LC3-II through lipidation by a ubiquitin-like system involving Atg7 and Atg3 that allows for LC3 to become associated with autophagic vesicles (6-10). The presence of LC3 in autophagosomes and the conversion of LC3 to the lower migrating form, LC3-II, have been used as indicators of autophagy (11).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The Ras family small GTPase Ran is involved in nuclear envelope formation, assembly of the mitotic spindle, and nuclear transport (1,2). Like other small GTPases, Ran is active in its GTP-bound form and inactive in its GDP-bound form. Nuclear RanGTP concentration is maintained through nuclear localization of guanine nucleotide exchange factor (GEF) activity, which catalyzes the exchange of bound GDP for GTP. Regulator of chromatin condensation 1 (RCC1) is the only known RanGEF (3). RCC1 is dynamically chromatin-bound throughout the cell cycle, and this localization is required for mitosis to proceed normally (4,5). Appropriate association of RCC1 with chromatin is regulated through amino-terminal phosphorylation (5,6) and methylation (7). RCC1 regulation of RanGTP levels in response to histone modifications regulates nuclear import during apoptosis (8). In mitosis RCC1 is phosphorylated at Ser11, possibly by cyclin B/cdc2 (9-11). This phosphorylation may play a role in RCC1 interaction with chromatin and RCC1 RanGEF activity (6).

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

Application Methods: Western Blotting

Background: Glycine decarboxylase (GLDC) is a component of a mitochondrial protein complex that catalyzes the degradation of glycine (1). The glycine cleavage system is composed of three distinct enzymes (P-, T- and L-proteins) and an additional component (H-protein) that transfers a glycine methylamine group from one enzyme to another. The GLDC protein (P-protein) is the decarboxylase that binds the methylamine group for transfer to the T-protein (2). Tumor-initiating cells in the primary non-small cell lung cancer (NSCLC) express high levels of GLDC and LIN28B, both of which are essential for the proliferation of tumor-initiating cells (3). GLDC is an oncogene that promotes tumorigenesis through its metabolic activity (3). Mutations in the corresponding GLDC gene account for the majority of reported cases of glycine encephalopathy, which is a metabolic disorder characterized by the accumulation of glycine, lethargy, hypotonia, intractable seizures, and death (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: GGA3 is a member of the GGA family of proteins which also includes GGA1 and GGA2. These proteins consist of four distinct segments: a VHS domain that binds the di-leucine sorting signal DXXLL; a GAT domain that binds Arf-GTP; a hinge region that recruits clathrin; and a GAE domain that has sequence similarity to γ-adaptin and recruits a number of proteins. Arf1-GTPase recruits GGA3 to the trans-Golgi network. GGAs sort acid hydrolases to the lysosome and are involved in transporting proteins containing the DXXLL signal from the Golgi complex to the endosome (1). During apoptosis or cerebral ischemia, GGA3 is cleaved by caspase-3 at Asp313, reducing GGA3 levels and lysosomal degradation of β-secretase (BACE). The resulting elevated amount and activity of BACE plays a role in amyloid-β (Aβ) production, consistent with BACE elevation and Aβ accumulation in Alzheimer’s Disease (2).

$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).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Hic-5 is a LIM domain family member orginally identified as a TGFbeta1 and hydrogen peroxide inducible gene, and is nearly identical to the androgen receptor co-activator ARA55 (1-3). Hic-5 is structurally related to paxillin, and both proteins are localized to focal adhesions and thought to serve as adaptor molecules, linking signals from the extracellular matrix to cytoskeletal regulation and intracelluar signaling (4,5). Like paxillin, Hic-5 contains four LD motifs and four LIM domains. Expression of Hic-5 can affect cell growth and differentiation (6-8). Increased expression of Hic-5 is observed during cellular senescence in fibroblasts, and ectopic expression in immortalized fibroblasts suppressed cell growth (8). Unlike paxillin, Hic-5 may translocate to the nucleus in response to oxidants like hydrogen peroxide (9). It has been proposed that Hic-5 serves to shuttle redox signaling from focal adhesions to the nucleus where it acts as a transcriptional co-activator for some transciption factors including, Sp1 and PPARgamma (7,9,10). Phosphorylation of Hic-5 at Tyr60 by CAKbeta and Fyn may activiate Hic-5 signaling by allowing binding to downstream SH2 domain containing proteins (11).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Western Blotting

Background: Platelet derived growth factor (PDGF) family proteins exist as several disulphide-bonded, dimeric isoforms (PDGF AA, PDGF AB, PDGF BB, PDGF CC, and PDGF DD) that bind in a specific pattern to two closely related receptor tyrosine kinases, PDGF receptor α (PDGFRα) and PDGF receptor β (PDGFRβ). PDGFRα and PDGFRβ share 75% to 85% sequence homology between their two intracellular kinase domains, while the kinase insert and carboxy-terminal tail regions display a lower level (27% to 28%) of homology (1). PDGFRα homodimers bind all PDGF isoforms except those containing PDGF D. PDGFRβ homodimers bind PDGF BB and DD isoforms, as well as the PDGF AB heterodimer. The heteromeric PDGF receptor α/β binds PDGF B, C, and D homodimers, as well as the PDGF AB heterodimer (2). PDGFRα and PDGFRβ can each form heterodimers with EGFR, which is also activated by PDGF (3). Various cells differ in the total number of receptors present and in the receptor subunit composition, which may account for responsive differences among cell types to PDGF binding (4). Ligand binding induces receptor dimerization and autophosphorylation, followed by binding and activation of cytoplasmic SH2 domain-containing signal transduction molecules, such as GRB2, Src, GAP, PI3 kinase, PLCγ, and NCK. A number of different signaling pathways are initiated by activated PDGF receptors and lead to control of cell growth, actin reorganization, migration, and differentiation (5). Tyr751 in the kinase-insert region of PDGFRβ is the docking site for PI3 kinase (6). Phosphorylated pentapeptides derived from Tyr751 of PDGFRβ (pTyr751-Val-Pro-Met-Leu) inhibit the association of the carboxy-terminal SH2 domain of the p85 subunit of PI3 kinase with PDGFRβ (7). Tyr740 is also required for PDGFRβ-mediated PI3 kinase activation (8).