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cell+culture+plates
Numéro de catalogue:
(BOSSBS-3384R-FITC)
Fournisseur:
Bioss
Description:
Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. Phosphorylates PTK2/FAK1. Regulates both cell death/survival balance and positional information. Required for the molecular mechanisms orchestration during intestine organogenesis; involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e.g. ITGB1 and ITGB3)-dependent manner. Involved in the development of the neural crest. Active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage. Acts as a dependence receptor; in the presence of the ligand GDNF in somatotrophs (within pituitary), promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF. Regulates nociceptor survival and size. Triggers the differentiation of rapidly adapting (RA) mechanoreceptors. Mediator of several diseases such as neuroendocrine cancers; these diseases are characterized by aberrant integrins-regulated cell migration.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-2793R-FITC)
Fournisseur:
Bioss
Description:
Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. Phosphorylates PTK2/FAK1. Regulates both cell death/survival balance and positional information. Required for the molecular mechanisms orchestration during intestine organogenesis; involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e.g. ITGB1 and ITGB3)-dependent manner. Involved in the development of the neural crest. Active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage. Acts as a dependence receptor; in the presence of the ligand GDNF in somatotrophs (within pituitary), promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF. Regulates nociceptor survival and size. Triggers the differentiation of rapidly adapting (RA) mechanoreceptors. Mediator of several diseases such as neuroendocrine cancers; these diseases are characterized by aberrant integrins-regulated cell migration.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3384R-A555)
Fournisseur:
Bioss
Description:
Receptor tyrosine-protein kinase involved in numerous cellular mechanisms including cell proliferation, neuronal navigation, cell migration, and cell differentiation upon binding with glial cell derived neurotrophic factor family ligands. Phosphorylates PTK2/FAK1. Regulates both cell death/survival balance and positional information. Required for the molecular mechanisms orchestration during intestine organogenesis; involved in the development of enteric nervous system and renal organogenesis during embryonic life, and promotes the formation of Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue. Modulates cell adhesion via its cleavage by caspase in sympathetic neurons and mediates cell migration in an integrin (e.g. ITGB1 and ITGB3)-dependent manner. Involved in the development of the neural crest. Active in the absence of ligand, triggering apoptosis through a mechanism that requires receptor intracellular caspase cleavage. Acts as a dependence receptor; in the presence of the ligand GDNF in somatotrophs (within pituitary), promotes survival and down regulates growth hormone (GH) production, but triggers apoptosis in absence of GDNF. Regulates nociceptor survival and size. Triggers the differentiation of rapidly adapting (RA) mechanoreceptors. Mediator of several diseases such as neuroendocrine cancers; these diseases are characterized by aberrant integrins-regulated cell migration.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-1862R-CY3)
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-6995R-HRP)
Fournisseur:
Bioss
Description:
Polyadenylation of mRNA precursors is a two-step reaction that requires multiple protein factors. The first step, endonucleolytic cleavage of polyadenylation substrates, requires CstF (cleavage stimulation factor), a heterotrimer that is composed of three distinct subunits. CstF-64 contains an RNA binding domain and is responsible for the RNA binding activity of CstF. CstF-64 is expressed in all somatic cells and in pre- and postmeiotic, but not meiotic, germ cells. However, a large variant of CstF-64, called t CstF-64, is abundantly expressed in meiotic and postmeiotic cells in the testis and to a lesser extent in the brain, and promotes the germ cell pattern of polyadenylation. The gene encoding CstF-64 (designated CSTF2) maps to the X chromosome, whereas t CstF-64 is encoded by an autosomal gene. The increase in CstF-64 concentration during B cell activation switches IgM heavy chain mRNA expression from membrane-bound to secreted forms, suggesting that CstF-64 plays a key role in regulating IgM heavy chain expression during B cell differentiation.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-11073R-A750)
Fournisseur:
Bioss
Description:
