124600 Results for: "3+ml+k2edta"

Supplier: VWR International

The VWR® Advanced 3500 Orbital Shaker is designed for a wide range of applications including cell cultures that require accurate and repeatable results. The microprocessor control provides consistent uniform shaking while safely ramping the set speed.

Supplier: Prosci

Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. The ribosomal protein is a component of the 60S subunit. The protein, which is the functional equivalent of the E. coli L10 ribosomal protein, belongs to the L10P family of ribosomal proteins. It is a neutral phosphoprotein with a C-terminal end that is nearly identical to the C-terminal ends of the acidic ribosomal phosphoproteins P1 and P2. The P0 protein can interact with P1 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein, which is the functional equivalent of the E. coli L10 ribosomal protein, belongs to the L10P family of ribosomal proteins. It is a neutral phosphoprotein with a C-terminal end that is nearly identical to the C-terminal ends of the acidic ribosomal phosphoproteins P1 and P2. The P0 protein can interact with P1 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Transcript variants derived from alternative splicing exist; they encode the same protein. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein, which is the functional equivalent of the E. coli L10 ribosomal protein, belongs to the L10P family of ribosomal proteins. It is a neutral phosphoprotein with a C-terminal end that is nearly identical to the C-terminal ends of the acidic ribosomal phosphoproteins P1 and P2. The P0 protein can interact with P1 and P2 to form a pentameric complex consisting of P1 and P2 dimers, and a P0 monomer. The protein is located in the cytoplasm. Transcript variants derived from alternative splicing exist; they encode the same protein. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.

Supplier: Prosci

SMAD1 belongs to the SMAD family. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. SMAD1 mediates the signals of the bone morphogenetic proteins (BMPs), which are involved in a range of biological activities including cell growth, apoptosis, morphogenesis, development and immune responses. In response to BMP ligands, SMAD1 can be phosphorylated and activated by the BMP receptor kinase. The phosphorylated form of SMAD1 forms a complex with SMAD4, which is important for its function in the transcription regulation. SMAD1 is a target for SMAD-specific E3 ubiquitin ligases, such as SMURF1 and SMURF2, and undergoes ubiquitination and proteasome-mediated degradation.The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signals of the bone morphogenetic proteins (BMPs), which are involved in a range of biological activities including cell growth, apoptosis, morphogenesis, development and immune responses. In response to BMP ligands, this protein can be phosphorylated and activated by the BMP receptor kinase. The phosphorylated form of this protein forms a complex with SMAD4, which is important for its function in the transcription regulation. This protein is a target for SMAD-specific E3 ubiquitin ligases, such as SMURF1 and SMURF2, and undergoes ubiquitination and proteasome-mediated degradation. Alternatively spliced transcript variants encoding the same protein have been observed.The protein encoded by this gene belongs to the SMAD, a family of proteins similar to the gene products of the Drosophila gene 'mothers against decapentaplegic' (Mad) and the C. elegans gene Sma. SMAD proteins are signal transducers and transcriptional modulators that mediate multiple signaling pathways. This protein mediates the signals of the bone morphogenetic proteins (BMPs), which are involved in a range of biological activities including cell growth, apoptosis, morphogenesis, development and immune responses. In response to BMP ligands, this protein can be phosphorylated and activated by the BMP receptor kinase. The phosphorylated form of this protein forms a complex with SMAD4, which is important for its function in the transcription regulation. This protein is a target for SMAD-specific E3 ubiquitin ligases, such as SMURF1 and SMURF2, and undergoes ubiquitination and proteasome-mediated degradation. Alternatively spliced transcript variants encoding the same protein have been observed.

