3,5-Bis(trifluoromethyl)phenylboronic+acid
Catalog Number:
(76011-616)
Supplier:
Prosci
Description:
HLA-DQA1 belongs to the HLA class II alpha chain paralogues. The class II molecule is a heterodimer consisting of an alpha (DQA) and a beta chain (DQB), both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B Lymphocytes, dendritic cells, macrophages). The alpha chain is approximately 33-35 kDa. It is encoded by 5 exons; exon 1 encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, and exon 4 encodes the transmembrane domain and the cytoplasmic tail. Within the DQ molecule both the alpha chain and the beta chain contain the polymorphisms specifying the peptide binding specificities, resulting in up to four different molecules. Typing for these polymorphisms is routinely done for bone marrow transplantation.
Catalog Number:
(76011-686)
Supplier:
Prosci
Description:
HLA-DQA1 belongs to the HLA class II alpha chain paralogues. The class II molecule is a heterodimer consisting of an alpha (DQA) and a beta chain (DQB), both anchored in the membrane. It plays a central role in the immune system by presenting peptides derived from extracellular proteins. Class II molecules are expressed in antigen presenting cells (APC: B Lymphocytes, dendritic cells, macrophages). The alpha chain is approximately 33-35 kDa. It is encoded by 5 exons; exon 1 encodes the leader peptide, exons 2 and 3 encode the two extracellular domains, and exon 4 encodes the transmembrane domain and the cytoplasmic tail. Within the DQ molecule both the alpha chain and the beta chain contain the polymorphisms specifying the peptide binding specificities, resulting in up to four different molecules. Typing for these polymorphisms is routinely done for bone marrow transplantation.
Catalog Number:
(100504-028)
Supplier:
Electron Microscopy Sciences
Description:
The strength of the gel is based on the bloom number. The higher the bloom number the stronger the gel.
Used as a combination Acrylamide-Gelatin-Jung resin for cryosectioning of large and soft tissues (eggs, fishes, insects) Hartmann, R. (1984). A new embedding medium for cryosectioning eggs of high yolk and lipid content. Eur. J. Cell Biol., 34:206 Used to prepare gelatin-chrome alum adhesive to coat glass slides for mounting semi-thin sections for staining. ![]()
Supplier:
TCI America
Description:
CAS Number: 1709-70-2
MDL Number: MFCD00026284
Molecular Formula: C54H78O3
Molecular Weight: 775.22
Purity/Analysis Method: <gt/>95.0% (GC)
Form: Crystal
Color: White
Melting point (°C): 243
Catalog Number:
(10049-832)
Supplier:
Enzo Life Sciences
Description:
Cyclooxygenases-1 and 2 (COX-1 and COX-2), also known as prostaglandin endoperoxide H synthases-1 and 2, are integral membrane proteins which catalyze the first step of prostaglandin, thromboxane and prostacyclin production from arachidonic acid. Both COX-1 and COX-2 catalyze a cyclooxygenase (bis-oxygenase) reaction in which arachidonate plus two molecules of O2 are converted to PGG2 (prostaglandin G2), and a peroxidase reaction in which PGG2 undergoes a two-electron reduction to PGH2. COX-1 and COX-2 proteins are encoded by separate genes located on different chromosomes, and both enzymes are very similar in structure. They are homodimeric, heme containing, glycosylated proteins with two catalytic sites, but they differ substantially in their pattern of expression and biology. COX-1 is expressed constitutively in most tissues and at high levels in selected cells and tissues, including endothelium, monocytes, platelets, renal collecting tubules and seminal vesicles. COX-1 is thought to regulate a number of housekeeping activities involved in renal, gastrointestinal and platelet function. Inducible COX-2 is undetectable in most mammalian tissues but its expression can be induced rapidly (2-6h) in fibroblasts, endothelial cells, monocytes and ovarian follicles in response to growth factors, tumor promoters, hormones, bacterial endotoxin and cytokines. COX-2 is also expressed constitutively in specialized cell types or tissues where it plays specific functions in individual biological processes. These include reproduction, immunity, renal physiology, neurotransmission, bone resorption and pancreatic secretion. The COX-1 and COX-2 enzymes are important pharmacologically as targets of nonsteroidal anti-inflammatory drugs (NSAIDs) including aspirin, ibuprofen and the COX-2 inhibitors. Inhibition of cyclooxygenases with NSAIDs acutely reduces inflammation, pain and fever. Some methods to determine COX activity include measuring uptake of oxygen using an oxygraph, measuring the conversion of radioactive arachidonic acid, or measuring prostaglandins formed from PGH2 (such as determining PGH2 using immunoassays). These methods can be complex, time consuming and prone to interferences.