The cadherins are a family of Ca2+-dependent adhesion molecules that function to mediate cell-cell binding events that are critical to the maintenance of cell structure and morphogenesis. EY-cadherin, also known as CDH18 (cadherin 18), CDH14 (cadherin 14), CDH24 or CDH14L, is a 790 amino acid single-pass type I membrane protein that contains five cadherin domains. One of several members of the cadherin superfamily, EY-cadherin functions as a type II classical cadherin that is expressed specifically in the central nervous system (CNS), where it plays a role in cell-cell binding events. Specifically, EY-cadherin is thought to be involved in axon guidance and outgrowth, as well as synaptic adhesion within the CNS. EY-cadherin contains a highly conserved C-terminal domain characteristic of all cadherins, but lacks the HAV cell adhesion sequence that is specific to type I cadherins. The gene encoding EY-cadherin is located within a region on chromosome five that is commonly deleted in carcinomas, implicating EY-cadherin as a potential tumour suppressor.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
This MAb reacts with the HLA-DRB1 antigen, a member of MHC class II molecules. It does not cross react with HLA-DP and HLA-DQ. It binds a conformational epitope on HLA-DR, which depends on the correct folding of the α/β heterodimer. This MAb has been reported to block mixed lymphocyte reactions. The L243 antibody recognizes a different epitope than the LN3 monoclonal antibody, and these antibodies do not cross-block binding to each other's respective epitopes. HLA-DR is a heterodimeric cell surface glycoprotein comprised of a 36kD alpha (heavy) chain and a 28kD beta (light) chain. It is expressed on B-cells, activated T-cells, monocytes/macrophages, dendritic cells and other non-professional APCs. In conjunction with the CD3/TCR complex and CD4 molecules, HLA-DR is critical for efficient peptide presentation to CD4 T cells. It is an excellent histiocytic marker in paraffin sections producing intense staining. True histiocytic neoplasms are similarly positive. HLA-DR antigens also occur on a variety of epithelial cells and their corresponding neoplastic counterparts.
Fournisseur:
Biotium
Description:
This MAb reacts with the HLA-DRB1 antigen, a member of MHC class II molecules. It does not cross react with HLA-DP and HLA-DQ. It binds a conformational epitope on HLA-DR, which depends on the correct folding of the α/β heterodimer. This MAb has been reported to block mixed lymphocyte reactions. The L243 antibody recognizes a different epitope than the LN3 monoclonal antibody, and these antibodies do not cross-block binding to each other's respective epitopes. HLA-DR is a heterodimeric cell surface glycoprotein comprised of a 36kD alpha (heavy) chain and a 28kD beta (light) chain. It is expressed on B-cells, activated T-cells, monocytes/macrophages, dendritic cells and other non-professional APCs. In conjunction with the CD3/TCR complex and CD4 molecules, HLA-DR is critical for efficient peptide presentation to CD4 T cells. It is an excellent histiocytic marker in paraffin sections producing intense staining. True histiocytic neoplasms are similarly positive. HLA-DR antigens also occur on a variety of epithelial cells and their corresponding neoplastic counterparts.
Numéro de catalogue:
(BOSSBS-3353R-A680)
Fournisseur:
Bioss
Description:
Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilisation of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis.
UOM:
1 * 100 µl
Numéro de catalogue:
(BOSSBS-3353R-A488)
Fournisseur:
Bioss
Description:
Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylation and inhibition of proapoptotic proteins (BAD, MAP3K5, FOXO3). Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase of transcriptional activity. The stabilization of MYC exerted by PIM1 might explain partly the strong synergism between these two oncogenes in tumorigenesis. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Phosphorylation of MAP3K5, an other proapoptotic protein, by PIM1, significantly decreases MAP3K5 kinase activity and inhibits MAP3K5-mediated phosphorylation of JNK and JNK/p38MAPK subsequently reducing caspase-3 activation and cell apoptosis. Stimulates cell cycle progression at the G1-S and G2-M transitions by phosphorylation of CDC25A and CDC25C. Phosphorylation of CDKN1A, a regulator of cell cycle progression at G1, results in the relocation of CDKN1A to the cytoplasm and enhanced CDKN1A protein stability. Promote cell cycle progression and tumorigenesis by down-regulating expression of a regulator of cell cycle progression, CDKN1B, at both transcriptional and post-translational levels. Phosphorylation of CDKN1B,induces 14-3-3-proteins binding, nuclear export and proteasome-dependent degradation. May affect the structure or silencing of chromatin by phosphorylating HP1 gamma/CBX3. Acts also as a regulator of homing and migration of bone marrow cells involving functional interaction with the CXCL12-CXCR4 signaling axis.
