129630 Results for: "Silver+sulphate&pageNo=10"

Supplier: AAT BIOQUEST INC

Although Lissamine Rhodamine B chloride is one of the most popular labeling reagents of sulfonyl chloride, it is quite unstable in water. Even in anhydrous DMF, Lissamine Rhodamine B chloride tends to give a very complicated reaction mixture. It reacts with thiols, alcohols, phenols, aliphatic amines and aromatic amines indiscriminatingly. LRB Red™ is a succinimidyl ester and has the spectral properties identical to those of Lissamine Rhodamine B chloride. LRB Red™ is a superior replacement for Lissamine Rhodamine B chloride. LRB Red™ only reacts with aliphatic amines such as amino acids, peptides and proteins to give bright red fluorescent conjugates that are extremely stable. Compared to Lissamine Rhodamine B chloride, LRB Red™ has much higher labeling efficiency, and more importantly the resulted conjugates are much easier to be purified due to its much cleaner reactions. We strongly recommend that you consider using LRB Red™ to replace Lissamine Rhodamine B chloride for labeling peptides and oligonucleotides.

Supplier: MP Biomedicals

Storage: +4°C, protect from light
3- (4,5-Dimethyl-2-thiazolyl-2)-2,5-diphenyl-tetrazolium bromide is used as a colorimetric metabolic activity indicator in cell viability assays. Thiazolyl Blue Tetrazolium Blue (MTT) is a dye used in measurement of cell proliferation. MTT produces a yellowish solution that is converted to dark blue, water-insoluble MTT formazan by mitochondrial dehydrogenases of living cells. The blue crystals are solubilized with acidified isopropanol and the intensity is measured colorimetrically at 570 nm. MTT has been used as a histochemical/cytochemical reagent and for the detection of NAD. ADP-linked enzyme systems in tissue cannot be detected with MTT, due to binding of the cation by the cyanide trap used. MTT is rapidly reduced to the formazan, which chelates with nickel, copper, and cobalt; the cobalt chelate has been used in oxidative systems.

Supplier: Thermo Fisher Scientific

TSX™ core series is engineered for reliability and designed for everyday use. When choosing a ULT freezer, protecting your valuable samples is the top priority.  The Thermo Scientific™ TSX™ core series ULT freezers are designed with this in mind, offering reliable sample protection even in the busiest laboratory environments.

Supplier: Prosci

The ion channels activated by glutamate are typically divided into two classes. Those that are sensitive to N-methyl-D-aspartate (NMDA) are designated NMDA receptors (NMDAR) while those activated by beta-amino-3-hydroxy-5-methyl-4-isoxalone propionic acid (AMPA) are known as AMPA receptors (AMPAR). The AMPAR are comprised of four distinct subunits GluR1-4 and they play key roles in virtually all excitatory neurotransmission in the brain. The GluR1 subunit is widely expressed throughout the nervous system. GluR1 is also potentiated by phosphorylation at Ser831. In addition, phosphorylation of this site has been linked to synaptic plasticity as well and learning and memory.

Supplier: Prosci

The NMDA receptor (NMDAR) plays an essential role in memory, neuronal development and it has also been implicated in several disorders of the central nervous system including Alzheimer’s, epilepsy and ischemic neuronal cell death (Grosshans et al., 2002; Wenthold et al., 2003; Carroll and Zukin, 2002). The rat NMDAR1 (NR1) was the first subunit of the NMDAR to be cloned. The NR1 protein can form NMDA activated channels when expressed in Xenopus oocytes but the currents in such channels are much smaller than those seen in situ. Channels with more physiological characteristics are produced when the NR1 subunit is combined with one or more of the NMDAR2 (NR2 A-D) subunits (Ishii et al., 1993). Phosphorylation of Tyr1252 is thought to potentiate NMDA receptor-dependent influx of calcium (Takasu et al., 2002).

