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2,6-Diaminohex-4-enoic+acid
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2,6-Diaminohex-4-enoic+acid
Catalog Number:
(IC19519910)
Supplier:
MP Biomedicals
Description:
Glutaraldehyde is also referred to as glutaral, 1,5-pentanedione, potentiated acid glutaraldehyde, sonacide, and glutardialdehyde. Pure monomeric glutaraldehyde has an absorbance peak at 280 nm and the main impurity, possibly a polymer, has an absorbance peak at 235 nm. Upon analysis, this product is 25-28% by titration and has an A235/A280 ratio of not more than 0,5. Monomeric glutaraldehyde may be purified from polymeric glutaraldehyde by treatment with charcoal (5% w/v) and subsequent filtration (3-4 times). Untreated glutaraldehyde has an absorption at 235 nm that is 5 times greater than that at 280 nm, whereas, after three washings the values are about equal. Glutaraldehyde is a bifunctional cross-linking reagent, reacting with NH2 groups to form Schiff's bases.
Catalog Number:
(76010-350)
Supplier:
Prosci
Description:
The myeloid cell nuclear differentiation antigen (MNDA) is detected only in nuclei of cells of the granulocyte-monocyte lineage. A 200-amino acid region of human MNDA is strikingly similar to a region in the proteins encoded by a family of interferon-inducible mouse genes, designated Ifi-201, Ifi-202, and Ifi-203, that are not regulated in a cell- or tissue-specific fashion. The 1.8-kb MNDA mRNA, which contains an interferon-stimulated response element in the 5-prime untranslated region, was significantly upregulated in human monocytes exposed to interferon alpha. MNDA is located within 2,200 kb of FCER1A, APCS, CRP, and SPTA1. In its pattern of expression and/or regulation, MNDA resembles IFI16, suggesting that these genes participate in blood cell-specific responses to interferons.
Supplier:
PeproTech, Inc.
Description:
IL-6 is a pleiotropic cytokine that plays an important role in host defense by regulating immune and inflammatory responses. Produced by T cells, monocytes, fibroblasts, endothelial cells and keratinocytes, IL-6 has diverse biological functions. It stimulates B cell differentiation and antibody production, synergizes with IL-3 in megakaryocyte development and platelet production, induces expression of hepatic acute-phase proteins, and regulates bone metabolism. IL-6 signals through the IL-6 receptor system that consists of two chains, IL-6Rα and gp130. Murine IL-6 is inactive on human cells, while both human and murine are equally active on murine cells. Recombinant Murine IL-6 is a 21.7 kDa protein containing 188 amino acid residues.
Supplier:
MP Biomedicals
Description:
Tris have been useful as buffers in a wide variety of biological systems. It has been used as a starting material for polymers, oxazolones (with carboxylic acids) and oxazolidines (with aldehydes). It does not precipitate calcium salts and is of value in maintaining solubility of manganese salts. It can be used for the direct standardization of a strong acid solution; the equivalence point can be determined either potentiometrically or by use of a suitable indicator such as 3-(4-Dimethylamino-1-naphthylazo)-4-methoxybenzenesulfonic acid. It is RNAse and DNAse-free. Tris is relatively non-hygroscopic ; but, if needed, it can be dried at 100 °C for up to 4 hours to remove any water.
Tris is used in pH control in vitro and in vivo for body fluids and in buffering systems for electrophoresis applications.Tris is used in assays used to characterize the activity and kinetics of the enzymes that catalyze SUMOylation of Small ubiquitin-like proteins (SUMO) and SUMO-dependent protein-protein interactions.
Catalog Number:
(89162-330)
Supplier:
Enzo Life Sciences
Description:
Studies have demonstrated that PR39, a proline/arginine rich 39 amino acid antibacterial peptide originally derived from porcine bone marrow, exhibits a broad spectrum of biological activities, including the ability to induce angiogenesis and to limit inflammatory damage in a variety of animal models. The angiogenic effect is in part explained by the ability of PR39 to inhibit proteasome-dependent degradation of the transcription factor HIF-1a, while anti-inflammatory activity is associated with inhibition of IκBα degradation that in turn prevents activation of NFκB-dependent gene expression. The activities of PR39 reside in the N-terminal portion of the molecule encompassed by PR11. The most recent findings have demonstrated that PR39 is a non-competitive and reversible inhibitor of the proteasome function, which is achieved by a unique allosteric mechanism allowing for specific inhibition of degradation of selected proteins without affecting total proteasome-dependent proteolysis. A proline-arginine-rich 11 amino acid peptide derived from the naturally occurring peptide antibiotic PR39. PR39 has been shown to act as an inhibitor of both 20S and 26S proteasomes with proposed selectivity for the inhibition of the degradation of IκBα, HIF-1a and certain other proteins. PR39 has been reported to inhibit the proteasomal degradation of IκBα without effecting overall proteasome activity, or degradation of p21Cip1/Waf1 and c-fos, cell-cycle genes regulated by proteasome-dependent degradation. In vitro studies have demonstrated PR39 to be an efficient inhibitor of all three activities of the 20S proteasome. Unlike MG132 and lactacystin, long-term exposure to PR39 shows little toxicity or induction of HSP-70. In mouse models of myocardial infarction it has been shown that infusion with PR11 results in a significant reduction of myocardial infarct size. PR39, PR11 and related peptides may therefore provide novel means to regulate cellular function and the control of NF-κB-dependent gene expression for therapeutic purposes.
