1510 Results for: "assay 6-50"

Supplier: Genetex

Superoxide dismutase (SOD) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells. They are: extracellular SOD (EC SOD), copper and zinc-containing SOD (CuZn SOD) and manganese-containing SOD (Mn SOD). The CuZn form contains Cu and Zn ions and exists as a 32 kDa dimer in the cytosol. Mn SOD is an 80 kDa tetramer that contains Mn ion and resides in the mitochondrial matrix. Mn SOD is a tumor necrosis factor (TNF)- inducible enzyme that protects cells from TNF-mediated apoptosis via superoxide anion detoxification and the subsequent regulation of apoptosis through cytochrome c release and the modulation of the redox state of the mitochondria. Mn SOD has also been shown to be a tumor suppressor in human breast cancer. Overexpression of this enzyme protects neurons from NMDA- and nitric oxide-induced neurotoxicity.

Supplier: Genetex

Mouse monoclonal [24612.111] to HGF

Supplier: Genetex

Goat polyclonal to HGF

Supplier: MP Biomedicals

Thrombin is the final coagulation protease in regard to hemostasis, promoting both procoagulant and anticoagulant effects. It is a lyophilized powder containing sucrose, sodium chloride and Tris. The predominant form of thrombin in vivo is the zymogen, prothrombin (factor II), which is produced in the liver. The concentration of prothrombin in normal human plasma is 5–10 mg/dL. Prothrombin is a glycoprotein with a glycan content of ~12%.

Supplier: Shenandoah Biotechnology

Basic fibroblast growth factor (bFGF), also known as FGF2, is expressed by endothelial cells and is a mediator of angiogenesis. bFGF also has cardioprotective functions during heart injury. The application of bFGF is a critical component for embryonic stem cell culture systems and is necessary for maintaining cells in an undifferentiated state. Degredation of the full length bFGF N-terminus results in a truncated bFGF147aa protein, when the protein is isolated from biological sources. The N-terminus extensions influence the localization of bFGF within the cell, but do not affect the biological activity of bFGF. Therefore, there are no detectable differences in biological activity between the full length bFGF-154aa and the truncated bFGF-147aa recombinant proteins.

Supplier: Shenandoah Biotechnology

Basic fibroblast growth factor (bFGF), also known as FGF2, is expressed by endothelial cells and is a mediator of angiogenesis. bFGF also has cardioprotective functions during heart injury. The application of bFGF is a critical component for embryonic stem cell culture systems and is necessary for maintaining cells in an undifferentiated state. Degredation of the full length bFGF N-terminus results in a truncated bFGF147aa protein, when the protein is isolated from biological sources. The N-terminus extensions influence the localization of bFGF within the cell, but do not affect the biological activity of bFGF. Therefore, there are no detectable differences in biological activity between the full length bFGF-154aa and the truncated bFGF-147aa recombinant proteins.

Supplier: Biotium

Biotium’s DNA Gel Extraction Kit is a silica-gel, spin column based DNA extraction kit.

Supplier: Genetex

Bassoon is a 420 kDa protein that is a localized at the presynaptic nerve terminals and is believed to play a role in the structural and functional organization of the synaptic vesicle cycle. Bassoon does not belong to any known protein families. It has been found in rat and mouse with sequence identity of the two proteins at 96%. The human BASSOON gene has recently been cloned and localized. Bassoon is predicted to contain two double-zinc fingers, three coiled-coil regions, and two polyglutamine domains. The polyglutamine domains in the C-terminus are of interest, since it is known that for some human proteins, such as Huntingtin, abnormal amplification of this region can cause late-onset neurodegeneration. Bassoon is concentrated at sites opposite to postsynaptic densities in synaptic terminals and in cultured neurons, it is found to colocalize with GABA (A) and glutamate (GluR1) receptors.Another presynaptic protein, Piccolo was found to colocalize with Bassoon in cultured hippocampal neurons. These observations suggested that they serve specific functions at synaptic junctions and may be involved in organization of the cytoskeleton at the site of neurotransmitter release.