Supplier: Tonbo Biosciences

The O323 antibody reacts with human CD27 (TNFRSF7), a cell surface homodimer of 55 kDa subunits, which provides co-stimulatory signaling in support of the T cell (TCR) and B cell (BCR) receptors. By comparison with CD28, whose TCR co-stimulatory signal can trigger cell proliferation, CD27 signaling appears to promote cell survival and differentiation to effector / memory stages. Also in contrast with CD28, the CD27 receptor may be shed following interaction with its ligand CD70, which is typically expressed on activated dendritic cells, T cells and B cells. With respect to B cells, CD27 is considered to be a phenotypic marker for memory B cells. CD27 has been included within a group of phenotypic markers for identifying human B regulatory cells (Bregs), a cell type proposed to regulate CD4+ T cell proliferation and Foxp3 / CTLA-4 expression in Treg cells.

Supplier: Genetex

p38 is a 38 kDa Stress Activated Protein Kinase / Map Kinase (SAPK / MAPK) that is fully activated by dual phosphorylation on threonine 180 and tyrosine 182, within the activation loop. p38 MAPK plays a critical role in the initiation of G2 delay after ultraviolet radiation; gene knock-out studies have also revealed a critical role for p38 in cardiac remodeling. Downstream targets of p38 include the transcription factors ELK1 and ATF2 and the kinases MAPKAPK2 and MAPKAPK5. p38 MAPK plays a role in the production of IL-6 and is thought to stabilize erythropoietin production during hypoxic stress. It is activated by environmental stress, many pro-inflammatory cytokines and lipopolysaccharide. Dual phosphorylation by MAP2K3 and MAP2K6 is required for activation of p38 MAPK. It interacts with MAX, Cdc25B, Cdc25C and binds to the kinase interaction domain in the protein tyrosine phosphatase PTPRR; this interaction retains p38 MAPK in the cytoplasm.

Supplier: Peprotech

PDGFs are disulfide-linked dimers consisting of two 12.0-13.5 kDa polypeptide chains, designated PDGF-A and PDGF-B chains. The three naturally occurring PDGFs, PDGF-AA, PDGF-BB and PDGF-AB, are potent mitogens for a variety of cell types, including smooth muscle cells, connective tissue cells, bone and cartilage cells, and some blood cells. The PDGFs are stored in platelet α-granules, and are released upon platelet activation. The PDGFs are involved in a number of biological processes, including hyperplasia, chemotaxis, embryonic neuron development, and respiratory tubule epithelial cell development. Two distinct signaling receptors used by PDGFs have been identified and named PDGFR-α and PDGFR-β. PDGFR-α is high-affinity receptor for each of the three PDGF forms. On the other hand, PDGFR-β interacts with only PDGF-BB and PDGF-AB. Recombinant Murine PDGF-AA is a 28.7 kDa disulfide-linked homodimer of two α chains (250 total amino acids).

Supplier: Prosci

EphrinB proteins are thought to play key roles in cellular functions as diverse as neuronal migration and blood vessel development (Flanagan and Vanderhaeghen, 1998; Dufour et al., 2003; Oike et al., 2002). EphrinB molecules expressed at the membrane surface bind to the EphB family receptors on target cells during cell-to cell contact. This interaction leads to cell signaling in the target cell but also generates a reverse signal in the cell expressing EphrinB on its surface. This reverse signaling event is thought to be critical for vessel maturation and neuronal development. Importantly, tyrosine phosphorylation of EphrinB is thought to be a critical component of this reverse signaling event (Palmer et al., 2002). Recent work demonstrated that Tyr331 of EphrinB was phosphorylated in HEK293 cells after stimulation by the soluble EphB2 receptor tyrosine kinase (Kalo et al., 2001).

Supplier: Prosci

The protein encoded by this gene is a member of the fibroblast growth factor receptor (FGFR) family, where amino acid sequence is highly conserved between members and throughout evolution. FGFR family members differ from one another in their ligand affinities and tissue distribution. A full-length representative protein would consist of an extracellular region, composed of three immunoglobulin-like domains, a single hydrophobic membrane-spanning segment and a cytoplasmic tyrosine kinase domain. The extracellular portion of the protein interacts with fibroblast growth factors, setting in motion a cascade of downstream signals, ultimately influencing mitogenesis and differentiation. A marked difference between this gene product and the other family members is its lack of a cytoplasmic tyrosine kinase domain. The result is a transmembrane receptor that could interact with other family members and potentially inhibit signaling. Multiple alternatively spliced transcript variants encoding the same isoform have been found for this gene.