Supplier: Prosci

VPREB1 belongs to the immunoglobulin superfamily and is expressed selectively at the early stages of B cell development, namely, in proB and early preB cells. This gene encodes the iota polypeptide chain that is associated with the Ig-mu chain to form a molecular complex which is expressed on the surface of pre-B cells. The complex is thought to regulate Ig gene rearrangements in the early steps of B-cell differentiation.CD179a (VpreB) is a 126 aa-long polypeptide with apparent MW of 16-18 kDa. It is expressed selectively at the early stages of B cell development, namely, in proB and early preB cells. CD179a has an Ig V domain-like structure, but lacks the last beta-strand (beta7) of a typical V domain. Instead, it has a carboxyl terminal end that shows no sequence homologies to any other proteins. CD179a associates non-covalently with CD179b (lambda5 or lambda-like) carrying an Ig C domain-like structure to form an Ig light chain-like structure, which is called the surrogate light chain or pseudo light chain. In this complex, the incomplete V domain of CD179a appears to be complemented by the extra beta7 strand of CD179b. On the surface of early preB cells, CD179a/CD179b surrogate light chain is disulfide-linked to membrane-bound Ig mu heavy chain in association with a signal transducer CD79a/CD79b heterodimer to form a B cell receptor-like structure, so-called preB cell receptor (preBCR). Though no CD179a-related human disease or pathology has been reported yet, the deficiency of other components of preB cell receptor such as CD179b, Ig mu heavy chain and CD79a has been shown to result in severe impairment of B cell development and agammaglobulinemia in human. PreBCR transduces signals for: 1) cellular proliferation, differentiation from the proB cell to preB cell stage, 2) allelic exclusion at the Ig heavy chain gene locus, and 3) promotion of Ig light chain gene rearrangements. Thus, preBCR functions as a checkpoint in early B cell development to monitor the production of Ig mu heavy chain through a functional rearrangement of Ig heavy chain gene as well as the potency of Ig mu heavy chain to associate with Ig light chain. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

Supplier: VWR International

Our VWR® laboratory-grade water purification systems feature an inspiring, application-oriented design. Perform your workflows faster and more reliably, simplifying your daily lab work while ensuring cost-efficient operation over the long term. All instruments offer flexible solutions as they can be adapted to your requirements and integrated into your laboratory environment.

Supplier: Cytiva

Ettan™ IPGphor™ 3 is a fully integrated isoelectric focusing (IEF) system optimized to deliver high throughput, speed, reproducibility and high protein-loading capacity.

Supplier: BD

Urine collection tubes and kits are easy-to-use, and ideal for microbiology and urinalysis applications

Supplier: Rockland Immunochemical

Cell division control protein 42 homolog also known as CDC42 is a protein involved in regulation of the cell cycle. In humans, CDC42 is encoded by the CDC42 gene.CDC42 is a small GTPase of the Rho-subfamily, which regulates signaling pathways that control diverse cellular functions including cell morphology, migration, endocytosis and cell cycle progression. This protein is highly similar to Saccharomyces cerevisiae Cdc 42, and is able to complement the yeast cdc42-1 mutant. The product of oncogene Dbl was reported to specifically catalyze the dissociation of GDP from this protein. This protein could regulate actin polymerization through its direct binding to Neural Wiskott-Aldrich syndrome protein (N-WASP), which subsequently activates Arp2/3 complex. Alternative splicing of this gene results in multiple transcript variants. This antibody is suitable for researchers interested in cell signaling, epigenetics an cancer research.

Supplier: Rockland Immunochemical

BAFF antibody detects human BAFF. Members in the TNF superfamily regulate immune responses and induce apoptosis. A novel member in the TNF family was recently identified by several groups and designated BAFF (for B cell Activating Factor belonging to the TNF Family), BLyS (for B Lymphocyte Stimulator), TALL-1 (for TNF- and ApoL-related Leukocyte-expressed Ligand), and THANK (for TNF Homologue that Activate Apoptosis, NF-alpha;B and c-jun N-terminal Kinase). BAFF/BLyS was characterized as a B cell activator since it induced B cell proliferation and immunoglobulin secretion. Three receptors for BAFF were recently identified and designated TACI, BCMA and BAFF-R. BAFF and its receptors are essential for B cell development, survival, and humoral immune responses. BAFF is involved in the development of autoimmune diseases including systemic lupus erythaematosus and rheumatoid arthritis. Anti-BAFF antibodies are ideal for investigators involved in NFkappaB, Cytokine and Growth Factor research.

Supplier: MP Biomedicals

The complement system provides innate defense against microbial infection and is a "complement" to antibody mediated immunity. The complement system consists of thirty-five interacting plasma and membrane associated proteins which contribute to host-defense and initiate and amplify inflammation, even in the preimmune state where specific antibodies and lymphocytes are not available. In addition to the complement components themselves, this system also contains several soluble factors that prevent spontaneous complement activation from occurring in solution, as well as, several regulatory membrane associated proteins that protect host cells from accidental complement attack. Cleavage of the C3 component by either the classical pathway or the alternative pathway releases C3a and C3b. C3a appears to be important in many inflammatory responses while the C3b fragment covalently binds to the cell or bacterial surface and plays a role in opsonisation. Binding of C3b to the C4b component of the C3 convertase, results in C5 convertase (C4b3b2a) formation.