Supplier: Genetex

Lysosomal enzymes containing one or two mannose 6-phosphate (man6P) moieties are moved about in the cell by two distinct but interconnected cycles by means of 300 kDa cation-independent mannose 6-phospate receptors (MPR). MPR cycles and transports newly synthesized lysosomal enzymes between the TGN and late endosomes / early lysosomes. It also cycles and transports extracellular lysosomal enzymes between the plasma membrane and early endosomes via clathrin coated vesicles. The bulk of the MPR protein is in the extracellular/lumenal domain. The entire pool of MPRs cycles between these cellular compartments every 3 hours. The steady state distribution of MPR's is predominantly within late endosomes, fewer in the trans Golgi network and ~5-10 % at the cell surface. In addition to its man6P binding activity, the MPR contains a separate binding site for the type II insulin-like growth factor and is capable of binding both man6P and IGF-II simultaneously. An ~240 kDa soluble, truncated form, representing the extracellular domain of the protein, has also been found circulating in serum and is capable of binding both ligands.

Supplier: Genetex

Superoxide dismutase (SOD) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells. They are: extracellular SOD (EC SOD), copper and zinc-containing SOD (Cu/Zn SOD) and manganese-containing SOD (Mn SOD). The Cu/Zn form contains Cu and Zn ions and exists as a 32 kDa dimer in the cytosol. Mn SOD is an 80 kDa tetramer that contains Mn ion and resides in the mitochondrial matrix. Mn SOD is a tumor necrosis factor (TNF)-inducible enzyme that protects cells from TNF-mediated apoptosis via superoxide anion detoxification and the subsequent regulation of apoptosis through cytochrome c release and the modulation of the redox state of the mitochondria. Mn SOD has also been shown to be a tumor suppressor in human breast cancer. Overexpression of this enzyme protects neurons from NMDA- and nitric oxide-induced neurotoxicity.

Supplier: Zymo Research

Quick (2 minute) recovery of ultra-pure DNA and RNA oligonucleotides.

Supplier: Genetex

The description of specific intranuclear structures known today as Cajal bodies was first published in 1903 by the neuro-cytologist Ramon-y-Cajal. He observed that neurons stained with silver contained spherical structures of around 0.5 micron in diameter that were often associated with nucleoli and called them nucleolar accessory bodies. Later, the same bodies were called coiled bodies since when these structures were viewed by electron microscopy, they resembled a tangle of coiled threads. It was found that patients with autoantibodies against coiled bodies recognize a protein of 80 kDa termed p80-coilin. Using these antibodies, coiled bodies were identified in plants, flies, frogs, birds, and mammals. The gene encoding p80-coilin has been cloned and sequenced. It contains two nuclear localization sequences (NLS) (at amino acid 107-112 and 181-198) and several serine residues that are phosphorylated in vivo. Mutating Serine-202 to Aspartate causes the disappearance of coiled bodies and a redistribution of coilin to intranucleolar domains. Nuclear antigens shown to colocalize with p80 coilin in Cajal bodies include basal transcription factors, cell cycle factors (cdks), splicing snRNPs and nucleolar factors including snoRNPs.

Supplier: Genetex

Arginine methylation is an irreversible post translational modification which has only recently been linked to protein activity. At least three types of PRMT enzymes have been identified in mammalian cells. These enzymes have been shown to have essential regulatory functions by methylation of key proteins in several fundamental areas. These protein include nuclear proteins (Histone 2A, 3, 4), IL enhancer binding factor, nuclear factors (NF45, 90, ILF3, Nucleolin, STAT1, Poly(A) binding protein II), cell cycle proteins (phosphoprotein phosphatase 2A), signal transduction proteins (FGF2, Fibrillarin, FN, INFAR1, Jak, MBP, Src-adaptor Sam68), apoptosis proteins (FADD, ICE-like protease), and viral proteins (Hepatitis C NS3 RNA Helicase, HIV TAR). The mammalian PRMT family currently consists of 5 members that share two large domains of homology. Outside of these domains, epitopes were identified and antibodies against all five PRMT members have been developed. These antibodies can be utilized to explore arginine methylation and its regulatory functions.

