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Product listing: Notch3 Antibody, UniProt ID Q9UM47 #2889 to p38 MAPK Antibody, UniProt ID P53778 #9212

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

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

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Niemann-Pick C1-like 1 (NPC1L1) is a transmembrane protein that plays a critical role in cholesterol absorption (1). It is highly expressed in small intestine and localized along the brush border in both human and mouse epithelial cells (2,3). NPC1L1 mediates cholesterol uptake via vesicular endocytosis (4). Ezetimibe, a potent cholesterol absorption inhibitor used to treat hypercholesterolemia (5), inhibits cholesterol uptake by preventing NPC1L1 from incorporating into clathrin-coated vesicles (4).

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

Application Methods: Western Blotting

Background: Nuclear protein localization protein 4 (NPL4, NPLOC4) was originally identified as a yeast nuclear transport protein that was later recognized as a critical component of the endoplasmic reticulum-associated degradation (ERAD) pathway (1,2). Mammalian NPL4 protein has an amino-terminal ubiquitin-like domain containing a p97 binding site, and a conserved carboxy-terminal zinc finger (NZF) motif responsible for binding ubiquitinated target proteins (2,3). NPL4 binds ubiquitin fusion degradation protein 1 (UFD1) to form a heterodimer that associates with the p97 AAA-ATPase, creating a protein complex that mediates delivery of ubiquitinated ER proteins to the proteasome (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Nucleophosmin (NPM; also known as B23, numatrin or NO38) is an abundant phosphoprotein primarily found in nucleoli. It has been implicated in several distinct cellular functions, including assembly and transport of ribosomes, cytoplasmic/nuclear trafficking, regulation of DNA polymerase α activity, centrosome duplication and molecular chaperoning activities (1,2). The NPM gene is also known for its fusion with the anaplastic lymphoma kinase (ALK) receptor tyrosine kinase. The NPM portion contributes to transformation by providing a dimerization domain, which results in activation of the fused kinase (3,4).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Nuclear Receptor Binding Factor-2 (NRBF-2), also referred to as Comodulator of PPAR and RXRα-2 (COPR-2), has been shown to interact with the AF-2 region of several nuclear hormone receptors with varying affinities such as PPARα, RARα, RARγ, and RXRα (1,2). NRBF-2 contains a LLYLL motif, which matches the LXXLL NR box consensus and is required for functional NRBF-2/nuclear receptor complex formation and repression of receptor function. NRBF-2 also contains a unique autonomous activation domain and, thus, does not completely abrogate nuclear receptor function, suggesting that NRBF-2 might serve as a molecular rheostat to fine-tune the transcriptional activity of liganded nuclear receptors (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Neuronal Cell Adhesion Molecule, or NRCAM, belongs to the immunoglobulins Cell Adhesion Molecules (CAM's) superfamily (1). NRCAM, an ankyrin-binding protein, contributes to the neurite outgrowth by providing directional signaling during axonal cone growth (2, 3, 4). Additionally, it plays a role in mediating the interaction between axons and Schwann cells and contributes to the formation and maintenance of Nodes of Ranvier (5, 6, 7, 8). NRCAM also plays an important role in the establishment of dendritic spines in developing cortical neurons (9). NRCAM is expressed in non-neuronal cells, mostly in endothelial cells (10).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Several protein-protein interactions are essential to membrane fusion during endocytosis. Membrane fusion requires interaction among SNARE1 proteins associated with both donor and acceptor membranes (1,2). Following membrane fusion, the α-SNAP cytoplasmic adapter protein binds to the SNARE complex. N-ethylmaleimide-sensitive factor (NSF), a hexameric ATPase, then associates with the α-SNAP/SNARE complex to mediate SNARE disassembly during membrane fusion (3,4). The ATPase activity of NSF induces a conformational change in the α-SNAP/SNARE complex that leads to its dissociation from the membrane, membrane fusion and eventual recycling of the SNARE complex for subsequent membrane fusion (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Western Blotting

Background: Sphingomyelinases (SMases) catalyze the hydrolysis of sphingomyelin to produce ceramide and phosphocholine (1). Ceramide is an important bioactive lipid triggering signal transduction involved in cell proliferation, apoptosis and differentiation (1,2). A number of SMases have been described and categorized based on their optimum pH activity, cation dependence, tissue distribution, and subcellular localization (1). These include a lysosomal acid SMase, a Zn++-dependent secreted acid SMase, a membrane-bound Mg++-dependent neutral SMase, a Mg++-independent neutral SMase, and an alkaline SMase.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Non-T cell activation linker (NTAL)/linker for activation of B cells (LAB) is a small transmembrane adaptor protein associated with glycolipid-enriched membrane fractions (1,2). NTAL/LAB is also known as LAT2 (linker for activation of T cells 2), WBSCR5, WBS15, and WBSCR15 (Williams-Beuren syndrome chromosome region 15 protein). It is expressed in B cells, monocytes, mast cells, and natural killer cells, but not in resting T cells (3). Upon activation of several receptors, NTAL/LAB becomes tyrosine-phosphorylated and recruits signaling molecules such as GRB2 and c-Cbl into receptor signaling complexes (4-6).