Supplier: Prosci

This mAb reacts with a 200kDa and 68kDa protein, identified as heavy and light sub-units of neurofilaments (NF-H & NF-L). Neurofilaments make up the main structural elements of axons and dendrites and are found in neurons, peripheral nerves, and sympathetic ganglion cells. Neurofilaments consist of three major subunits with molecular weights of 68kDa (NF-L), 160kDa (NF-M) and 200kDa (NF-H). Anti-neurofilament stains a number of neural, neuroendocrine, and endocrine tumors. Neuromas, ganglioneuromas, gangliogliomas, ganglioneuroblastomas, and neuroblastomas stain positively for anti-neurofilament. Neurofilaments are also present in paragangliomas as well as adrenal and extra-adrenal pheochromocytomas. Carcinoids, neuroendocrine carcinomas of the skin, and cell carcinomas of the lung also express neurofilament.

Supplier: Genetex

The synaptotagmins are integral membrane proteins of synaptic vesicles thought to serve as Ca(2+) sensors in the process of vesicular trafficking and exocytosis. Calcium binding to synaptotagmin participates in triggering neurotransmitter release at the synapse. The first C2 domain mediates Ca(2+)-dependent phospholipid binding. The second C2 domain mediates interaction with Stonin 2. Synaptotagmin may have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.

Supplier: Promega Corporation

The ApoTox-Glo Triplex Assay combines three assay chemistries to easily assess viability, cytotoxicity and apoptosis events in the same cell-based assay well.

Supplier: Rockland Immunochemical

Bst2 was first identified as a novel terminal B-cell-restricted antigen termed HM1.24 that is expressed on certain bone marrow cells as well as other tissues. The surface expression of Bst2 on fibroblast cell lines facilitated the stromal cell-dependent growth of DW34, a pre-B-cell line, suggesting that this protein is involved in pre-B-cell growth. Later experiments also showed it to be upregulated in several myeloma cells. More recently, Bst2 was identified an inhibitor of retroviral release from human cells whose activity is antagonized by the HIV-1 accessory protein Vpu. While Bst2 caused retention of virions on cell surfaces or endocytosis into Bst2-positive compartments, its depletion abolished the viral requirement for Vpu for virus release. This activity may represent a potential therapeutic strategy for the treatment of HIV/AIDS.

Supplier: Rockland Immunochemical

Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. These death signals finally cause the degradation of chromosomal DNA by activated DNase. A mouse DNase that causes DNA fragmentation was identified recently and designated CAD for caspase activated deoxyribonuclease. The human homologue of mouse CAD was more recently identified by three groups independently and termed CPAN, DFF40, and human CAD, respectively. DFF45/ICAD is the inhibitory protein of DFF40/CAD and forms complex with DFF40/CAD. Upon cleavage of DFF45/ICAD by activated caspase, DFF40/CAD is released and activated and eventually causes the degradation of DNA in the nuclei. Activation of DFF40/CAD, which causes DNA degradation, is the hallmark of apoptotic cell death.

Supplier: Rockland Immunochemical

PAKs, p21 activated kinases, are a family of serine/threonine protein kinases comprised of six isoforms, PAK1-6, and they play important roles in cytoskeleton dynamics, cell survival and proliferation. Each of these isoforms contains a C-terminal catalytic domain and an N-terminal regulatory domain with a small G protein binding motif. OSR1, oxidative stress response 1, is activated only by osmotic stresses, like sorbital or NaCl. It has been predicted that OSR1 phosphorylates PAK1 in the regulatory domain at thr84 and inhibits activation of JNK and MAPK pathway. It has also been suggested that OSR1 may have a regulating function with actin cytoskeleton because it can phosphorylate PAK1 at thr84 and bind to gelsolin. PAK1 pT84 Antibody is ideal for researchers interested in cell cycle research.

Supplier: Rockland Immunochemical

CARMA proteins belong to the membrane-associated guanylate kinase-like (MAGUK) family of proteins that can function as molecular scaffolds that assist assembly of signal transduction molecules. CARMA1, CARMA2, and CARMA3 share high degrees of sequence and functional homology, but their tissue-specific distribution suggests that they serve distinct biological functions in different cell types. As with CARMA1, the CARD domain of CARMA3 has been shown to specifically interact with BCL10, a protein known to function as a positive regulator of cell apoptosis and NF-kB activation. When expressed in cells, this protein binds to BCL10 and activates NF-kB Recent experiments have shown that CARMA3 is required for EGF-induced NF-kB activation and contributes to tumor growth in vivo, suggesting that CARMA3 may serve as a new therapeutic target for the treatment of EGFR-driven tumors.

