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cell+culture+flasks
Numéro de catalogue:
(BOSSBS-1318R-HRP)
Fournisseur:
Bioss
Description:
Factor that induces terminal differentiation of late-developing B-cells to immunoglobulin secreting cells.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2521R-CY7)
Fournisseur:
Bioss
Description:
Plays a role as a receptor for the recognition of MHC class I HLA-E molecules by NK cells and some cytotoxic T-cells.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
This antibody recognizes a protein of 30 kDa, identified as CD70. It is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This cytokine is a ligand for TNFRSF27/CD27. It is a surface antigen on activated, but not on resting, T- and B-lymphocytes. It induces proliferation of co-stimulated T cells, enhances the generation of cytolytic T cells, and contributes to T cell activation. This cytokine is also reported to play a role in regulating B-cell activation, cytotoxic function of natural killer cells, and immunoglobulin synthesis. This MAb blocks the interaction between CD27 and CD70, and has been shown toinhibit T cell proliferation induced by dendritic cells.
Numéro de catalogue:
(BOSSBS-5444R)
Fournisseur:
Bioss
Description:
The ILK protein is important in different biological pathways such as cell adhesion, anchorage-dependent cell cycle progression, oncogenic transformation, and growth factor signaling. The kinase activity of ILK is low in non-activated cells; its activity is stimulated by cell-ECM interactions and by certain growth factors. 3 Negative regulation of ILK is mediated by two phosphatases: PTEN, a tumor suppressor lipid sphatase, and ILKAP, a PP2C protein phosphatase. In tumor cells that do not express PTEN protein, ILK is constitutively active.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6914R-A555)
Fournisseur:
Bioss
Description:
Tyrosine kinase of the non-receptor type. Probably performs an important function, perhaps in regulatory processes such as cell cycle control.Fer protein is a member of the FPS/FES family of nontransmembrane receptor tyrosine kinases. It regulates cell-cell adhesion and mediates signaling from the cell surface to the cytoskeleton via growth factor receptors. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5811R-HRP)
Fournisseur:
Bioss
Description:
Stress-activated kinase involved in tolerance to glucose starvation. Induces cell-cell detachment by increasing F-actin conversion to G-actin. Expression is induced by CD95 or TNF-alpha, via NF-kappa-B. Protects cells from CD95-mediated apoptosis and is required for the increased motility and invasiveness of CD95-activated tumor cells. Able to phosphorylate 'Ser-464' of LATS1.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-6914R-A350)
Fournisseur:
Bioss
Description:
Tyrosine kinase of the non-receptor type. Probably performs an important function, perhaps in regulatory processes such as cell cycle control.Fer protein is a member of the FPS/FES family of nontransmembrane receptor tyrosine kinases. It regulates cell-cell adhesion and mediates signaling from the cell surface to the cytoskeleton via growth factor receptors. [provided by RefSeq, Jul 2008].
UOM:
1 * 100 µl
Numéro de catalogue:
(BNUM0099-50)
Fournisseur:
Biotium
Description:
This MAb is an excellent marker for human cells in xenographic model research. It reacts specifically with human cells. It is a part of a new panel of reagents, which recognizes subcellular organelles or compartments of human cells. These markers may be useful in identification of these organelles in cells, tissues, and biochemical preparations. MAb 235-1 recognizes an antigen associated with the nuclei in human cells. It can be used to stain the nuclei in cell or tissue preparations and can be used as a nuclear marker in subcellular fractions. It produces a speckled pattern in normal and malignant cells and may be used to stain the nuclei of cells in fixed or frozen tissue sections. It can also be used with paraformaldehyde fixed frozen tissue or cell preparations.