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

Application Methods: Western Blotting

Background: Both the NEDD8 ultimate buster 1 (NUB1) and the related NUB1L isoform are interferon-inducible adaptor proteins that negatively regulate ubiquitin-like protein NEDD8 (1,2). NUB1 protein contains an amino terminal ubiquitin-like (UBL) domain and multiple carboxy terminal ubiquitin-associated (UBA) domains. The NUB1L isoform is generated by alternative splicing and contains an extra UBA domain relative to NUB1 (2). Research studies indicate that NUB1 and NUB1L non-covalently bind NEDD8 and facilitate delivery of both NEDD8 monomers and NEDD8 conjugates to the proteasome for degradation (2-5). In addition, NUB1L binds and enhances the proteasomal degradation of the FAT10 ubiquitin-like protein (6). Additional research shows that NUB1 negatively regulates cell proliferation, likely due to inhibition of NEDD8 conjugation to SCF ubiquitin ligases, which leads to inhibition of p27 and cyclin E ubiquitination (3,7). NUB1 has been identified as a putative therapeutic target in Huntington's disease as NUB1 promotes a decrease in levels of mutant HTT protein (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Nucleomethylin (NML), also known as ribosomal RNA-processing protein 8 (RRP8) and human cerebral protein 1 (Hucep-1), is a nucleolar protein (1,2). NML interacts with the histone de-acetylase protein SirT1 and histone methyl-transferase protein SUV39H1 to form the energy-dependent nucleolar silencing complex (eNoSC) that regulates ribosomal RNA (rRNA) transcription in response to changes in the energy state of the cell (2). As energy levels in the cell decrease due to caloric restriction, eNoSC binds to rRNA genes and represses transcription by SirT1-mediated de-acetylation of histones and SUV39H1-mediated methylation of histone H3 on Lys9. NML binds to di-methylated Lys9 of histone H3 and likely functions in the recruitment and spreading of eNoSC along the rRNA genes (2). NML also contains a methyltransferases-like domain, which binds to S-adenosyl-methionine (SAM) and is required for eNoSC function (2). By limiting the transcription of rRNA genes during caloric restriction, eNoSC promotes the restoration of energy balance and protects cells from energy-dependent apoptosis.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Nucleostemin (GNL3) is a member of the MMR1/HSR1 GTP-binding protein family. It is essential in early embryogenesis (1) and investigators have shown that nucleostemin participates in the control of stem and cancer cell cycle proliferation (2), possibly through regulation of p53 activity (3). Nucleostemin has been found to be expressed in CNS stem cells, embryonic stem cells, and several cancer cell lines, and is localized to both the nucleus and the nucleolus in a cell-cycle dependent manner (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: The nuclear mitotic apparatus protein (NuMA) is a coiled coil protein involved in the formation and maintenance of the mitotic spindle. NuMA plays a role in chromatin organization during interphase, which influences mammary epithelial differentiation (1,2). During apoptosis, carboxy-terminal cleavage of NuMA may amplify signaling in the cell death pathway (2). NuMA is phosphorylated at numerous sites, with phosphorylation at Ser395 occurring in an ATM/ATR-dependent manner in response to DNA damage (3,4).Phosphorylation at Thr2055 by CDK1 is required for spindle pole association of NuMA at the onset of mitosis. Dephosphorylation by PPP2CA leads to enhancement of NuMA at the cell cortex in anaphase and proper cell-cycle progression (5,6).