Catalog Number:
(10801-332)
Supplier:
Rockland Immunochemical
Description:
Programmed cell death regulates a number of biological processes such as normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. FAIM2 is a recently identified protein that can inhibit the apoptotic signal transduced by the Fas receptor but not from the related tumor necrosis factor-alpha death signal. In this respect, FAIM2 is functionally similar to the anti-apoptotic proteins FAIM, FLIP and Bcl-xL. FAIM2, a seven membrane spanning protein, can bind the Fas receptor but does not regulate Fas expression or inhibit binding of FADD to Fas. FAIM2 is widely distributed, but highly expressed in the hippocampus and other neural tissues. FAIM2 was also identified as the neural membrane protein 35 (NMP35) and its expression is known to be regulated by the Phosphatidylinositol 3-kinase-Akt/PKB pathway.
Catalog Number:
(100504-108)
Supplier:
Electron Microscopy Sciences
Description:
Used as a counterstain in Almann's aniline acid fuchsin technique for mitochrondria; used in Kurnick's Methyl Green-Pyonin stain for nuclei and cystoplasmic granules of liver cells. Marker for DNA at acid and neutral conditions (J.B. Boyd, H.R. Mitchell, (1965) Anal. Biochem., 13, 28). Used for epoxy-embedded thick sections (Sievers, J. (1971)).
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Supplier:
PeproTech, Inc.
Description:
Sclerostin, a glycoprotein predominantly secreted by osteocytes, is a member of the Cerberus/DAN family of putative BMP antagonists that functions as an endogenous regulator of the canonical Wnt signaling pathway and an inhibitory regulator of bone homeostasis. Although expressed nearly exclusively by osteocytes, sclerostin can also be found at significant levels elsewhere, such as bone, bone marrow, cartilage, the kidney, and the liver, and has also been shown to be produced by hypertrophic chondrocytes and cementocytes. Like DKK family members DKK-1 and DKK-4, sclerostin plays an important regulatory role in the Wnt/beta-catenin signaling pathway by forming inhibitory complexes with LDL Receptor-related proteins 5 and 6 (LRP5 and LRP6), which are essential components of the Wnt/beta-catenin signaling system. LRP5 and LRP6 are single-pass transmembrane proteins that appear to act as co-receptors for Wnt ligands involved in the Wnt/beta-catenin signaling cascade. Sclerostin has also been shown to interact directly with LRP4 via its extracellular domain to facilitate inhibition of Wnt signaling, and can catabolically promote osteoclast activity by increasing osteocyte expression of RANKL. Sclerostin's critical involvement in the regulation of bone formation and resorption is emphasized by two bone dysplasia disorders, sclerosteosis and van Buchem disease (VBD), caused by rare autosomal recessive mutations that result in progressive bone overgrowth and hypermineralization due to markedly decreased sclerostin levels. PeproTech's CHO cell-derived Recombinant Human Sclerostin is a 190-amino-acid-length glycoprotein with a calculated molecular weight of 21.5 kDa. As a result of glycosylation, Recombinant Human Sclerostin migrates with an apparent molecular mass of approximately 28-35 kDa by SDS-PAGE gel, under non-reducing conditions.
Catalog Number:
(100504-026)
Supplier:
Electron Microscopy Sciences
Description:
The strength of the gel is based on the bloom number. The higher the bloom number the stronger the gel.
Used as a combination Acrylamide-Gelatin-Jung resin for cryosectioning of large and soft tissues (eggs, fishes, insects) Hartmann, R. (1984). A new embedding medium for cryosectioning eggs of high yolk and lipid content. Eur. J. Cell Biol., 34:206 Used to prepare gelatin-chrome alum adhesive to coat glass slides for mounting semi-thin sections for staining. ![]()
Catalog Number:
(75932-844)
Supplier:
Rockland Immunochemical
Description:
The Transcription factor EB (TFEB) is a member in the basic helix-loop-helix leucine zipper superfamily of transcription factors that is translocated in a subset of renal tumors (1,2). Recent studies have shown that lysosomal biogenesis is regulated by TFEB (3), which is in turn regulated by the mammalian target of rapamycin (mTOR) complex 1 (4). Other evidence suggests that TFEB coordinates the major steps of the autophagic pathway by driving the expression of autophagy and lysosomal genes (5).
Supplier:
PeproTech, Inc.