Supplier: Genetex

The serum amyloid A (SAA) family comprises a number of differentially expressed lipoproteins, acute-phase SAA1 and SAA2, the former being a major component in plasma, and constitutive SAA's (C-SAAs). Although the liver is the primary site of synthesis of both SAA types, extrhepatic production has been reported. The in-vivo concentrations increase by as much as 1000 fold during inflammation. Several studies have expressed it's importance in the diagnosis and monitoring of various diseases. Pathological SAA values are often detected in association with normal CRP concentrations. SAA rises earlier and more sharply than CRP.SAA enhances the binding of HDL's to macrophages and thus helps the delivery of lipid to sites of injury for use in tissue repair. It is thus thought to be an integral part of the disease process. In addition, recent experiments suggest that SAA may play a "houekeeping" role in normal human tissues.Elevated levels of SAA over time predispose secondary amyloidosis, extracellular accumulation of amyloid fibrils, derived from a circulating precursor, in various tissues and organs. The most common form of amyloidosis occurs secondary to chronic inflammatory disease, particularly rheumatoid artheritis.

Supplier: Genetex

RAS proteins are signal-transducing, guanine nucleotide-binding proteins that appear to function as a branchpoint in signal transduction. RAS coordinates the activity of multiple signalling pathways, regulating diverse cellular functions including cell growth, differentiation and apoptosis. The human RAS gene family consists of three identified members which encode proteins of 21 kDa. Human cH RAS and cK RAS are the cellular homologs of vH- and vK RAS originally isolated from Harvey and Kirsten strains of rat sarcoma viruses. The third family member is designated cN RAS. Normal cellular ras genes are referred to as protooncogenes and have the potential for activation to oncogenes by mutations occurring in codons 12, 13 and 61. Such mutated, activated and transforming ras genes have been identified and isolated from human tumors and cultured tumor cells. Although the expression patterns of ras proto-oncogene proteins in normal human tissues are known, similar information for activated ras oncogene encoded p21s and their relevance to human disease diagnosis and prognosis remains to be determined.

Supplier: Enzo Life Sciences

CaMKIIa, the alpha subunit of Ca2+ calmodulin-dependent protein kinase II is part of a family of multifunctional protein kinases, which play a major role in Ca2+-mediated signal transduction.  CaMKIIa is expressed in many different tissues but is specifically found in the neurons of the forebrain and its mRNA is found within the dendrites as well as the soma of the neuron.  The neuronal CaMKII consists of two major subunits of 52 and 60 kDa which are encoded by a- and b-CaMKII genes, respectively.  Additional isoforms are generated by alternative splicing of these as well as of the ubiquitious g- and d-CaMKII genes.  Each subunit has an ATP-binding domain (arginine-X-X-serune/threonine), consensus phosphorylation site, catalytic domain, and a centrally located regulatory domain which has calmodulin binding activity. Activation and autophosphorylation of CaMKII may regulate numerous neuronal processes which includes two forms of synaptic plasticity, long term potentiation and long term depression.  Neuronal CaMKII subunits assemble as large multimeric holoenzymes.  The C-terminal association domains of  6-12 subunits assemble into a central globular structure from which the N-terminal catalytic/regulatory domains extend radially like petals of a flower. The subunit composition of the rat forebrain CaMKII holoenzyme consists of heteromers composed of a and β subunits at a ratio of 2:1 and homomers composed of only a subunits.  The association of CaMKII subunits leads to the positioning of their catalytic/regulatory domains in close proximity and the neighboring calmodulin-bound subunits cooperate to rapidly phosphorylate each other.  Autophosphorylation also enables CaMKII to attain an enhanced affinity for NMDA receptors in postsynaptic densities.

Supplier: Genetex

Myosin is the major component of thick muscle filaments, and is a long asymmetric molecule containing a globular head and a long tail. The molecule consists of two heavy chains each ~200,000 daltons, and four light chains each ~16,000 - 21,000 daltons. Activation of smooth and cardiac muscle primarily involves pathways that increase calcium levels and myosin phosphorylation, resulting in contraction. Myosin light chain phosphatase acts to regulate muscle contraction by dephosphorylating activated myosin light chain. This antibody is specific for the phosphorylated form of myosin light chain. The selected peptide sequence used to generate the polyclonal antibody is located near the amino terminal end of the polypeptide corresponding to the smooth/non-muscle form of myosin regulatory light chain found in cardiac myocytes in addition to smooth and non-muscle cells. This sequence differs from that of the sarcomeric/cardiac form of myosin regulatory light chain that has a different sequence around the phosphorylation site. Human and mouse have almost identical sequences. In human the phosphorylation site is pS19, while in mouse the site maps to pS20.

