1653 Results for: "assay 11-50"

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 (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: 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

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: Prosci

CD254, also known as RANKL, TNFSF11, TRANCE, OPGL and ODF, is a type II membrane protein of the tumor necrosis factor (TNF) superfamily, and affects the immune system and control bone regeneration and remodeling. RANKL is the ligand of nuclear factor (NF)-κB (RANK). When RANKL binds to RANK, it will undergo trimerization and then bind to an adaptor molecule TNF receptor-associated factor 6 (TRAF6). This results in the activation of several downstream signaling cascades, including the NFκB, mitogen-activated protein kinases (MAPK), activating protein 1 (AP-1), and nuclear factor of activated T cells (NFATc1), resulting in the formation of multinucleated bone-resorbing osteoclasts. RANKL is widely expressed in skeletal muscle, thymus, liver, colon, small intestine, adrenal gland, osteoblast, mammary gland epithelial cells, prostate and pancreas.

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: 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: 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: 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: 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

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: 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: 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

Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.

Supplier: Genetex

Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.

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.

Supplier: VWR International

VWR® 96 Sample Purification System is a high throughput, automated system that improves the efficiency and reproducibility of magnetic bead-based purification protocols.

Supplier: Genetex

The RNAs that direct protein synthesis in animals and plant cells are synthesized in the nucleus as large precursors (pre-mRNAs). The protein coding sequences in pre-mRNA molecules are arranged in discontinuous segments - exons interspersed with noncoding sequences - introns. In a process termed splicing, these introns are efficiently removed before the pre-mRNA is transported from the nucleus to the cytoplasm, where it is translated into protein. Studies have shown that nuclear pre-mRNA splicing takes place in a multi-component structure termed a spliceosome. The polypyrimidine tract-binding (PTB) protein-associated splicing factor (PSF), which plays an essential role in mammalian spliceosomes, is a ubiquitous nuclear matrix protein. A complex between PTB and PSF is necessary for pre-mRNA splicing. PSF contains two consensus RNA-binding domains and an unusual amino terminus rich in proline and glutamine residues. The RNA-binding properties of PSF are apparently identical to those of PTB. Both proteins, together and independently, bind the polypyrimidine tract of mammalian introns. However, the nuclear localization of PSF and PTB and their distribution in subnuclear fractions differ markedly: isolated nuclear matrices contain a bulk of PSF, but only minor amounts of PTB. In confocal microscopy both proteins appear in speckles, the majority of which do not co-localize. These PTB/PSF complexes, as well as the observed PSF-PTB interaction, may reflect the presence of PTB and PSF in spliceosomal complexes during RNA processing, although other data point to different cellular distribution and nuclear matrix association of the majority of PSF and PTB. The cleavage of PSF during lysis of immature myeloid cells is accompanied by digestion of the PTB splicing regulator but not other proteins tested. In contrast, during apoptosis PTB is degraded while PSF remains intact. Proteolytic degradation of PSF specifically occurs in intact myeloid cells and this process is enhanced upon immature myeloid cell lysis; PSF is completely cleaved to a 47 kDa proteolytic cleavage product (p47), due to potent proteolytic activity found in these cells but rare in other cells and tissues. Furthermore, p47 is abundant in intact normal and tumor myeloid cells while in other cell types it is undetectable. The bone marrow 47 kDa protein is a fragment constituting the N-terminal, protease-resistant half of the splicing factor PSF. PSF is highly basic and migrates anomalously on SDS gels. The 47 kDa protein of mouse cells of immature myeloid origin (bone marrow and acute myeloid leukemia) exhibits a gel migration pattern corresponding to a 49 kDa molecule. In other cell types such as lymphoid cells and in peripheral blood cells, PSF appears as approx. 100 kDa or 75 kDa molecules. The sequence of a fragment of mouse PSF was found to be remarkably similar to that of human PSF ( > 98% homology). Also, the sequences of PSF and the human (h) 100 kDa DNA-pairing protein (hPOMp100) reveals identity. Homologous pairing is a fundamental biological reaction implicated in various cellular processes such as DNA recombination and repair, chromosome pairing, sister chromatid cohesion and chromosome condensation, gene inactivation and initiation of replication. The base pairing is also involved in spliceosome assembly resulting in formation of a dynamic Holliday-like structure within which splicing occurs. Indeed, PSF/hPOMp100 bind both singlestranded (ss) and double-stranded (ds) DNA and facilitates the renaturation of complementary ssDNA molecules. Importantly, PSF/hPOMp100 promotes the formation of D-loops in superhelical duplex DNA. PSF/hPOMp100 also serves as an efficient substrate for protein kinase C (PKC) in vitro. PKC phosphorylation of PSF/hPOMp100 stimulates its DNA binding and D-loop formation activity suggesting a possible regulatory mechanism. PSF has been demonstrated to interact with a variety of cellular targets including the human pro-oncoproteins EWS, hPOMp75/TLS and calmodulin, the RNA/DNAbinding nuclear protein p54nrb/NonO (the homolog of PSF) and DNA topoisomerase. A direct interaction has been observed, between PSF and topoisomerase I which has been implied in DNA recombination, DNA repair, and chromosome formation and may act as a transcription factor and a protein kinase. PSF is also expressed by differentiating neurons in developing mouse brain. Both the expression of PSF mRNA in cortex and cerebellum and PSF immunoreactivity in all brain areas has been found to be high during embryonic and early postnatal life. In adult tissue, only various neuronal populations in the hippocampus and olfactory bulb express PSF. PSF is expressed by differentiating neurons but not by astrocytic cells including radial glia; however oligodendrocytes differentiating in vitro were found to express it. The restricted expression of PSF suggests that it is involved in the control of neuronal-specific splicing events occurring at particular stages of neuronal differentiation and maturation. Monoclonal antibodies reacting specifically with PSF are useful tools for the molecular identification and characterization of the functional activity of PSF.