Supplier: Rockland Immunochemical

Adipose tissue of an organism plays a major role in regulating physiologic and pathologic processes such as metabolism and immunity by producing and secreting a variety of bioactive molecules termed adipokines. One highly conserved family of adipokines is adiponectin/ACRP30 and its structural and functional paralogs, the C1q/tumor necrosis factor-alpha-related proteins (CTRPs) 1-7. Unlike adiponectin, which is expressed exclusively by differentiated adipocytes, the CTRPs are expressed in a wide variety of tissues. These proteins are thought to act mainly on liver and muscle tissue to control glucose and lipid metabolism. An analysis of the crystal structure of adiponectin revealed a structural and evolutionary link between TNF and C1q-containing proteins, suggesting that these proteins arose from a common ancestral innate immunity gene. CTRP5 has been suggested to be involved in age-related macular degeneration.

Supplier: MP Biomedicals

Arachidonic Acid is an essential fatty acid. Occurs in liver, brain, glandular organs, and depot fats of animals, in small amounts in human depot fats, and is a constituent of animal phosphatides.
Arachidonic Acid is a precursor in the biosynthesis of prostaglandins, thromboxanes, and leukotrienes. Arachidonic acid plays a key role in cellular regulation and is controlled through multiple interconnected pathways.
Arachidonic acid (AA) is an unsaturated ω6 fatty acid constituent of the phospholipids of cell membranes. Phospholipase A2 releases AA from the membrane phospholipids in response to inflammation. AA is subsequently metabolized to prostaglandins and thromboxanes by at least two cyclooxygenase (COX) isoforms, to leukotrienes and lipoxins by lipoxygenases, and to epoxyeicosatrienoic acids via cytochrome p450-catalyzed metabolism. AA and its metabolites play important roles in a variety of biological processes, including signal transduction, smooth muscle contraction, chemotaxis, cell proliferation and differentiation, and apoptosis. AA has been demonstrated to bind to the a subunit of G protein and inhibit the activity of Ras GTPase-activating proteins (GAPs). Cellular uptake of AA is energy dependent and involves protein-facilitated transport across the plasma membrane.
If ethanol is undesirable, arachidonic acid may be dissolved in acetonitrile, DMF, or DMSO. Simply evaporate the ethanol under a gentle stream of nitrogen (be certain not to evaporate the material to dryness) and redissolve the arachidonic acid in the solvent of choice.Just prior to use, make dilutions of the stock solution into aqueous buffer or isotonic saline to bring the arachidonic acid to the desired concentration. Ensure that the residual amount of organic solvent is insignificant, since organic solvents may have physiologic effects at low concentrations. A control using the solvent in the absence of the prostaglandin will address this potential variable. We do not recommend storing the aqueous solution for more than one day. It is difficult to obtain aqueous solutions of arachidonic acid directly. However, an organic solvent free solution of arachidonic acid can be prepared using concentrated basic buffers (pH > 8.0 and ionic strength not less than 0.1 M). Add 400 μL of cold buffer (0 °C) per mg of arachidonic acid and agitate vigorously and/or ultrasonicate.

Supplier: VWR International

The VWR® Advanced 3500 Orbital Shaker is designed for a wide range of applications including cell cultures that require accurate and repeatable results. The microprocessor control provides consistent uniform shaking while safely ramping the set speed.

Supplier: Prosci

CCL4 Antibody: CCL4, also known as macrophage inflammatory protein 1-beta (MIP1B), belongs to the intercrine beta (chemokine CC) family. Both CCL4 and the related protein CCL3 participate in the host response to invading bacterial, viral, parasite and fungal pathogens by regulating the trafficking and activation state of selected subgroups of inflammatory cells. While both CCL4 and CCL3 exert similar effects on monocytes, their effect on lymphocytes differ; with CCL4 selectively attracting CD4+ lymphocytes and CCL3 selectively attracting CD8+ lymphocytes. Additionally, both have been shown to be potent chemoattractants for B cells, eosinophils and dendritic cells. The processed form of CCL4 can induce down-modulation of surface expression of the chemokine receptor CCR5, thus inhibiting the CCR5-mediated entry of HIV-1 in T cells.

Supplier: Rockland Immunochemical

Human immunodeficiency virus (HIV) and related virus require coreceptors to infect target cells. Some G protein-coupled receptors including CCR5, CXCR4, CCR3, CCR2b, CCR8, GPR15, STRL33, and CX3CR1 in the chemokine receptor family were recently identified as HIV coreceptors. CCR5, CXCR4 and CCR3 are the principal receptors for HIV fusion and entry of target cells. CCR3 facilitates infection by a subset of virus. CCR3 and CCR5 promote efficient infection of microglia, the major target cells in the CNS. High levels of CCR3 and CXCR4 expression were found on the neurons from both the central and peripheral nervous systems. The CCR3 ligand, eotaxin, and an anti-CCR3 antibody inhibited HIV infection of microglia. These results indicate CCR3 plays an important role in HIV infection of CNS.

