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cell+culture+flasks
Fournisseur:
Biotium
Description:
MAb IPO-10 defines the antigen, which appears on B cell progenitors following HLA-DR and preceding CD10, CD19, CD22, CD37 and cym. It is expressed on resting B cells and than reappears and persists in cytoplasm and on cell surface until cytoplasmic Ig appears. It is a useful antibody for diagnostics of neoplasms of B cell origins. It reacts with human B cell lines Daudi, Raji, Namalva, EB-3, RPMI-8226 (50% of cells). The MAb does not label T cell lines, blood granulocytes, thymocytes or bone marrow stromal fibroblasts. No significant changes are detected after PHA or ConA stimulation while LPS and PWM stimulated cultures after 18-48h show decreased number of antigen-positive cells but in final terms of cultivation antigen is expressed again. This MAb labels B cell leukemias and some lymphomas. Hairy cell leukemia strongly reacts and 70% of B cell CLL and some B-NHL were also positive. IPO-10 reacts with AMML cells and in a majority of Hodgkin's disease cases a significant percentage of affected lymph node cells were detected.
Numéro de catalogue:
(ENZOBMLUW99150001)
Fournisseur:
ENZO LIFE SCIENCES
Description:
1. Ubiquitinylation of specific endogenous HeLa lysate proteins, followed by their immediate detection/analysis using antibodies to the protein/s of interest, indicating a particular protein is a substrate for the ubiquitin-proteasome pathway. 2. Ubiquitinylation of proteins of interest contained in exogenously added expression culture/cell extracts or tissue lysates/extracts, followed by their immediate detection/analysis or isolation/purification for use in subsequent experiments. 3. Modification of proteins using ubiquitin derivatives or mutants for improved detection/analysis or investigation of alternative (non-proteasomal) ubiquitin related pathways in subsequent experiments. For example, biotinylated-ubiquitin (Prod. No. BML-UW8705), for sensitive detection
UOM:
1 * 20 Tests
New Product
Fournisseur:
Biotium
Description:
Cyclins, regulatory subunits, which associate with kinases, control many of the important steps in cell cycle progression. The Cdc2 protein kinase (p34Cdc2) exhibits protein kinase activity in vitro and exists in a complex with both cyclin B and a protein homologous to p13SUC1. Cdc2 kinase is the active subunit of the M phase promoting factor (MPF) and the M phase-specific Histone H1 kinase. The p34Cdc2/cyclin B complex is required for the G2 to M transition. An additional cell cycle-dependent protein kinase, termed p55cdc, exhibits a high degree of homology with the S. cerevisiae proteins Cdc20 and Cdc4. The p55cdc transcript is readily detectable in a variety of cultured cell lines in growth phase, but disappears when cell growth is chemically arrested.
Fournisseur:
Biotium
Description:
Cyclins, regulatory subunits, which associate with kinases, control many of the important steps in cell cycle progression. The Cdc2 protein kinase (p34Cdc2) exhibits protein kinase activity in vitro and exists in a complex with both cyclin B and a protein homologous to p13SUC1. Cdc2 kinase is the active subunit of the M phase promoting factor (MPF) and the M phase-specific Histone H1 kinase. The p34Cdc2/cyclin B complex is required for the G2 to M transition. An additional cell cycle-dependent protein kinase, termed p55cdc, exhibits a high degree of homology with the S. cerevisiae proteins Cdc20 and Cdc4. The p55cdc transcript is readily detectable in a variety of cultured cell lines in growth phase, but disappears when cell growth is chemically arrested.
Fournisseur:
Biotium
Description:
Cyclins, regulatory subunits, which associate with kinases, control many of the important steps in cell cycle progression. The Cdc2 protein kinase (p34Cdc2) exhibits protein kinase activity in vitro and exists in a complex with both cyclin B and a protein homologous to p13SUC1. Cdc2 kinase is the active subunit of the M phase promoting factor (MPF) and the M phase-specific Histone H1 kinase. The p34Cdc2/cyclin B complex is required for the G2 to M transition. An additional cell cycle-dependent protein kinase, termed p55cdc, exhibits a high degree of homology with the S. cerevisiae proteins Cdc20 and Cdc4. The p55cdc transcript is readily detectable in a variety of cultured cell lines in growth phase, but disappears when cell growth is chemically arrested.
Numéro de catalogue:
(BNUM0672-50)
Fournisseur:
Biotium
Description:
Cyclins, regulatory subunits, which associate with kinases, control many of the important steps in cell cycle progression. The Cdc2 protein kinase (p34Cdc2) exhibits protein kinase activity in vitro and exists in a complex with both cyclin B and a protein homologous to p13SUC1. Cdc2 kinase is the active subunit of the M phase promoting factor (MPF) and the M phase-specific Histone H1 kinase. The p34Cdc2/cyclin B complex is required for the G2 to M transition. An additional cell cycle-dependent protein kinase, termed p55cdc, exhibits a high degree of homology with the S. cerevisiae proteins Cdc20 and Cdc4. The p55cdc transcript is readily detectable in a variety of cultured cell lines in growth phase, but disappears when cell growth is chemically arrested.