UOM:
1 * 100 µl
Fournisseur:
Biotium
Description:
Recognizes a protein of a disulfide-linked 120 kDa dimer, identified as CD27 (Workshop VI; Code 6T-028). CD27 is expressed on the majority of peripheral T cells, medullary thymocytes, memory-type B cells, and natural killer cells. It is a transmembrane phosphoglycoprotein that belongs to the tumor necrosis factor receptor (TNFR) superfamily. CD27 binds to its ligand CD70, a member of the TNF family, and induces T-cell co-stimulation and B-cell activation. It also interacts with TRAFs and is involved in activation of NFB and SAPK/JNK and induces apoptosis.
Fournisseur:
Biotium
Description:
Recognizes a protein of a disulfide-linked 120 kDa dimer, identified as CD27 (Workshop VI; Code 6T-028). CD27 is expressed on the majority of peripheral T cells, medullary thymocytes, memory-type B cells, and natural killer cells. It is a transmembrane phosphoglycoprotein that belongs to the tumor necrosis factor receptor (TNFR) superfamily. CD27 binds to its ligand CD70, a member of the TNF family, and induces T-cell co-stimulation and B-cell activation. It also interacts with TRAFs and is involved in activation of NFB and SAPK/JNK and induces apoptosis.
Fournisseur:
Biotium
Description:
Recognizes a protein of a disulfide-linked 120 kDa dimer, identified as CD27 (Workshop VI; Code 6T-028). CD27 is expressed on the majority of peripheral T cells, medullary thymocytes, memory-type B cells, and natural killer cells. It is a transmembrane phosphoglycoprotein that belongs to the tumor necrosis factor receptor (TNFR) superfamily. CD27 binds to its ligand CD70, a member of the TNF family, and induces T-cell co-stimulation and B-cell activation. It also interacts with TRAFs and is involved in activation of NFB and SAPK/JNK and induces apoptosis.
Fournisseur:
Biotium
Description:
Recognizes a protein of a disulfide-linked 120 kDa dimer, identified as CD27 (Workshop VI; Code 6T-028). CD27 is expressed on the majority of peripheral T cells, medullary thymocytes, memory-type B cells, and natural killer cells. It is a transmembrane phosphoglycoprotein that belongs to the tumor necrosis factor receptor (TNFR) superfamily. CD27 binds to its ligand CD70, a member of the TNF family, and induces T-cell co-stimulation and B-cell activation. It also interacts with TRAFs and is involved in activation of NFB and SAPK/JNK and induces apoptosis.
Fournisseur:
Biotium
Description:
CD2 interacts through its amino-terminal domain with the extracellular domain of CD58 (also designated CD2 ligand) to mediate cell adhesion. CD2/CD58 binding can enhance antigen-specific T cell activation. CD2 is a transmembrane glycoprotein that is expressed on peripheral blood T lymphocytes, NK cells and thymocytes. CD58 is a heavily glycosylated protein with a broad tissue distribution in hematopoietic and other cells, including endothelium. Interaction between CD2 and its counter receptor LFA3 (CD58) on opposing cells optimizes immune system recognition, thereby facilitating communication between helper T lymphocytes and antigen-presenting cells, as well as between cytolytic effectors and target cells.
Fournisseur:
Biotium
Description:
CD2 interacts through its amino-terminal domain with the extracellular domain of CD58 (also designated CD2 ligand) to mediate cell adhesion. CD2/CD58 binding can enhance antigen-specific T cell activation. CD2 is a transmembrane glycoprotein that is expressed on peripheral blood T lymphocytes, NK cells and thymocytes. CD58 is a heavily glycosylated protein with a broad tissue distribution in hematopoietic and other cells, including endothelium. Interaction between CD2 and its counter receptor LFA3 (CD58) on opposing cells optimizes immune system recognition, thereby facilitating communication between helper T lymphocytes and antigen-presenting cells, as well as between cytolytic effectors and target cells.
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