Supplier: Genetex

This gene encodes coagulation factor XII which circulates in blood as a zymogen. This single chain zymogen is converted to a two-chain serine protease with an heavy chain (alpha-factor XIIa) and a light chain. The heavy chain contains two fibronectin-type domains, two epidermal growth factor (EGF)-like domains, a kringle domain and a proline-rich domain, whereas the light chain contains only a catalytic domain. On activation, further cleavages takes place in the heavy chain, resulting in the production of beta-factor XIIa light chain and the alpha-factor XIIa light chain becomes beta-factor XIIa heavy chain. Prekallikrein is cleaved by factor XII to form kallikrein, which then cleaves factor XII first to alpha-factor XIIa and then to beta-factor XIIa. The active factor XIIa participates in the initiation of blood coagulation, fibrinolysis, and the generation of bradykinin and angiotensin. It activates coagulation factors VII and XI. Defects in this gene do not cause any clinical symptoms and the sole effect is that whole-blood clotting time is prolonged. [provided by RefSeq]

Supplier: Scientific Industries

Space-saving multi-action platform rotator/rocker produces six different mixing motions: rotating, rotating/rocking, rotating/rolling, rolling/rocking, and rocking/shaking, as well as a combination of all of these.

Supplier: Restek

Designed and intended specifically for use on LC-MS/MS systems, the Raptor™ ARC-18 column offers a well-balanced retention profile without the drawbacks of using an ordinary C18 in the harsh, acidic mobile phases needed for mass spectrometry (MS).

Supplier: Corning

PP, graduated. The DeckWorks™ system is designed to maximize storage space and help reduce the production and waste of plastic materials. Both the hinged racks and reload decks within this system are manufactured with recycled plastic.

Supplier: Prosci

Since their discovery in the early 1990's, the peroxisome proliferator activated receptors (PPARs) have attracted significant attention. This is primarily because PPARs serve as receptors for two very important classes of drugs: the hypolipidemic fibrates and the insulin sensitizing thiazolidinediones. Peroxisome proliferators are non-genotoxic carcinogens that are purported to exert their effect on cells through their interaction with members of the nuclear hormone receptor family termed PPARs. Nuclear hormone receptors are ligand-dependent intracellular proteins that stimulate transcription of specific genes by binding to specific DNA sequences following activation by the appropriate ligand. Upon binding fatty acids or hypolipidemic drugs, PPARs form heterodimers with retinoid X receptors (RXRs) and these heterodimers regulate the expression of target genes. There are 3 known subtypes of PPARs: PPAR-alpha, PPAR-delta and PPAR-gamma. Mostly target genes are involved in the catabolism of fatty acids. Conversely, PPAR-gamma is activated by peroxisome proliferators such as prostaglandins, leukotrienes and anti-diabetic thiazolidinediones and affects the expression of genes involved in the storage of the fatty acids. PPAR-gamma may also be involved in adipocyte differentiation. It has also been shown that PPARs can induce transcription of acyl coenzyme A oxidase and cytochrome P450 through interaction with specific response elements.

Supplier: Greiner Bio-One

Made of polycarbonate or polystyrene resin, these lids are best suited for chimney-well style 96-well plates in cell culture applications.

Supplier: Genetex

Agrin is an essential extracellular matrix component which promotes clustering of nicotinic acetylcholine receptors (nAChRs) and other proteins during development at the neuromuscular junction. Agrin, MuSK and Rapsyn are all essential components for AChR aggregation, through an unknown mechanism. The C-terminal region of agrin is released into the medium, interacts with receptors on the muscle surface and induces AChR aggregation. The central region contains two O-linked glycosylation sites and a domain homologous to domain III of laminin. The N-terminal region anchors agrin to the extracellular matrix via other basal membrane components. This region also contains a protease inhibitor domain and glycosaminoglycan attachment sites; increasing the predicted MW from 200kDa to ~600kDa.

Supplier: Genetex

The INK4a-ARF locus is comprised of two tumor suppressors, p16INK4a and p14ARF. These two proteins are encoded through differential splicing of alternative first exons. The p16INK4a (exon 1alpha) protein inhibits the cyclin D-dependent kinases (CDK) that control the phosphorylation of the Rb protein and cell proliferation. The p14ARF gene product complexes with the MDM2 protein within the nucleus, thus modulating the activity of the p53 protein. P14ARF is a potent tumor suppressor in the presence of wild-type p53, while mutant p53 substantially reduces growth inhibition by p14ARF.