UOM:
1 * 50 µl
Numéro de catalogue:
(BOSSBS-5814R-A488)
Fournisseur:
Bioss
Description:
Prominin 2 is a 112 kDa glycoporotein structurally related to Prominin 1 (CD133) although amino acid similarity is not more than 30%, but their genomic organization is strikingly similar. Like Prominin 1, the prominin 2 exhibit similar membrane topology with 5 trans-membrane domains and two large glycosylated extracellular domains. Similar to Prominin1 localization, the Prominin 2 is also associated with membrane protrusions of the epithelial cells from adult kidney, and all along the digestive track and other epithelial tissues.Prominin 2 expression is down-regulated in aggressive prostate cancer cell lines and transient transfection of PROML2 expression vectors has been shown to induce apoptosis in cultured prostate cancer cells, suggesting a tumor suppressive role for Prominin 2. Prominin 2 expression is likely to be involved in growth suppression in the prostate, and down-regulation of Prominin 2 may disrupt normal prostatic homeostasis and lead to uncontrolled prostatic growth.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5814R-CY5.5)
Fournisseur:
Bioss
Description:
Prominin 2 is a 112 kDa glycoporotein structurally related to Prominin 1 (CD133) although amino acid similarity is not more than 30%, but their genomic organization is strikingly similar. Like Prominin 1, the prominin 2 exhibit similar membrane topology with 5 trans-membrane domains and two large glycosylated extracellular domains. Similar to Prominin1 localization, the Prominin 2 is also associated with membrane protrusions of the epithelial cells from adult kidney, and all along the digestive track and other epithelial tissues.Prominin 2 expression is down-regulated in aggressive prostate cancer cell lines and transient transfection of PROML2 expression vectors has been shown to induce apoptosis in cultured prostate cancer cells, suggesting a tumor suppressive role for Prominin 2. Prominin 2 expression is likely to be involved in growth suppression in the prostate, and down-regulation of Prominin 2 may disrupt normal prostatic homeostasis and lead to uncontrolled prostatic growth.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5814R-A647)
Fournisseur:
Bioss
Description:
Prominin 2 is a 112 kDa glycoporotein structurally related to Prominin 1 (CD133) although amino acid similarity is not more than 30%, but their genomic organization is strikingly similar. Like Prominin 1, the prominin 2 exhibit similar membrane topology with 5 trans-membrane domains and two large glycosylated extracellular domains. Similar to Prominin1 localization, the Prominin 2 is also associated with membrane protrusions of the epithelial cells from adult kidney, and all along the digestive track and other epithelial tissues.Prominin 2 expression is down-regulated in aggressive prostate cancer cell lines and transient transfection of PROML2 expression vectors has been shown to induce apoptosis in cultured prostate cancer cells, suggesting a tumor suppressive role for Prominin 2. Prominin 2 expression is likely to be involved in growth suppression in the prostate, and down-regulation of Prominin 2 may disrupt normal prostatic homeostasis and lead to uncontrolled prostatic growth.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5814R-CY3)
Fournisseur:
Bioss
Description:
Prominin 2 is a 112 kDa glycoporotein structurally related to Prominin 1 (CD133) although amino acid similarity is not more than 30%, but their genomic organization is strikingly similar. Like Prominin 1, the prominin 2 exhibit similar membrane topology with 5 trans-membrane domains and two large glycosylated extracellular domains. Similar to Prominin1 localization, the Prominin 2 is also associated with membrane protrusions of the epithelial cells from adult kidney, and all along the digestive track and other epithelial tissues.Prominin 2 expression is down-regulated in aggressive prostate cancer cell lines and transient transfection of PROML2 expression vectors has been shown to induce apoptosis in cultured prostate cancer cells, suggesting a tumor suppressive role for Prominin 2. Prominin 2 expression is likely to be involved in growth suppression in the prostate, and down-regulation of Prominin 2 may disrupt normal prostatic homeostasis and lead to uncontrolled prostatic growth.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13736R-CY5)
Fournisseur:
Bioss
Description:
ADAM13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was also found in liver, heart, and intestines from adult Xenopus. ADAM13 may regulate cellular signaling via Src and Src tyrosine kinase. ADAM13 may also act as a cell attachment molecule, by binding integrins through the cysteine rich domain amoung many other roles. A member of the metalloproteinase family containing disintegrin like domains (ADAMs) the functions of ADAM13 are still poorly understood. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine rich, EFG like, transmembrane and Cytoplasmic domains. ADAM13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF like domain. ADAM13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM13 is a 52 kD protein, and can form complexes with a2 macroglobulin, suggesting it is a competent protease. Xenopus ADAM13 has greatest homology with human ADAM 33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM13 may be a unique protein. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine rich regions give Xenopus ADAM13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13736R-HRP)
Fournisseur:
Bioss
Description:
