381442 Results for: "single-use assemblies"

Supplier: New England Biolabs (NEB)

The Monarch® Spin Plasmid Miniprep kit is a newer version of the original Monarch® Miniprep kit, and offers a unique method for plasmid preparation and purification. This kit enables extraction of highly concentrated plasmid DNA from various bacterial strains, with yields of up to 20 µg of high-quality DNA.

Supplier: Prosci

Interleukin-2 (IL-2) is a 133 amino acid glycoprotein with one intramolecular disulfide bond and variable glycosylation. It is secreted by activated T cells and induces proliferation and maturation of activated T cells, natural killer cells and lymphokine activated killer cells. IL-2 also stimulates proliferation of antibody-producing B cells, activates neutrophils and induces mononuclear cells to secrete IFN-gamma and TNF-alpha and -beta. Moreover, studies have shown that IL-2 is required for activation-induced apoptosis, an important homeostatic mechanism in the immune system, which is involved in the maintenance of peripheral tolerance to self-antigens. IL-2 promotes T cell proliferation and particularly naive T cells. IL-2 signaling on activated T cells is effected through a quaternary high-affinity receptor complex consisting of IL-2, IL-2Ralpha (CD25), IL-2Rbeta and IL-2Rgamma. Naive T cells are relatively insensitive to IL-2 as they only express small amounts of IL-2Rbeta and IL-2Rgamma. They only acquire sensitivity after CD25 expression, which captures the cytokine and presents it to the IL-2Rbeta and IL-2Rgamma receptors. IL-2 Superkine (Fc) is an artificial variant of IL-2 containing mutations at positions L80F / R81D / L85V / I 86V / I92F. These mutations are located in the molecule's core that acts to stabilize the structure and to give it a receptor-binding conformation mimicking native IL-2 bound to CD25. These mutations effectively eliminate the functional requirement of IL-2 for CD25 expression and elicit proliferation of T cells. Compared to IL-2, the IL-2 superkine induces superior expansion of cytotoxic T cells, leading to improved antitumour responses in vivo, and elicits proportionally less toxicity by lowering the expansion of Tregulatory cells and reducing pulmonary oedema.

Supplier: Zymo Research

Simple and efficient isolation of DNA from insects, including mosquitoes, bees, lice, ticks, and D

Supplier: Promega Corporation

The Wizard SV Gel and PCR Clean-Up System is designed to purify DNA fragments of 100bp-10kb from standard or low-melting agarose gels or to purify products directly from PCR or restriction digests.

Supplier: New England Biolabs (NEB)

The Monarch® HMW DNA extraction kit for cells and blood provides a rapid and reliable process for extracting high molecular weight (HMW), intact genomic DNA from cultured cells and whole blood.

Supplier: Omega Bio-Tek

The E-Z 96 Plant DNA DS Kit is designed for efficient recovery of genomic DNA up to 30 kb in size from fresh, frozen, or dried plant tissue samples rich in polysaccharides, polyphenols, or those having a lower DNA content.

Supplier: IBI Scientific

The Total RNA Mini and Maxi Tissue Kits are specially designed for purification of total RNA from a variety of animal tissues or cells

Supplier: Rockland Immunochemical

Anti-Nuclear receptor ROR gamma pS203 was designed, produced, and validated as part of the Joy Cappel Young Investigator Award (JCYIA). Nuclear receptor ROR gamma pS203 antibody detects mouse receptor ROR gamma phosphorylated at the serine 203 position. RAR-related orphan receptor gamma is a member of the nuclear receptor family of transcription factors. (ROR-gamma) is a key regulator of cellular differentiation, immunity, peripheral circadian rhythm as well as lipid, steroid, xenobiotics and glucose metabolism. ROR-gamma regulates the circadian expression of clock genes such as CRY1, ARNTL/BMAL1 and NR1D1 in peripheral tissues and in a tissue-selective manner. It is also involved in the regulation of the rhythmic expression of genes involved in glucose and lipid metabolism and is a negative regulator of adipocyte differentiation. It controls adipogenesis as well as adipocyte size and modulates insulin sensitivity in obesity. Isoform 2, ROR-gamma is essential for lymphoid organogenesis, in particular lymph nodes and Peyer's patches. ROR-gamma also plays an important regulatory role in thymopoiesis, and in inhibiting apoptosis of undifferentiated T cells. Anti-nuclear receptor ROR gamma pS203 is ideal for researcher's interested in autoimmune diseases such as psoriasis and rheumatoid arthritis, circadian rhythms, and immune system disorders.