Catalog Number:
(76008-992)
Supplier:
Prosci
Description:
This gene is one of several cytokine genes clustered on the q-arm of chromosome 17. Cytokines are a family of secreted proteins involved in immunoregulatory and inflammatory processes. This protein is similar to CCL4 which inhibits HIV entry by binding to the cellular receptor CCR5. The copy number of this gene varies among individuals; most individuals have 1-5 copies in the diploid genome, although rare individuals do not contain this gene at all. The human genome reference assembly contains two copies of this gene. This record represents the more centromeric gene. [provided by RefSeq].
Catalog Number:
(10254-122)
Supplier:
Bioss
Description:
c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labeling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr -->Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.
Catalog Number:
(76195-564)
Supplier:
Prosci
Description:
This antibody is specific to the rod domain of human Cytokeratin 19 (CK19), a polypeptide of 40kDa. Its epitope maps between amino acid 312-335. Cytokeratin 19 is expressed in sweat gland, mammary gland ductal and secretory cells, bile ducts, gastrointestinal tract, bladder urothelium, oral epithelia, esophagus, and ectocervical epithelium. Cytokeratin 19 antibody reacts with a wide variety of epithelial malignancies including adenocarcinomas of the colon, stomach, pancreas, biliary tract, liver, and breast. Perhaps the most useful application is the identification of thyroid carcinoma of the papillary type, although 50%-60% of follicular carcinomas are also labeled. Cytokeratin 19 antibody is a useful marker for detection of tumor cells in lymph nodes, peripheral blood, bone marrow and breast cancer.
Catalog Number:
(76011-974)
Supplier:
Prosci
Description:
Olfactory receptors interact with odorant molecules in the nose, to initiate a neuronal response that triggers the perception of a smell. The olfactory receptor proteins are members of a large family of G-protein-coupled receptors (GPCR) arising from single coding-exon genes. Olfactory receptors share a 7-transmembrane domain structure with many neurotransmitter and hormone receptors and are responsible for the recognition and G protein-mediated transduction of odorant signals. The olfactory receptor gene family is the largest in the genome. The nomenclature assigned to the olfactory receptor genes and proteins for this organism is independent of other organisms.
Catalog Number:
(10254-128)
Supplier:
Bioss
Description:
c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labeling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr -->Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.
Catalog Number:
(76008-716)
Supplier:
Prosci
Description:
This gene encodes a member of the tropomyosin family of actin-binding proteins involved in the contractile system of striated and smooth muscles and the cytoskeleton of non-muscle cells. Tropomyosins are dimers of coiled-coil proteins that polymerize end-to-end along the major groove in most actin filaments. They provide stability to the filaments and regulate access of other actin-binding proteins. In muscle cells, they regulate muscle contraction by controlling the binding of myosin heads to the actin filament. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq].
Catalog Number:
(10256-594)
Supplier:
Bioss
Description:
c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labeling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr -->Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.
Catalog Number:
(10254-124)
Supplier:
Bioss
Description:
c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labeling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr -->Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.
Catalog Number:
(10254-126)
Supplier:
Bioss
Description:
c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labeling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr -->Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.
Catalog Number:
(10254-118)
Supplier:
Bioss
Description:
c-Src tyrosine kinase plays a critical role in signal transduction downstream of growth factor receptors, integrins and G protein-coupled receptors. We used stable isotope labeling with amino acids in cell culture (SILAC) approach to identify additional substrates of c-Src tyrosine kinase in human embryonic kidney 293T cells. We have identified 10 known substrates and interactors of c-Src and Src family kinases along with 26 novel substrates. We have experimentally validated 4 of the novel proteins (NICE-4, RNA binding motif 10, FUSE-binding protein 1 and TRK-fused gene) as direct substrates of c-Src using in vitro kinase assays and cotransfection experiments. Significantly, using a c-Src specific inhibitor, we were also able to implicate 3 novel substrates (RNA binding motif 10, EWS1 and Bcl-2 associated transcription factor) in PDGF signaling. Finally, to identify the exact tyrosine residues that are phosphorylated by c-Src on the novel c-Src substrates, we designed custom peptide microarrays containing all possible tyrosine-containing peptides (312 unique peptides) and their mutant counterparts containing a Tyr -->Phe substitution from 14 of the identified substrates. Using this platform, we identified 34 peptides that are phosphorylated by c-Src. We have demonstrated that SILAC-based quantitative proteomics approach is suitable for identification of substrates of nonreceptor tyrosine kinases and can be coupled with peptide microarrays for high-throughput identification of substrate phosphopeptides.
Supplier:
MP Biomedicals
Description:
Tris have been useful as buffers in a wide variety of biological systems. It has been used as a starting material for polymers, oxazolones (with carboxylic acids) and oxazolidines (with aldehydes). It does not precipitate calcium salts and is of value in maintaining solubility of manganese salts. It can be used for the direct standardization of a strong acid solution; the equivalence point can be determined either potentiometrically or by use of a suitable indicator such as 3-(4-Dimethylamino-1-naphthylazo)-4-methoxybenzenesulfonic acid. It is RNAse and DNAse-free. Tris is relatively non-hygroscopic; but, if needed, it can be dried at 100°C for up to 4 hours to remove any water.
Tris is used in pH control in vitro and in vivo for body fluids and in buffering systems for electrophoresis applications. Tris is used in assays used to characterize the activity and kinetics of the enzymes that catalyze SUMOylation of Small ubiquitin-like proteins (SUMO) and SUMO-dependent protein-protein interactions.
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is still displayed and you need assistance, please call us at 1-800-932-5000.
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