ADAM13 was first described as a protein expressed in somatic mesoderm and neural crest cells, in developing Xenopus embryos. ADAM13 was also found in liver, heart, and intestines from adult Xenopus. ADAM13 may regulate cellular signaling via Src and Src tyrosine kinase. ADAM13 may also act as a cell attachment molecule, by binding integrins through the cysteine rich domain amoung many other roles. A member of the metalloproteinase family containing disintegrin like domains (ADAMs) the functions of ADAM13 are still poorly understood. ADAM13 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, as well as disintegrin, cysteine rich, EFG like, transmembrane and Cytoplasmic domains. ADAM13 has been shown to be proteolytically active, cleaving fibronectin after binding it to the EGF like domain. ADAM13 is also shed from cells in culture, cleaved aminoterminal from the transmembrane domain, and is released into the culture media. Shed ADAM13 is a 52 kD protein, and can form complexes with a2 macroglobulin, suggesting it is a competent protease. Xenopus ADAM13 has greatest homology with human ADAM 33 (51% identical), and is 46% identical with human or mouse ADAM12 or ADAM19. It is still unclear if any of these ADAMs are species orthologs of Xenopus ADAM13, but there are significant differences between the related sequences, suggesting that ADAM13 may be a unique protein. The full length Xenopus ADAM13 sequence codes for a 914 amino acid protein. Predicted mass is 99.749 kD, but glycosylation and cyteine rich regions give Xenopus ADAM13 an apparent MW of 120 kD unprocessed, and 97 kD processed forms, on reduced SDS PAGE gels. ADAM13 contains a putative furin cleavage site, suggesting that a prohormone convertase cleaves the propeptide domain away from the catalytic domain
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11027R)
Fournisseur:
Bioss
Description:
NKHC1 is a neuronal-specific component of a multi-subunit “molecular motor†complex that mediates intracellular organelle transport. Mutations in the gene encoding NKHC1 cause autosomal dominant spastic paraplegia 10. NKHC1 has a pan-neuronal distribution in the nervous system. Rat tissue extracts by immunoblot of NKHC1 can produce a doublet only in brain and sciatic nerve tissue. NKHC1 is distributed throughout the central nervous system and is enriched in subsets of neurons. Within cultured hippocampal neurons, NKHC1 is concentrated in the perinuclear region of the cell body. Kinesin superfamily proteins like NKHC1 are the molecular motors conveying cargos along microtubules.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5814R-A555)
Fournisseur:
Bioss
Description:
Prominin 2 is a 112 kDa glycoporotein structurally related to Prominin 1 (CD133) although amino acid similarity is not more than 30%, but their genomic organization is strikingly similar. Like Prominin 1, the prominin 2 exhibit similar membrane topology with 5 trans-membrane domains and two large glycosylated extracellular domains. Similar to Prominin1 localization, the Prominin 2 is also associated with membrane protrusions of the epithelial cells from adult kidney, and all along the digestive track and other epithelial tissues.Prominin 2 expression is down-regulated in aggressive prostate cancer cell lines and transient transfection of PROML2 expression vectors has been shown to induce apoptosis in cultured prostate cancer cells, suggesting a tumor suppressive role for Prominin 2. Prominin 2 expression is likely to be involved in growth suppression in the prostate, and down-regulation of Prominin 2 may disrupt normal prostatic homeostasis and lead to uncontrolled prostatic growth.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5814R-FITC)
Fournisseur:
Bioss
Description:
Prominin 2 is a 112 kDa glycoporotein structurally related to Prominin 1 (CD133) although amino acid similarity is not more than 30%, but their genomic organization is strikingly similar. Like Prominin 1, the prominin 2 exhibit similar membrane topology with 5 trans-membrane domains and two large glycosylated extracellular domains. Similar to Prominin1 localization, the Prominin 2 is also associated with membrane protrusions of the epithelial cells from adult kidney, and all along the digestive track and other epithelial tissues.Prominin 2 expression is down-regulated in aggressive prostate cancer cell lines and transient transfection of PROML2 expression vectors has been shown to induce apoptosis in cultured prostate cancer cells, suggesting a tumor suppressive role for Prominin 2. Prominin 2 expression is likely to be involved in growth suppression in the prostate, and down-regulation of Prominin 2 may disrupt normal prostatic homeostasis and lead to uncontrolled prostatic growth.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-13070R)
Fournisseur:
Bioss
Description:
The rTS gene codes for a naturally occurring antisense RNA to thymidylate synthase (TS) mRNA and two proteins (rTSalpha and rTSbeta (also known as ENOSF1)). The role of the major protein product of rTS, ENOSF1 has been linked to alterations in TS protein expression, but the precise function of ENOSF1 is unknown. Expression of rTS is associated with growth arrest in cell culture, but its overexpression has been noted in cells resistant to anticancer drugs such as 5-fluorouracil and methotrexate. Studies have shown that increased expression of ENOSF1 is associated with the decrease in TS protein expression due to production of novel, diffusible signal molecules.
UOM:
1 * 100 µl
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