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3-(4-Bromophenyl)-5-methyl-2-thioxo-2,3-dihydro-4(1H)-quinazolinone
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3-(4-Bromophenyl)-5-methyl-2-thioxo-2,3-dihydro-4(1H)-quinazolinone
Catalog Number:
(76118-316)
Supplier:
Bioss
Description:
FOLH1B.
Supplier:
THERMO FISHER SCIENTIFIC CHEMICALS
Description:
tert-Butyl-3-oxoazetidine-1-carboxylate 97%
Catalog Number:
(10354-682)
Supplier:
Bioss
Description:
SIGLEC10 is a putative adhesion molecule that mediates sialic-acid dependent binding to cells. It preferentially binds to alpha2,3- or 2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. SIGLEC10 interacts with PTPN6/SHP-1 upon phosphorylation. The protein is expressed by peripheral blood leukocytes (eosinophils, monocytes and a natural killer cell subpopulation).
Catalog Number:
(101912-874)
Supplier:
Matrix Scientific
Description:
Matrix Scientific Part Number: 057272-1G , MDL Number:
Catalog Number:
(220018-224)
Supplier:
R&D Systems
Description:
Anti-IL26 Mouse Monoclonal Antibody (PE (Phycoerythrin)) [clone: 510414]
Catalog Number:
(10103-158)
Supplier:
Prosci
Description:
It may catalyze the formation of the NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- or NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc-sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. It may be involved in the biosynthesis of the sialyl Lewis X determinant.Synthesis of alpha-2,3-linked sialic acid to Gal (beta-1,3)GalNAc is mediated by at least 3 distinct beta-galactoside alpha-2,3-sialyltransferases (EC 2.4.99.4), including ST3GAL4. In contrast, only a single gene encodes the beta-galactoside alpha-2,6-sialyltransferase (EC 2.4.99.1), ST6GAL1 (MIM 109675) (Chang et al., 1995 [PubMed 7655169]).
Catalog Number:
(76101-540)
Supplier:
Bioss
Description:
Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).
Catalog Number:
(101935-184)
Supplier:
Matrix Scientific
Description:
MF=C16H22N2O4 MW=306.36 250Mg
Catalog Number:
(89512-340)
Supplier:
Abgent
Description:
Western Blot: 1:1000, Immunofluorescence: 1:10~50,
Catalog Number:
(102519-366)
Supplier:
Matrix Scientific
Description:
MF=C10H11CLN2O MW=210.66 MDL=MFCD20487080 250MG
Supplier:
Matrix Scientific
Description:
Matrix Scientific Part Number: 054500-1G , MDL Number: MFCD14584796
Catalog Number:
(10335-966)
Supplier:
Bioss
Description:
Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).
Catalog Number:
(10335-968)
Supplier:
Bioss
Description:
Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).
Catalog Number:
(10335-948)
Supplier:
Bioss
Description:
Putative adhesion molecule of myelomonocytic-derived cells that mediates sialic-acid dependent binding to cells. Preferentially binds to alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface. In the immune response, may act as an inhibitory receptor upon ligand induced tyrosine phosphorylation by recruiting cytoplasmic phosphatase(s) via their SH2 domain(s) that block signal transduction through dephosphorylation of signaling molecules. Induces apoptosis in acute myeloid leukemia (in vitro).
Catalog Number:
(10169-208)
Supplier:
Genetex
Description:
Mouse Monoclonal Antibody [3A8B8] to SCGB1A1
Catalog Number:
(75932-822)
Supplier:
Rockland Immunochemical
Description:
The tenascins are a family of extracellular matrix proteins (ECMs). Tenascin is an extracellular matrix protein. It expressed in an unusually restricted pattern during embryogenesis and has been implicated in a variety of morphogenetic phenomena. Human hexabrachion gene(tenascin) is mapped to chromosome 9, bands q32-q34. The coding region of the hexabrachion gene spans approximately 80 kilobases of DNA and consists of 27 exons separated by 26 introns. This antibody is suitable for researchers interested in extracellular matrix antibodies.
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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the
is still displayed and you need assistance, please call us at 1-800-932-5000.
This product is marked as restricted and can only be purchased by approved Shipping Accounts. If you need further assistance, email VWR Regulatory Department at Regulatory_Affairs@vwr.com
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