Supplier: Genetex

The nuclear factor of activated T-cells (NFAT) transcription complex is required for the expression of a group of proteins that collectively regulate the immune response. Four NFAT proteins, encoded on separate genes and expressed as several splice variants, have been described: NFAT1 (also known as NFATp or NFATc2), NFAT2 (NFATc or NFATc1), NFAT3, and NFAT4 (NFATx or NFATc3). These proteins show a low level of sequence similarity with the Dorsal/Rel/NFkB family of transcription factors. Another NFAT-related protein termed NFAT5 differs from isoforms 1-4 in that it lacks many of the Fos/Jun contact sites observed in its predecessors and its subcellular localization is not calcineurin-dependent.

Supplier: Genetex

Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.

Supplier: IBI Scientific

The DNA/RNA/Protein Extraction Kit provides an efficient method for purifying genomic DNA, total RNA, and total protein simultaneously from cultured cells, animal tissues, whole blood, and biological fluids

Supplier: Molecular Devices

The GenePix® 4300A and GenePix® 4400A Scanners from Molecular Devices offer maximum imaging quality with optimal resolution in highly configurable platforms.

Supplier: Genetex

CD95, also known as FAS or APO-1, is a 36 kDa cell surface type I- membrane glycoprotein with an apparent molecular weight of 44 kDa on SDS-PAGE. CD95 is a member of the TNF receptor family, which includes TNFR-1, TNFR-2, CD27, CD30 and CD40. Binding of CD95 Ligand to CD95 or crosslinking of CD95 by anti-CD95 monoclonal antibodies leads to apoptosis of CD95 expressing cells. CD95 belongs to a subgroup of family members that have a death domain (DD) which contains 70 amino acids near the carboxyl-terminal region of the molecule. The binding of adaptor molecules to this DD is responsible for transmitting the death signal for apoptosis. Stimulation of CD95 results in aggregation of its DD, leading to the recruitment of FADD and caspase-8 that together with the receptor form the death-inducing signaling complex (DISC).

Supplier: Genetex

Lamins are type V intermediate filament proteins and are grouped into constitutively expressed B-type lamins and developmentally regulated A-type lamins. Lamin-binding proteins in the nuclear lamina and the nuclear interior include several protein families and/or types of proteins in higher eukaryotes such as the inner nuclear membrane proteins, lamin B receptor, emerin, and MANI, three isoforms of lamina-associated polypeptide 1 (LAP1), and several isoforms of LAP2. Up to six LAP 2 isoforms derive from a single gene by alternative splicing in mammals and various isoforms have been described in Xenopus. The best characterized LAP2 isoforms are the inner nuclear membrane protein LAP2 beta and the nucleoplasmic protein LAP2 alpha, which are identical in their N-terminal 187-amino acid constant region but differ in their C termini. While LAP2 beta binds to B-type lamins at the nuclear periphery and was suggested to regulate nuclear lamina growth , LAP2 alpha specifically interacts with A-type lamins within the nuclear interior as part of a detergent/salt-resistant nucleoskeletal structure.