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

Application Methods: Western Blotting

Background: Nucleoporin 98 kDa (NUP98) is a component of the nuclear pore complex. It is expressed as three different precursors that undergo auto-cleavage to generate a common amino-terminal 98 kDa peptide (NUP98) and carboxy-terminal 6, 96 (NUP96) and 88 (p88) kDa peptides (1,2). NUP98 contains FG and GLFG repeat domains at its amino terminus and a RNA-binding domain in its carboxy terminus (3). The NUP98 gene is localized on chromosome 11p15.5, a region frequently rearranged in leukemias. To date, 15 fusion partners have been identified for NUP98 (4,5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Nucleoporin 98 kDa (NUP98) is a component of the nuclear pore complex. It is expressed as three different precursors that undergo auto-cleavage to generate a common amino-terminal 98 kDa peptide (NUP98) and carboxy-terminal 6, 96 (NUP96) and 88 (p88) kDa peptides (1,2). NUP98 contains FG and GLFG repeat domains at its amino terminus and a RNA-binding domain in its carboxy terminus (3). The NUP98 gene is localized on chromosome 11p15.5, a region frequently rearranged in leukemias. To date, 15 fusion partners have been identified for NUP98 (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Cadherins are a superfamily of transmembrane glycoproteins that contain cadherin repeats of approximately 100 residues in their extracellular domain. Cadherins mediate calcium-dependent cell-cell adhesion and play critical roles in normal tissue development (1). The classic cadherin subfamily includes N-, P-, R-, B-, and E-cadherins, as well as about ten other members that are found in adherens junctions, a cellular structure near the apical surface of polarized epithelial cells. The cytoplasmic domain of classical cadherins interacts with β-catenin, γ-catenin (also called plakoglobin), and p120 catenin. β-catenin and γ-catenin associate with α-catenin, which links the cadherin-catenin complex to the actin cytoskeleton (1,2). While β- and γ-catenin play structural roles in the junctional complex, p120 regulates cadherin adhesive activity and trafficking (1-4). Investigators consider E-cadherin an active suppressor of invasion and growth of many epithelial cancers (1-3). Research studies indicate that cancer cells have upregulated N-cadherin in addition to loss of E-cadherin. This change in cadherin expression is called the "cadherin switch." N-cadherin cooperates with the FGF receptor, leading to overexpression of MMP-9 and cellular invasion (3). Research studies have shown that in endothelial cells, VE-cadherin signaling, expression, and localization correlate with vascular permeability and tumor angiogenesis (5,6). Investigators have also demonstrated that expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers (7,8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: OCRL1 is an inositol 5-phosphatase that selectively dephosphorylates the 5 position of the inositol ring. Its substrates include phosphatidylinositol 4,5-bisphosphate, inositol 1,4,5-trisphosphate, and inositol 1,3,4,5-tetrakisphosphate (1). Research studies indicate that mutations in OCRL1 are linked to Oculocerebrorenal syndrome or Lowe syndrome, an X-linked disorder distinguished by mental retardation and congenital cataracts, as well as Dent's disease (2,3). OCRL1 interacts with several endocytic proteins, including clathrin, AP-2, and RabGTPases (4-7). OCRL1 is localized to the Golgi complex, endosomes, and late stage clathrin-coated pits (6,8). OCRL1 controls early endosome function (8), regulating membrane traffic from endosomes to the Golgi. It is also involved in cytokinesis (9) and cilia assembly (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Oct-1 (POU2F1) is a ubiquitously expressed, octamer-binding transcription factor containing a POU domain with a homeobox subdomain (1). Oct-1 has been shown to interact with several transcription factors in mediating specific gene expression, including SNAPc (2), OBF-1 (a B-cell transcriptional coactivator protein) (3), TFIIB (4), and TBP (TATA-box-binding protein) (5). Its POU DNA-binding domain allows Oct-1 the flexibility to facilitate the binding and recruitment of several tissue-specific cofactors to either positively or negatively regulate a variety of genes, exerting an important role in development (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Oct-4 (POU5F1) is a transcription factor highly expressed in undifferentiated embryonic stem cells and embryonic germ cells (1). A network of key factors that includes Oct-4, Nanog, and Sox2 is necessary for the maintenance of pluripotent potential, and downregulation of Oct-4 has been shown to trigger cell differentiation (2,3). Research studies have demonstrated that Oct-4 is a useful germ cell tumor marker (4). Oct-4 exists as two splice variants, Oct-4A and Oct-4B (5). Recent studies have suggested that the Oct-4A isoform has the ability to confer and sustain pluripotency, while Oct-4B may exist in some somatic, non-pluripotent cells (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Chromatin IP, Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: Oct-4 (POU5F1) is a transcription factor highly expressed in undifferentiated embryonic stem cells and embryonic germ cells (1). A network of key factors that includes Oct-4, Nanog, and Sox2 is necessary for the maintenance of pluripotent potential, and downregulation of Oct-4 has been shown to trigger cell differentiation (2,3). Research studies have demonstrated that Oct-4 is a useful germ cell tumor marker (4). Oct-4 exists as two splice variants, Oct-4A and Oct-4B (5). Recent studies have suggested that the Oct-4A isoform has the ability to confer and sustain pluripotency, while Oct-4B may exist in some somatic, non-pluripotent cells (6,7).