Supplier: Prosci

This antibody recognizes a protein of 36kDa, identified as Cyclin D1. It is a putative proto-oncogene overexpressed in a wide variety of human neoplasms and a key cell cycle regulator. This antibody neutralizes the activity of Cyclin D1 in vivo. About 60% of mantle cell lymphomas (MCL) contain a t(11; 14)(q13; q32) translocation resulting in over-expression. Cyclin D1 antibody is useful in identifying mantle cell lymphomas, which stain positive, from CLL/SLL and follicular lymphomas, which stain negative. Occasionally, hairy cell leukemia and plasma cell myeloma weakly express Cyclin D1.

Supplier: Prosci

This antibody recognizes a protein of 25-26kDa, identified as the Bcl-2 alpha oncoprotein. It shows no cross-reaction with Bcl-x or Bax protein. Expression of Bcl-2 alpha oncoprotein inhibits the programmed cell death (apoptosis). In most follicular lymphomas, neoplastic germinal centers express high levels of Bcl-2 alpha protein, whereas the normal or hyperplastic germinal centers are negative. Consequently, this antibody is valuable when distinguishing between reactive and neoplastic follicular proliferation in lymph node biopsies. It may also be used in distinguishing between those follicular lymphomas that express Bcl-2 protein and the small number in which the neoplastic cells are Bcl-2 negative.

Supplier: Prosci

Recognizes a protein of 110kDa, which is identified as androgen receptor (AR). It reacts with full length, and the newly described A form of the receptor. It does not cross react with estrogen, progesterone, or glucocorticoid receptors. The expression of AR is reportedly inversely correlated with histologic grade i.e. well differentiated prostate tumors show higher expression than the poorly differentiated tumors. In prostate cancer, AR has been proposed, as a marker of hormone-responsiveness and thus it may be useful in identifying patients likely to benefit from anti-androgen therapy. Anti-androgen receptor has been useful clinically in differentiating morpheaform basal cell carcinoma (mBCC) from desmoplastic trichoepithelioma (DTE) in the skin. This mAb is superb for staining of formalin/paraffin tissues.

Supplier: Prosci

Recognizes a protein of 75kDa, identified as mu heavy chain of human immunoglobulins. It does not cross-react with alpha (IgA), gamma (IgG), epsilon (IgE), or delta (IgD), heavy chains, T-cells, monocytes, granulocytes, or erythrocytes. Monomeric IgM is expressed as a membrane bound antibody on the surface of B cells and as a pentamer when secreted by plasma cells. IgM antibody is prominent in early immune responses to most antigens. Aberrant levels are associated with immune deficiency states, hereditary deficiencies, myeloma, Waldenstrom's macroglobulinemia, chronic infection and hepatocellular disease. This mAb is useful in the identification of leukemias, plasmacytomas, and certain non-Hodgkins lymphomas. The most common feature of these malignancies is the restricted expression of a single heavy chain class. Demonstration of clonality in lymphoid infiltrates indicates that the infiltrate is clonal and therefore malignant.

Supplier: Prosci

This gene is thought to play an important role in calcium homeostasis. The gene is expressed from two promoters and undergoes extensive alternative splicing. The encoded set of proteins share varying amounts of overlap near their N-termini but have substantial variations in their C-terminal domains resulting in distinct functional properties. The longest isoforms (a and f) include a C-terminal Aspartyl/Asparaginyl beta-hydroxylase domain that hydroxylates aspartic acid or asparagine residues in the epidermal growth factor (EGF)-like domains of some proteins, including protein C, coagulation factors VII, IX, and X, and the complement factors C1R and C1S. Other isoforms differ primarily in the C-terminal sequence and lack the hydroxylase domain, and some have been localized to the endoplasmic and sarcoplasmic reticulum. Some of these isoforms are found in complexes with calsequestrin, triadin, and the ryanodine receptor, and have been shown to regulate calcium release from the sarcoplasmic reticulum. Some isoforms have been implicated in metastasis.