UOM:
1 * 50 µl
Numéro de catalogue:
(BOSSBS-8519R-A350)
Fournisseur:
Bioss
Description:
Calmodulin consists of two glycoproteins, 34 and 39 kDa, sometimes designated epithelial antigen, epithelial specific antigen, and epithelial glycoprotein. The glycoproteins are located on the cell membrane surface and in the cytoplasm of virtually all epithelial cells with the exception of most squamous epithelia, hepatocytes, renal proximal tubular cells, gastric parietal cells and myoepithelial cells. Epithelial Calmodulin is found in the large majority of adenocarcinomas of most sites (50-100% in various studies; as well as neuroendocrine tumours, including small cell carcinoma. Renal cell carcinoma and hepatocellular carcinoma stain in about 30% of the cases. Calmodulin mediates the control of a large number of enzymes and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin Ca(2+) complex are a number of protein kinases and phosphatases. Calmodulin has four functional calcium binding sites.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8519R-FITC)
Fournisseur:
Bioss
Description:
Calmodulin consists of two glycoproteins, 34 and 39 kDa, sometimes designated epithelial antigen, epithelial specific antigen, and epithelial glycoprotein. The glycoproteins are located on the cell membrane surface and in the cytoplasm of virtually all epithelial cells with the exception of most squamous epithelia, hepatocytes, renal proximal tubular cells, gastric parietal cells and myoepithelial cells. Epithelial Calmodulin is found in the large majority of adenocarcinomas of most sites (50-100% in various studies; as well as neuroendocrine tumours, including small cell carcinoma. Renal cell carcinoma and hepatocellular carcinoma stain in about 30% of the cases. Calmodulin mediates the control of a large number of enzymes and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin Ca(2+) complex are a number of protein kinases and phosphatases. Calmodulin has four functional calcium binding sites.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-8519R-HRP)
Fournisseur:
Bioss
Description:
Calmodulin consists of two glycoproteins, 34 and 39 kDa, sometimes designated epithelial antigen, epithelial specific antigen, and epithelial glycoprotein. The glycoproteins are located on the cell membrane surface and in the cytoplasm of virtually all epithelial cells with the exception of most squamous epithelia, hepatocytes, renal proximal tubular cells, gastric parietal cells and myoepithelial cells. Epithelial Calmodulin is found in the large majority of adenocarcinomas of most sites (50-100% in various studies; as well as neuroendocrine tumours, including small cell carcinoma. Renal cell carcinoma and hepatocellular carcinoma stain in about 30% of the cases. Calmodulin mediates the control of a large number of enzymes and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin Ca(2+) complex are a number of protein kinases and phosphatases. Calmodulin has four functional calcium binding sites.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1862R-A555)
Fournisseur:
Bioss
Description:
The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.MMP17 has been reported to be elevated in several tumor cell lines, and is constituitively produced by some normal cell lines. Treatment of cells with Concanavolin A or the phorbol ester TPA stimulates production of MMP17 in some cell types, and the enzyme can be recovered in cell lysates. Shed forms of MMP17 have also been reported.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1862R-CY5)
Fournisseur:
Bioss
Description:
The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.MMP17 has been reported to be elevated in several tumor cell lines, and is constituitively produced by some normal cell lines. Treatment of cells with Concanavolin A or the phorbol ester TPA stimulates production of MMP17 in some cell types, and the enzyme can be recovered in cell lysates. Shed forms of MMP17 have also been reported.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-5587R-A750)
Fournisseur:
Bioss
Description:
Phosphoinositide-3-kinase (PI3K) that phosphorylates PftdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Mediates immune responses. Plays a role in B-cell development, proliferation, migration, and function. Required for B-cell receptor (BCR) signaling. Mediates B-cell proliferation response to anti-IgM, anti-CD40 and IL4 stimulation. Promotes cytokine production in response to TLR4 and TLR9. Required for antibody class switch mediated by TLR9. Involved in the antigen presentation function of B-cells. Involved in B-cell chemotaxis in response to CXCL13 and sphingosine 1-phosphate (S1P). Required for proliferation, signaling and cytokine production of naive, effector and memory T-cells. Required for T-cell receptor (TCR) signaling. Mediates TCR signaling events at the immune synapse. Activation by TCR leads to antigen-dependent memory T-cell migration and retention to antigenic tissues. Together with PIK3CG participates in T-cell development. Contributes to T-helper cell expansion and differentiation. Required for T-cell migration mediated by homing receptors SELL/CD62L, CCR7 and S1PR1 and antigen dependent recruitment of T-cells. Together with PIK3CG is involved in natural killer (NK) cell development and migration towards the sites of inflammation. Participates in NK cell receptor activation. Have a role in NK cell maturation and cytokine production. Together with PIK3CG is involved in neutrophil chemotaxis and extravasation. Together with PIK3CG participates in neutrophil respiratory burst. Have important roles in mast-cell development and mast cell mediated allergic response. Involved in stem cell factor (SCF)-mediated proliferation, adhesion and migration.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
This MAb recognizes a protein of 130 kDa, identified as Ksp-cadherin. Cadherins form a superfamily of related glycoproteins that mediate calcium-dependent cell adhesion and transmit signals from the extracellular matrix to the cytoplasm. Cadherins have been implicated in embryogenesis, tissue morphogenesis, tissue structure maintenance, cell polarization, neoplastic invasiveness and metastasis, and membrane transport. It is suggested that Ksp-cadherin is a marker for terminal differentiation of the basolateral membranes of renal tubular epithelial cells. Within the kidney, Ksp-Cadherin is found exclusively in the basolateral membrane of renal tubular epithelial cells and collecting duct cells, and not in glomeruli, renal interstitial cells, or blood vessels.Ksp-Cadherin has been suggested to distinguish Chromophobe Renal-Cell Carcinoma from Oncocytoma.
Fournisseur:
Biotium
Description:
This MAb recognizes a protein of 130 kDa, identified as Ksp-cadherin. Cadherins form a superfamily of related glycoproteins that mediate calcium-dependent cell adhesion and transmit signals from the extracellular matrix to the cytoplasm. Cadherins have been implicated in embryogenesis, tissue morphogenesis, tissue structure maintenance, cell polarization, neoplastic invasiveness and metastasis, and membrane transport. It is suggested that Ksp-cadherin is a marker for terminal differentiation of the basolateral membranes of renal tubular epithelial cells. Within the kidney, Ksp-Cadherin is found exclusively in the basolateral membrane of renal tubular epithelial cells and collecting duct cells, and not in glomeruli, renal interstitial cells, or blood vessels.Ksp-Cadherin has been suggested to distinguish Chromophobe Renal-Cell Carcinoma from Oncocytoma.
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