Supplier: Genetex

BRCA1 (breast and ovarian cancer susceptibility protein 1) is a RING finger protein containing a BRCT domain. BRCA1 exists as a heterodimer with 22 possible isoforms. The full length protein has a reported molecular weight of 208 kD. BRCA1 localizes to the mitotic spindle microtubules, centriole walls, pericentriolar fibers at centrosomes. Unphosphorylated BRCA1 localizes on chromosomes from metaphase through telophase; phosphorylated BRCA1 resides in inner chromosomal structure, centrosome, cleavage furrow during prophase through telophase, and relocalizes to the perinuclear region when cells are subjected to IR or UV radiation in S phase. BRCA1 acts as a tumor suppressor and can function as a secreted growth inhibitory protein, participate in transcription coupled repair of oxidative DNA damage, X-chromosome inactivation, and can function as a E3 ubiquitin ligase. BRCA1 can be transcriptionally downregulated by Ets-2, Brg-1, and Hmga-1. BRCA1 can be modified by glycosylation, ubiquitination and phosphorylation by CDK4, ATM/ATR, cdk2, and hChk2. The BRCA1 protein has been reported to interact with RNA polymerase II holoenzyme and BARD1. BRCA1 contains at least two nuclear localization signals and is proposed to be a tumor suppressor protein. It is a serine phosphoprotein that undergoes hyperphosphorylation during late G1 and S phases of the cell cycle and is transiently dephosphorylated early after M phase. BRCA1 protein alters in a qualitative and quantitative manner during cell cycle progression. The amount of BRCA1 protein is highest during S phase and remains elevated toward G2 / M, before it declines in early G1 phase. Inherited loss of BRCA1 function confers an increased susceptibility for both breast and ovarian cancer.

Supplier: IBI Scientific

IBI's Viral Nucleic Acid Extraction Kit was designed specifically for purification of viral DNA/RNA from cell-free samples; such as serum, plasma, body fluids, and the supernatant of viral infected cell cultures

Supplier: Genetex

BRCA1 (breast and ovarian cancer susceptibility protein 1) is a RING finger protein containing a BRCT domain. BRCA1 exists as a heterodimer with 22 possible isoforms. The full length protein has a reported molecular weight of 208 kD. BRCA1 localizes to the mitotic spindle microtubules, centriole walls, pericentriolar fibers at centrosomes. Unphosphorylated BRCA1 localizes on chromosomes from metaphase through telophase; phosphorylated BRCA1 resides in inner chromosomal structure, centrosome, cleavage furrow during prophase through telophase, and relocalizes to the perinuclear region when cells are subjected to IR or UV radiation in S phase. BRCA1 acts as a tumor suppressor and can function as a secreted growth inhibitory protein, participate in transcription coupled repair of oxidative DNA damage, X-chromosome inactivation, and can function as a E3 ubiquitin ligase. BRCA1 can be transcriptionally downregulated by Ets-2, Brg-1, and Hmga-1. BRCA1 can be modified by glycosylation, ubiquitination and phosphorylation by CDK4, ATM/ATR, cdk2, and hChk2. The BRCA1 protein has been reported to interact with RNA polymerase II holoenzyme and BARD1. BRCA1 contains at least two nuclear localization signals and is proposed to be a tumor suppressor protein. It is a serine phosphoprotein that undergoes hyperphosphorylation during late G1 and S phases of the cell cycle and is transiently dephosphorylated early after M phase. BRCA1 protein alters in a qualitative and quantitative manner during cell cycle progression. The amount of BRCA1 protein is highest during S phase and remains elevated toward G2 / M, before it declines in early G1 phase. Inherited loss of BRCA1 function confers an increased susceptibility for both breast and ovarian cancer.

Supplier: Genetex

Goat polyclonal antibody to IFN gamma

Supplier: VWR

VWR® Phenol-FreeTotal RNA Purification Kit provides a rapid method for the isolation and purification of total RNA from cultured animal cells, tissue samples, blood, bacteria, yeast, fungi, plants and viruses.