Supplier: Prosci

Beta-catenin associates with the cytoplasmic portion of E-cadherin, which is necessary for the function of E-cadherin as an adhesion molecule. In normal tissues, beta-catenin is localized to the membrane of epithelial cells, consistent with its role in the cell adhesion complex. In breast ductal neoplasia, it is usually localized in cellular membranes. However, in lobular neoplasia, a marked redistribution throughout the cytoplasm results in a diffuse cytoplasmic pattern. Staining with beta-catenin antibody and E-cadherin antibody helps in the accurate identification of ductal and lobular neoplasms, including a distinction between low-grade ductal carcinoma in situ (DCIS) and lobular carcinoma. Additionally, some rectal and gastric adenocarcinomas demonstrate diffuse cytoplasmic staining and a lack of membranous staining, mimicking the staining pattern observed with lobular breast carcinomas.

Supplier: Prosci

CD31, also called PECAM-1, is a transmembrane glycoprotein member of the immunoglobulin supergene family of adhesion molecules. It is expressed by stem cells of the hematopoietic system and CD31 antibody can be used to identify and concentrate these cells for experimental studies as well as for bone marrow transplantation. CD31 antibody has shown to be highly specific and sensitive for vascular endothelial cells. Staining of nonvascular tumors (excluding hematopoietic neoplasms) is rare. This antibody reacts with normal, benign, and malignant endothelial cells which make up blood vessel lining. The level of CD31 expression can help to determine the degree of tumor angiogenesis, and a high expression level may imply a rapidly growing tumor and potentially a predictor of tumor recurrence.

Supplier: Prosci

Recognizes a protein of 210-220kDa, which is identified as the Complement receptor 1 or CD35. This mAb is specific for a site in CR1 that is distal from the C3b-binding site, so that it is unable to block CR1/CD35 activity. It is highly specific and shows no cross-reaction with CR2/CD21. The primary function of CR1 is to serve as the cellular receptor for C3b and C4b, the most important components of the complement system leading to clearance of foreign macromolecules. The Knops blood group system is a system of antigens located on this protein. Follicular dendritic cells (FDC) are restricted to the B-cell regions of secondary lymphoid follicles. They are CD21+/CD35+/CD1a-. This mAb labels follicular dendritic cells and follicular dendritic cell sarcoma.

Supplier: Proteintech

Beta actin, also named as ACTB and F-Actin, belongs to the actin family. Actins are highly conserved globular proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. At least six isoforms of actins are known in mammals and other vertebrates: alpha (ACTC1, cardiac muscle 1), alpha 1 (ACTA1, skeletal muscle) and 2 (ACTA2, aortic smooth muscle), beta (ACTB), gamma 1 (ACTG1) and 2 (ACTG2, enteric smooth muscle). Beta and gamma 1 are two non-muscle actin proteins. Most actins consist of 376aa, while ACTG2 (rich in muscles) has 375aa and ACTG1(found in non-muscle cells) has only 374aa. Beta actin has been widely used as the internal control in RT-PCR and Western Blotting as a 42-kDa protein. This antibody was generated against N-terminal region of human beta actin protein and can cross-react with other actins.

Supplier: Prosci

It is well known that the control of gene expression involves activation of protein kinase cascades that regulate transcription factors within the nucleus (Karin and Hunter, 1995). The cyclic AMP response element binding protein (CREB) is one of the best characterized stimulus-induced transcription factors (Montminy, 1997). This transcription factor is a component of intracellular signaling events that regulate a wide range of biological functions, from spermatogenesis to circadian rhythms and memory (Shaywitz and Greenberg, 1999; Silva et al., 1998). A variety of protein kinases including protein kinase A (PKA), mitogenactivated protein kinases (MAPKs), and Ca2+/calmodulin-dependent protein kinases (CaMKs) phosphorylate CREB at serine 133 (Ser133), and phosphorylation of Ser133 are required for CREB-mediated transcription (Johannessen et al., 2004; Kornhauser et al., 2002).