Supplier: Rockland Immunochemical

B-raf belongs to the raf/mil family of serine/threonine protein kinases and plays a role in regulating the MAP kinase/ERKs signaling pathway, which affects cell division, differentiation, and secretion. The Ras/Raf/MEK/ERK and Ras/PI3K/PTEN/Akt pathways interact with each other to regulate growth and in some cases tumorigenesis. Mutations in B-raf have been associated with several cancers, including non-Hodgkin lymphoma, colorectal cancer, malignant melanoma, thyroid carcinoma, non-small cell lung carcinoma, and adenocarcinoma of lung, leading to speculation on the possibility of B-raf as a therapeutic target for treating cancers. Mutations in this gene have also been associated with cardiofaciocutaneous syndrome (CFCS), a disease characterized by heart defects, mental retardation and a distinctive facial appearance.

Supplier: DRG International

An enzyme immunoassay for the quantitative determination of caridac specific troponin I in serum.

Supplier: Omega Bio-Tek

100ml.

Supplier: Electron Microscopy Sciences

Hard-Plus Resin-812 is supplied only as a premix kit

Supplier: BioVendor

Urocortin 3 (Ucn3) or stresscopin (SCP) is a new member of the corticotropin-releasing factor (CRF) peptide family identified in the mouse and human

Supplier: Diagnostic Biosystems

Glypican-3 (GPC3) is a glycosylphospatidyl inositol-anchored membrane protein, which may also be found in a secreted form. Anti-GPC3 has been identified as a useful tumor marker for the diagnosis of hepatocellular carcinoma (HCC), hepatoblastoma, melanoma, testicular germ cell tumors, and Wilms' tumor. In patients with HCC, GPC3 is overexpressed in neoplastic liver tissue and elevated in serum, but is undetectable in normal liver, benign liver, and the serum of healthy donors. GPC3 expression is also found to be higher in HCC liver tissue than in cirrhotic liver or liver with focal lesions such as dysplastic nodules and areas of hepatic adenoma (HA) with malignant transformation. In the context of testicular germ cell tumors, GPC3 expression is up regulated in certain histologic subtypes, specifically yolk sac tumors and choriocarcinoma. A high level of GPC3 expression is also found in some types of embryonal tumors, such as Wilms' tumor and hepatoblastoma, with a low or undetectable expression in normal adjacent tissue. In patients with thyroid cancer, expression of GPC3 is dramatically enhanced in certain types of cancers: 100% in follicular carcinoma and 70% in papillary carcinoma. Expression of GPC3 in follicular carcinoma is significantly higher than that offollicular adenoma.

Supplier: Prosci

This antibody detects a monomorphic general framework determinant of HLA-DR Class II antigen. It does not cross react with HLA-DP and HLA-DQ. HLA-DR is a heterodimeric cell surface glycoprotein comprised of a 36kDa alpha (heavy) chain and a 28kDa beta (light) chain. It is expressed on B-cells, activated T-cells, monocytes/macrophages, dendritic cells and other non-professional APCs. In conjunction with the CD3/TCR complex and CD4 molecules, HLA-DR is critical for efficient peptide presentation to CD4+ T cells. It is an excellent histiocytic marker in paraffin sections producing intense cytoplasmic staining. True histiocytic neoplasms are similarly positive. HLA-DR antigens also occur on a variety of epithelial cells and their corresponding neoplastic counterparts.

Supplier: Prosci

Recognizes a protein of 40kDa, identified as CD7 (Workshop IV; Code T155). CD7 is a member of the immunoglobulin gene superfamily. Its N-terminal amino acids 1-107 are highly homologous to Ig kappa-L chains whereas the carboxyl-terminal region of the extracellular domain is proline-rich and has been postulated to form a stalk from which the Ig domain projects. CD7 is expressed on the majority of immature and mature T-lymphocytes, and T cell leukemia. It is also found on natural killer cells, a small subpopulation of normal B cells and on malignant B cells. Cross-linking surface CD7 positively modulates T cell and NK cell activity as measured by calcium fluxes, expression of adhesion molecules, cytokine secretion and proliferation. CD7 associates directly with phosphoinositol 3'-kinase. CD7 ligation induces production of D-3 phosphoinositides and tyrosine phosphorylation.