Supplier: IBI Scientific

The Total RNA Mini and Maxi Kits are specially designed for purification of total RNA from fresh whole human blood and cultured cells

Supplier: Omega Bio-Tek

The Mag-Bind® Bacterial DNA 96 Kit allows rapid and reliable isolation of high-quality genomic DNA (gDNA) from a wide variety of bacterial species

Supplier: Ambeed

D-(+)-Camphor ≥98%

Supplier: Prosci

Interleukin-18 (IL-18) is a costimulatory factor for production of interferon-gamma (IFN-gamma) in response to toxic shock and shares functional similarities with IL-12. IL-18 is synthesized as a precursor 24kDa molecule without a signal peptide and must be cleaved to produce an active molecule. IL-1 converting enzyme (ICE; Caspase-1) cleaves pro-IL-18 at aspartic acid in the P1 position, producing the mature, bioactive peptide that is readily released from the cells. It is reported that IL-18 is produced from Kupffer cells, activated macrophages, keratinocytes, intestinal epithelial cells, osteoblasts, adrenal cortex cells and murine diencephalon. IFN-gamma is produced by activated T or NK cells and plays critical roles in the defense against microbiral pathogens. IFN-gamma activates macrophages and enhances NK activity and B cell maturation, proliferation and Ig secretion. IFN-gamma also induces expression of MHC class I and II antigens and inhibits osteoclast activation. IL-18 acts on T helper type-1 (Th1) T cells and in combination with IL-12 strongly induces them to produce IFN-gamma. Pleiotropic effects of IL-18 have also been reported, such as enhancement production of IFN-gamma and GM-CSF in peripheral blood mononuclear cells, production of Th1 cytokines, IL-2, GM-CSF, IFN-gamma in T cells and enhancement of Fas ligand expression by Th1 cells.

Supplier: Rockland Immunochemical

Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus was identified in specimens obtained from patients in Mexico and the United States. The virus spread quickly around the world and on June 11, 2009, the World Health Organization declared it a pandemic. Influenza A virus has one of sixteen possible Hemagglutinin (HA) surface proteins and one of nine possible Neuraminidase (NA) surface proteins. The Hemagglutinin protein facilitates viral attachment while Neuraminidase is involved in viral release. These proteins also elicit immune responses that prevent infection or independently reduce viral replication. The genetic make-up of this swine flu virus is unlike any other: it is an H1N1 strain that combines a triple assortment first identified in 1998 including human, swine, and avian influenza with two new pig H3N2 virus genes from Eurasia, themselves of recent human origin. The distinct antigenic properties of the new swine influenza virus compared with seasonal influenza A (H1N1) virus suggest that human immunity against new swine influenza virus is limited, although the age distribution of reported cases suggests some degree of protection in older age groups.

Supplier: Rockland Immunochemical

Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus was identified in specimens obtained from patients in Mexico and the United States. The virus spread quickly around the world and on June 11, 2009, the World Health Organization declared it a pandemic. Influenza A virus has one of sixteen possible Hemagglutinin (HA) surface proteins and one of nine possible Neuraminidase (NA) surface proteins. The Hemagglutinin protein facilitates viral attachment while Neuraminidase is involved in viral release. These proteins also elicit immune responses that prevent infection or independently reduce viral replication. The genetic make-up of this swine flu virus is unlike any other: it is an H1N1 strain that combines a triple assortment first identified in 1998 including human, swine, and avian influenza with two new pig H3N2 virus genes from Eurasia, themselves of recent human origin. The distinct antigenic properties of the new swine influenza virus compared with seasonal influenza A (H1N1) virus suggest that human immunity against new swine influenza virus is limited, although the age distribution of reported cases suggests some degree of protection in older age groups.

Supplier: Prosci

Profilin (PFN1) is a ubiquitous small (12-15kDa) phosphoinositide and poly-L-proline binding protein that plays a role in signal transduction pathways and actin filament dynamics. There are two mammalian profilins with similar biochemical properties. Whereas profilin I appears to be highly expressed in most tissues except for skeletal muscle, profilin II is predominantly expressed in brain and at lower levels also in skeletal muscle, uterus and kidney. Profilin is a mainly cytosolic protein with higher concentrations in dynamic membrane areas like the leading edge and ruffling membranes. Profilin binding to PIP2 interferes with PIP2 hydrolysis by soluble phospholipase C-gamma, an inhibition that can be overcome by tyrosine phosphorylation of PLC-gamma. Besides actin monomer sequestration and stimulation of actin nucleotide exchange, profilin can also promote cellular actin filament growth. Profilin is involved in the actin dependent intracellular motility of cytopathogenic bacteria, the regulation of cell adhesion and possibly also in linking the actin cytoskeleton and endocytosis. Profilin has been found to associate with defined complexes containing proteins such as Arp2/3 or the Rho/Rac pathways constituents ROCK-II and HEM2/NAP1. Defects in PFN1 are the cause of amyotrophic lateral sclerosis 18 (ALS18).

Supplier: New England Biolabs (NEB)

The Monarch spin columns S1A and tubes are a component of Monarch kits for DNA gel extraction, PCR cleanup, RNA cleanup, and also offered separately for convenience and flexibility.

Supplier: Zymo Research

A fast pellet-free method to isolate endotoxin-free plasmid DNA.

Supplier: New England Biolabs (NEB)

The Monarch® spin DNA gel extraction kit, a newer version of our original gel extraction kit, offers an efficient method for DNA gel extraction and purification, enabling up to 5 μg of high-quality DNA.