Supplier: Prosci

KEAP1 contains KELCH-1 like domains, as well as a BTB/POZ domain. Kelch-like ECH-associated protein 1 interacts with NF-E2-related factor 2 in a redox-sensitive manner and the dissociation of the proteins in the cytoplasm is followed by transportation of NF-E2-related factor 2 to the nucleus. This interaction results in the expression of the catalytic subunit of gamma-glutamylcysteine synthetase.This gene encodes a protein containing KELCH-1 like domains, as well as a BTB/POZ domain. Kelch-like ECH-associated protein 1 interacts with NF-E2-related factor 2 in a redox-sensitive manner and the dissociation of the proteins in the cytoplasm is followed by transportation of NF-E2-related factor 2 to the nucleus. This interaction results in the expression of the catalytic subunit of gamma-glutamylcysteine synthetase. Two alternatively spliced transcript variants encoding the same isoform have been found for this gene.

Supplier: Proteintech

DNA methylation in vertebrate animals is an epigenetic modification that is important for embryonic development, imprinting, and the inactivation of X chromosomes. DNA methylation is catalyzed by a family of DNA methyltransferases (DNMTs) that include the maintenance enzyme DNMT1 and de novo methyltransferases DNMT3a and DNMT3b. The overexpression of DNMT1, DNMT3a, and DNMT3b has been reported in various malignancies, including gastric, urothelial, and lung cancers, and may be related to tumorigenesis, tumor progression, and poor survival. Two isoforms of DNMT3a exist: the full-length DNMT3a, and the shorter form DNMT3a2 which lacks the N-terminal fragment. DNMT3a is expressed ubiquitously at low levels, while DNMT3a2 is specially expressed at high levels in embryonic stem cells and shows restricted expression in tissues known to undergo de novo methylation including testis and ovary. This antibody was raised against the N-terminal region of human DNMT3a. It is expected to detect the 120-130 kDa DNMT3a but not 72-100 kDa DNMT3a2.

Supplier: Prosci

ETV6 (ETS-related protein Tel1, ETS translocation variant 6 , Tel) is an ETS family transcription factor. This protein contains two functional domains: a N-terminal pointed (PNT) domain that is involved in the protein-protein interactions with itself and other proteins, and a C-terminal DNA-binding domain. Gene knockout studies in mice suggest that it is required for hematopoiesis and maintenance of the developing vascular network. This gene is known to be involved in a large number of chromosomal rearrangements associated with leukemia and congenital fibrosarcoma.This gene encodes an ETS family transcription factor. The product of this gene contains two functional domains: a N-terminal pointed (PNT) domain that is involved in the protein-protein interactions with itself and other proteins, and a C-terminal DNA-binding domain. Gene knockout studies in mice suggest that it is required for hematopoiesis and maintenance of the developing vascular network. This gene is known to be involved in a large number of chromosomal rearrangements associated with leukemia and congenital fibrosarcoma.

Supplier: Genetex

Dendritic cells (DCs) that control immune responses were recently found to capture and transport HIV from the mucosal area to remote lymph nodes, where DCs hand over HIV to CD4+ T lymphocytes. DCs also amplify the amount of virus and extend the duration of viral infectivity. Multiple strains of HIV1, HIV2 and SIV bind to DCs via DCSIGN. ICAM3 is the natural ligand for DC-SIGN. A DC-SIGN homologue (termed DC-SIGNR, L-SIGN, and DCSIGN2) was identified recently. DC-SIGN forms a novel gene family with DC-SIGNR and many alternatively spliced isoforms of DC-SIGN and DC-SIGNR. The expression of DC-SIGN was found in mucosal tissues including placenta, small intestine, and rectum.