$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).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey

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

Background: SPAK (STE20/SPS1-related Pro/Ala-rich kinase) and OSR1 (oxidative stress responsive 1) are members of the GCK family serine/threonine kinases. Overexpression and in vitro studies demonstrate that SPAK is able to activate p38 MAP kinase indicating a possible role for SPAK in the stress response (1). Yeast two-hybrid screening revealed that SPAK and OSR1 bind to Na-K-2Cl cotransporters NKCC1 and NKCC2 and K-Cl cotransporter KCC3 (2). WNK1 and WNK4 phosphorylate SPAK at Thr243/247 and Ser380 (3-5). Similarly, WNK1 and WNK4 phosphorylate OSR1 at Thr185 and Ser315 (3,4). Phosphorylation at these sites stimulates SPAK and OSR1 activity, leading to NKCC1 phosphorylation and enhanced NKCC1 activity (3-5). SPAK is also phosphorylated at Ser311 by PKCθ in response to T cell activation. Substitution of Ser311 with Ala or specific siRNA knock-down of SPAK dramatically reduces TCR/CD28-induced AP-1 activation, suggesting SPAK is involved in T cell signaling as well (6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein ubiquitination and deubiquitination are reversible processes catalyzed by ubiquitinating enzymes and deubiquitinating enzymes respectively (1,2). Deubiquitinating enzymes (DUBS) are categorized into five subfamilies based on catalytic domain structure: USP, UCH, OTU, MJD, and JAMM. The deubiquitinase cellular zinc-finger anti-NF-κB (Cezanne-1, OTUD7B) is an OTU family deubiquitinase that contains amino-terminal catalytic and ubiquitin-associated (UBA) domains, and a carboxy-terminal A20-like zinc finger (A20-ZnF) that is involved in ubiquitin binding (3,4). Research studies demonstrate that Cezanne-1 negatively regulates canonical NF-κB signaling induced by TNF receptor signaling by removing K63-linked ubiquitin chains from the RIP1 adaptor protein (5,6). Cezanne-1 negatively regulates non-canonical NF-κB signaling through the deubiquitination and stabilization of the TRAF3 signal transduction protein (7). Additional research suggests that Cezanne-1 is a breast cancer oncogene as the corresponding OTUD7B gene is amplified in a subset of breast cancers and enhances EGFR signaling through a mechanism involving receptor stabilization (8).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein ubiquitination and deubiquitination are reversible processes catalyzed by ubiquitinating enzymes (UBEs) and deubiquitinating enzymes (DUBs) (1,2). Five subfamilies of DUBs have been characterized to date, and include USP, UCH, OTU, MJD, and JAMM deubiquitinating enzymes (1,2). The ovarian tumor (OTU) DUB subfamily comprises a group of approximately 100 putative cysteine proteases that are homologous to the Drosophila ovarian tumor gene product (3). OTU domain-containing deubiquitinase with linear linkage specificity (OTULIN, FAM105B, Gumby) is an OTU subfamily deubiquitinating enzyme that antagonizes the E3 linear ubiquitin chain assembly complex (LUBAC) by promoting disassembly of Met1-linked (linear) ubiquitin chains (4,5). LUBAC and OTULIN regulate NOD2 signaling in an antagonistic manner by controlling the level of Met1-ubiquitinated RIPK2 kinase (6). Binding of the OTULIN PUB-interacting motif to the HOIP subunit of LUBAC is critical for OTULIN inhibition of NF-κΒ signaling; this OTULIN-HOIP interaction is negatively regulated by tyrosine phosphorylation of OTULIN (7,8). The ability of OTULIN to influence LUBAC function and the presence of linear ubiquitin chains may play an important role in regulating angiogenesis, craniofacial, and neural development (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Cadherins are a superfamily of transmembrane glycoproteins that contain cadherin repeats of approximately 100 residues in their extracellular domain. Cadherins mediate calcium-dependent cell-cell adhesion and play critical roles in normal tissue development (1). The classic cadherin subfamily includes N-, P-, R-, B-, and E-cadherins, as well as about ten other members that are found in adherens junctions, a cellular structure near the apical surface of polarized epithelial cells. The cytoplasmic domain of classical cadherins interacts with β-catenin, γ-catenin (also called plakoglobin), and p120 catenin. β-catenin and γ-catenin associate with α-catenin, which links the cadherin-catenin complex to the actin cytoskeleton (1,2). While β- and γ-catenin play structural roles in the junctional complex, p120 regulates cadherin adhesive activity and trafficking (1-4). Investigators consider E-cadherin an active suppressor of invasion and growth of many epithelial cancers (1-3). Research studies indicate that cancer cells have upregulated N-cadherin in addition to loss of E-cadherin. This change in cadherin expression is called the "cadherin switch." N-cadherin cooperates with the FGF receptor, leading to overexpression of MMP-9 and cellular invasion (3). Research studies have shown that in endothelial cells, VE-cadherin signaling, expression, and localization correlate with vascular permeability and tumor angiogenesis (5,6). Investigators have also demonstrated that expression of P-cadherin, which is normally present in epithelial cells, is also altered in ovarian and other human cancers (7,8).