Supplier: Labconco

Ideal for biology, microbiology, biochemistry, pharmaceutical research, and analytical chemistry laboratories, centrifugal concentrators quickly process the evaporation of multiple small samples.

Supplier: BioVendor

Uromodulin (Tamm-Horsfall protein, UMOD) is approx. 85-kDa glycoprotein that is produced in the thick ascending limb of Henle´s loop and early distal convoluted tubules of the nephron. It is a transmembrane protein, which is secreted into the urine through proteolytic cleavage of the glycosylphosphatidylinositol (GPI) anchor. It belongs to the GPI family. Healthy individuals excrete tens of miligrams of uromodulin per day, making in the most abundant protein in the urine. Uromodulin modulates cell adhesion and signal transduction by interacting with cytokines and it inhibits the aggregation of calcium crystals. By reducing calcium oxalate precipitation, uromodulin plays a protective role with respect to renal stone formation as demonstrated by recent studies on THP- deficient mice prone to nephrolithiasis. THP acts as a host defense factor against urinary tract infections induced by uropathogens such as Esherichia coli, Staphylococcus saphrophyticus, Proteus mirabilis and Klebsiela pneumonie. Uromodulin binds to type 1 fimbriae of Escherichia coli and thereby blocks colonization of urothelial cells. Tamm-Horsfall protein interacts with other molecules and cells including IL-1, IL-2, TNF, IgG, neuthrophils, lymphocytes and monocytes. Binding of uromodulin to neutrophils induces synthesis of IL-8, provokes the respiratory burst and degranulation and stimulates chemotaxis and phagocytosis. Recently, genome-wide association studies identified uromodulin as a risk factor for chronic kidney disease and hypertension. Mutations in the Uromodulin gene are associated with three autosomal dominant tubulo-interstitial nephropathies such as familial juvenile hyperuricemic nephropathy (FJHN), medullary cystic kidney disease (MCKD2) and glomerulocystic kidney disease (GCKD). These disorders are characterized by juvenile onset of hyperuricemia, gout and progressive renal failure.

Supplier: Zymo Research

Spin columns for the purification of DNA or RNA.

Supplier: Zymo Research

Spin columns for the purification of DNA and/or RNA and fluorescent dye removal.

Supplier: Prosci

NF-κ-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-κ-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-κ-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-κ-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-κ-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-κ-B complex which translocates to the nucleus. NF-κ-B heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-κ-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-κ-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-κ-B complex

Supplier: Rockland Immunochemical

H1N1 Neuraminidas Antibody detects seasonal influenza (H1N1) Neuraminidase protein and the novel swine influenza Neuraminidase protein. Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus was identified in specimens obtained from patients in Mexico and the United States. The virus spread quickly around the world and on June 11, 2009, the World Health Organization declared it a pandemic. Influenza A virus has one of sixteen possible Hemagglutinin (HA) surface proteins and one of nine possible Neuraminidase (NA) surface proteins. The Hemagglutinin protein facilitates viral attachment while Neuraminidase is involved in viral release. These proteins also elicit immune responses that prevent infection or independently reduce viral replication. The genetic make-up of this swine flu virus is unlike any other: it is an H1N1 strain that combines a triple assortment first identified in 1998 including human, swine, and avian influenza with two new pig H3N2 virus genes from Eurasia, themselves of recent human origin. The distinct antigenic properties of the new swine influenza virus compared with seasonal influenza A (H1N1) virus suggest that human immunity against new swine influenza virus is limited, although the age distribution of reported cases suggests some degree of protection in older age groups. Anti-H1N1 Neuraminidase antibodies are ideal for investigators involved in infectious diease.

Supplier: Promega Corporation

The SV 96 Total RNA Isolation System provides a high-throughput technique to prepare intact RNA from tissue and cultured cells.

Supplier: Prosci

NF-κ-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-κ-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-κ-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-κ-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-κ-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-κ-B complex which translocates to the nucleus. NF-κ-B heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-κ-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-κ-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-κ-B complex

Supplier: Omega Bio-Tek

The Mag-Bind® cfDNA Kit is designed for rapid and reliable isolation of circulating DNA from 500 - 4 000 µL plasma/serum samples.

Supplier: Zymo Research

Quick-RNA plant miniprep kit is designed for rapid isolation of RNA from various plant samples such as leaves, stems, buds, flowers, fruits and seeds.

Supplier: Prosci

Kinase subunit of both mTORC1 and mTORC2, which regulate cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Amino-acid-signaling to mTORC1 is mediated by Rag GTPases, which cause amino-acid-induced relocalization of mTOR within the endomembrane system. Growth factor-stimulated mTORC1 activation involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-421', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'.

Supplier: Prosci

Kinase subunit of both mTORC1 and mTORC2, which regulate cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Amino-acid-signaling to mTORC1 is mediated by Rag GTPases, which cause amino-acid-induced relocalization of mTOR within the endomembrane system. Growth factor-stimulated mTORC1 activation involves AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-421', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'.