Supplier: Peprotech

The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro . IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions. Recombinant Murine IGF-I is a 7.6 kDa globular protein containing amino acids including 3 intra-molecular disulfide bonds.

Supplier: Peprotech

Proteases (also called Proteolytic Enzymes, Peptidases, or Proteinases) are enzymes that hydrolyze the amide bonds within proteins or peptides. Most proteases act in a specific manner, hydrolyzing bonds at, or adjacent to, specific residues, or a specific sequence of residues contained within the substrate protein or peptide. Proteases play an important role in most diseases and biological processes, including prenatal and postnatal development, reproduction, signal transduction, the immune response, various autoimmune and degenerative diseases, and cancer. They are also an important research tool, frequently used in the analysis and production of proteins. Enterokinase sequentially cleaves carboxyl side of D-D-D-D-K. Human Enterokinase is expressed as a linear 1019 amino acid polypeptide precursor glycoprotein. Proteolytic processing of this precursor generates the biologically active form of Enterokinase, which consists of two polypeptide chains (heavy chain and light chain) held together by a single disulfide bond, resulting in formation of a biologically active heterodimer. The heavy chain consists of 784 amino acid residues, and the light chain consists of 235 amino acid residues. The calculated molecular weight of Recombinant Human Enterokinase is 108.7 kDa.

Supplier: Prosci

KRT10 is a member of the type I (acidic) cytokeratin family, which belongs to the superfamily of intermediate filament (IF) proteins. Keratins are heteropolymeric structural proteins which form the intermediate filament. These filaments, along with actin microfilaments and microtubules, compose the cytoskeleton of epithelial cells. Mutations in the gene encoding KRT10 are associated with epidermolytic hyperkeratosis. This gene encodes a member of the type I (acidic) cytokeratin family, which belongs to the superfamily of intermediate filament (IF) proteins. Keratins are heteropolymeric structural proteins which form the intermediate filament. These filaments, along with actin microfilaments and microtubules, compose the cytoskeleton of epithelial cells. Mutations in this gene are associated with epidermolytic hyperkeratosis. This gene is located within a cluster of keratin family members on chromosome 17q21. 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: Bioss

FUSIP1 is a member of the Serine/Arginine (SR) family of splicing factors. Members of the SR family all contain one or more RNA recognition motifs (RRM) and an SR-rich domain. SR factors are not only essential for constitutive splicing but also regulate splicing in a concentration-dependent manner by influencing the selection of alternative splice sites. Expressed in a variety of tissues with low expression in kidney, liver and heart, FUSIP1 localizes to the cytoplasm and nuclear speckles. In its dephosphorylated form (occurring during M phase of the cell cycle), FUSIP1 functions as a potent general repressor of pre-mRNA splicing and can interact with U1 SnRNP 70. In its phosphorylated form, FUSIP1 interacts with Tra-2∫ and, together, they may cooperate in the regulation of splicing. Four isoforms exist for FUSIP1. In neurons, FUSIP1 isoforms may act to either positively or negatively regulate alternative splicing.

Supplier: Agilent Technologies

BL21 competent cells are an all-purpose strain for high-level protein expression and easy induction.

Supplier: Peprotech

The three mammalian isoforms of TGF-β, TGF-β1, β2, and β3, signal through the same receptor and elicit similar biological responses. They are multifunctional cytokines that regulate cell proliferation, growth, differentiation and motility, as well as synthesis and deposition of the extracellular matrix. They are involved in various physiological processes, including embryogenesis, tissue remodeling and wound healing. They are secreted predominantly as latent complexes, which are stored at the cell surface and in the extracellular matrix. The release of biologically active TGF-β isoform from a latent complex involves proteolytic processing of the complex and/or induction of conformational changes by proteins such as thrombospondin-1. TGF-β1 is the most abundant isoform secreted by almost every cell type. It was originally identified for its ability to induce phenotypic transformation of fibroblasts, and recently it has been implicated in the formation of skin tumors. Recombinant Human TGF-β1 derived from