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

Application Methods: Western Blotting

Background: Rho family GTPases are key regulators of diverse processes such as cytoskeletal organization, cell growth and differentiation, transcriptional regulation, and cell adhesion/motility. The activities of these proteins are controlled primarily through guanine nucleotide exchange factors (GEFs) that facilitate the exchange of GDP for GTP, promoting the active (GTP-bound) state, and GTPase activating proteins (GAPs) that promote GTP hydrolysis and the inactive (GDP-bound) state (1,2).The p190 RhoGAP proteins are widely expressed Rho family GAPs. p190-A has been characterized as a tumor suppressor, and research studies have shown that loss or rearrangement of the chromosomal region containing the gene for p190-A is linked to tumor development (3,4). p190-A binds the mitogen-inducible transcription factor TFII-I, sequestering it in the cytoplasm and inhibiting its activity. Phosphorylation of p190-A at Tyr308 reduces its affinity for TFII-I, relieving the inhibition (5). p190-A can also inhibit growth factor-induced gliomas in mice (6) and affect cleavage furrow formation and cytokinesis in cultured cells (7).Mice lacking p190-B RhoGAP show excessive Rho activation and a reduction in activation of the transcription factor CREB (8). Cells deficient in p190-B display defective adipogenesis (9). There is increasing evidence that p190 undergoes tyrosine phosphorylation, which activates its GAP domain (9-11). Levels of tyrosine phosphorylation are enhanced by Src overexpression (10,11). IGF-I treatment downregulates Rho through phosphorylation and activation of p190-B RhoGAP, thereby enhancing IGF signaling implicated in adipogenesis (9).

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

Application Methods: Western Blotting

Background: Rho family GTPases are key regulators of diverse processes such as cytoskeletal organization, cell growth and differentiation, transcriptional regulation, and cell adhesion/motility. The activities of these proteins are controlled primarily through guanine nucleotide exchange factors (GEFs) that facilitate the exchange of GDP for GTP, promoting the active (GTP-bound) state, and GTPase activating proteins (GAPs) that promote GTP hydrolysis and the inactive (GDP-bound) state (1,2).The p190 RhoGAP proteins are widely expressed Rho family GAPs. p190-A has been characterized as a tumor suppressor, and research studies have shown that loss or rearrangement of the chromosomal region containing the gene for p190-A is linked to tumor development (3,4). p190-A binds the mitogen-inducible transcription factor TFII-I, sequestering it in the cytoplasm and inhibiting its activity. Phosphorylation of p190-A at Tyr308 reduces its affinity for TFII-I, relieving the inhibition (5). p190-A can also inhibit growth factor-induced gliomas in mice (6) and affect cleavage furrow formation and cytokinesis in cultured cells (7).Mice lacking p190-B RhoGAP show excessive Rho activation and a reduction in activation of the transcription factor CREB (8). Cells deficient in p190-B display defective adipogenesis (9). There is increasing evidence that p190 undergoes tyrosine phosphorylation, which activates its GAP domain (9-11). Levels of tyrosine phosphorylation are enhanced by Src overexpression (10,11). IGF-I treatment downregulates Rho through phosphorylation and activation of p190-B RhoGAP, thereby enhancing IGF signaling implicated in adipogenesis (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunoprecipitation, Western Blotting

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

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

Application Methods: Immunoprecipitation, Western Blotting

Background: p27 Kip1 is a member of the Cip/Kip family of cyclin-dependent kinase inhibitors. Like its relatives, p57 Kip2 and p21 Waf1/Cip1, the ability to enforce the G1 restriction point is derived from its inhibitory binding to CDK2/cyclin E and other CDK/cyclin complexes. Expression levels of p27 are upregulated in quiescent cells and in cells treated with cAMP or other negative cell cycle regulators. Downregulation of p27 can be induced by treatment with interleukin-2 or other mitogens; this involves phosphorylation of p27 and its degradation by the ubiquitin-proteasome pathway (1-4).

$260
200 µl
$630
600 µl
APPLICATIONS
REACTIVITY
Guinea Pig, Human, Monkey, Mouse, Rat

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

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).