Description:
Lectins, of either plant or animal origin, are carbohydrate-binding proteins that interact with glycoproteins and glycolipids on the surface of animal cells. The Galectins are lectins that recognize and interact with β-galactoside moieties. Galectin-3 regulates a number of biological processes, including embryogenesis, inflammatory responses, cell progression and metastasis. Galectin-3 is normally expressed in epithelia of a variety of tissues, including colon and endometrium, and in various inflammatory cells, including macrophages. Galectin-3 can function intracellularly, controlling the cell cycle and preventing T-cell apoptosis, and also extracellularly, by activating various cells, including monocytes/macrophages, mast cells, neutrophils, and lymphocytes. Expression of Galectin-3 is affected by neoplastic transformation, being up-regulated in certain types of lymphomas, and in thyroid and hepatic carcinomas. Conversely, it is down-regulated in other cancers such as colon, breast, ovarian, and uterine. Recombinant Human Galectin-3 is a globular 26.0 kDa protein containing 250 amino acid residues, but no disulfide bonds.
Supplier:
AVANTOR PERFORMANCE MATERIALS US
Description:
pH adjusters are used to adjust the pH of formulations. This category includes acids that are notoriously difficult to source as truly cGMP-produced and amino acids that most companies do not fully test for EP, BP and JP. Avantor provides all that and more.
Catalog Number:
(75794-224)
Supplier:
Prosci
Description:
CD80 (B7-1) and CD86 (B7-2) together with their receptors CD28 and CTLA-4 constitute one of the dominant costimulatory pathways that regulate T cell and B cell responses. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28 and is involved in the down-regulation of the immune response. B7-1 is expressed on activated B cells, activated T cells and macrophages. B7-2 is constitutively expressed on interdigitating dendritic cells, Langerhans cells, peripheral blood dendritic cells, memory B cells, and germinal center B cells. Additionally, B7-2 is expressed at low levels on monocytes and can be up-regulated through interferon-gamma. B7-1 and B7-2 are both members of the immunoglobulin superfamily. It has been observed that both human and mouse B7-1 and B7-2 can bind to either human or mouse CD28 and CTLA-4, suggesting that there are conserved amino acids which form the B7-1/B7-2/CD28/CTLA-4 critical binding sites.
Catalog Number:
(75794-226)
Supplier:
Prosci
Description:
CD80 (B7-1) and CD86 (B7-2) together with their receptors CD28 and CTLA-4 constitute one of the dominant costimulatory pathways that regulate T cell and B cell responses. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28 and is involved in the down-regulation of the immune response. B7-1 is expressed on activated B cells, activated T cells and macrophages. B7-2 is constitutively expressed on interdigitating dendritic cells, Langerhans cells, peripheral blood dendritic cells, memory B cells, and germinal center B cells. Additionally, B7-2 is expressed at low levels on monocytes and can be up-regulated through interferon-gamma. B7-1 and B7-2 are both members of the immunoglobulin superfamily. It has been observed that both human and mouse B7-1 and B7-2 can bind to either human or mouse CD28 and CTLA-4, suggesting that there are conserved amino acids which form the B7-1/B7-2/CD28/CTLA-4 critical binding sites.
Catalog Number:
(10749-344)
Supplier:
Prosci
Description:
Acinus Antibody: Chromatin condensation and nuclear fragmentation (CCNF) is the hallmark of apoptosis. CCNF is triggered by the activation of members of caspase family, caspase activated DNase (CAD/DFF40), and several novel proteins including AIF and CIDE. A new inducer of chromatin condensation was recently identified and designated Acinus (for apoptotic chromatin condensation inducer in the nucleus). Acinus is cleaved by caspase-3 and an additional unknown protease generating a small active peptide p17, which causes chromatin condensation in vitro when it is added to purified nuclei. Acinus also induces apoptotic chromatin condensation in cells. Acinus is ubiquitously expressed. Three different spliced forms of Acinus have been identified in human and mouse and designated AcinusL, AcinusS and AcinusS'.
Catalog Number:
(10076-328)
Supplier:
Prosci
Description:
SIRT7 is a human member of a family of proteins called Sirtuins (Sir2-like proteins) and are present in prokaryotes and eukaryotes. All Sir2-like proteins have a sirtuin core domain, which contains a series of sequence motifs conserved in organisms ranging from bacteria to humans. Bacterial, yeast and mammalian sirtuins are able to metabolize NAD and possibly at as mono-ADP-ribosyltransferases. The enzymatic function of sirtuins is not yet completely understood but recent reports of histone-activated Sir2-mediated NAD metabolism and NAD-activated Sir2-mediated histone deacetylation suggest a possible coupled reciprocal activation mechanism involving interactions of Sir2 with NAD and the N epsilon-acetyl-lysine groups of acetylated histones.
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