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Cathepsin D [CTSD/3082]
Description Cathepsin D is a ubiquitously expressed lysosomal protease that is involved in proteolytic degradation, cell invasion, and apoptosis. It is suspected to play important roles in protein catabolism, antigen processing, degenerative diseases, and cancer progression. Cathepsin D is present in many types of cancer cells. In breast cancer, it is induced by estrogens and its expression is correlated with a higher risk of metastasis and poor disease-free survival. Extensive studies have been also performed to evaluate the clinical and therapeutic implication of Cathepsin D expression in nongynecological solid tumors. Although conflicting results have been observed in some reports, evidence emerging from these studies indicated that Cathepin D seems to facilitate early stages of tumor progression such as cell proliferation and local dissemination. (Shipping Cost: €200.00) Host Mouse Application Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat,Pig (Porcine), Dog -
Caveolin 1 (CAV1) [6C2B2]
Description Identified as a tyrosine phosphorylated protein in Rous sarcoma virus-transformed chick embryo fibroblasts (CEF), caveolin is now known to be ubiquitously expressed. Caveolin (also known as VIP21) localizes to non-clathrin membrane invaginations (caveolae) on the inner surface of the plasma membrane. This transmembrane protein plays a structural role in these specializations. Caveolin is also present at the trans-Golgi network (TGN) and similar quantities are found in apically and basolaterally destined transport vesicles. Caveolin is part of a complex containing glycosylphosphatidylinositol (GPI)-linked molecules and cytoplasmic signaling proteins. Caveolin is a transmembrane adaptor molecule that can simultaneously recognize GPI-linked proteins and interact with downstream cytoplasmic signaling molecules, such as c-yes, Annexin II, and hetero-trimeric G proteins. Caveolin-1 can generate two forms, α and ß, due to alternate splicing of the mRNA. Caveolin-1 forms large lipid-binding ho Host Mouse Application Bioimg , Immunohistochemistry (IHC) , Immunoprecipitation (IP) , Western Blot (WB) Reactivity Human, Mouse, Rat, Dog (Canine), Rabbit -
Caveolin 1 (CAV1) [6C2B2]
Description Identified as a tyrosine phosphorylated protein in Rous sarcoma virus-transformed chick embryo fibroblasts (CEF), caveolin is now known to be ubiquitously expressed. Caveolin (also known as VIP21) localizes to non-clathrin membrane invaginations (caveolae) on the inner surface of the plasma membrane. This transmembrane protein plays a structural role in these specializations. Caveolin is also present at the trans-Golgi network (TGN) and similar quantities are found in apically and basolaterally destined transport vesicles. Caveolin is part of a complex containing glycosylphosphatidylinositol (GPI)-linked molecules and cytoplasmic signaling proteins. Caveolin is a transmembrane adaptor molecule that can simultaneously recognize GPI-linked proteins and interact with downstream cytoplasmic signaling molecules, such as c-yes, Annexin II, and hetero-trimeric G proteins. Caveolin-1 can generate two forms, α and ß, due to alternate splicing of the mRNA. Caveolin-1 forms large lipid-binding ho Host Mouse Application Bioimg , Immunohistochemistry (IHC) , Immunoprecipitation (IP) , Western Blot (WB) Reactivity Human, Mouse, Rat, Dog (Canine), Rabbit -
CD105 (Endoglin/TGF-β Receptor) [SN6]
Description CD105/Endoglin is a Type I membrane glycoprotein located on cell surfaces and is part of the TGF-beta receptor complex. This protein has been found on endothelial cells, activated macrophages, fibroblasts, and smooth-muscle cells. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development. CD105 is highly expressed in endothelial cells during tumor angiogenesis and inflammation, with weak or negative expression in vascular endothelium of normal tissues. Angiogenesis is a promising prognostic marker in a variety of tumors. Endoglin is a more specific and sensitive marker for tumor angiogenesis than CD31 or CD34, as it labels only newly-formed blood vessels and may serve as a prognostic marker for Prostate Adenocarcinoma, and cancers of the lung, stomach, breast, and brain. (Shipping Cost: €200.00) Host Mouse Application Immunohistochemistry (IHC), Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Rat -
CD105 (Endoglin/TGF-β Receptor) [SN6]
Description CD105/Endoglin is a Type I membrane glycoprotein located on cell surfaces and is part of the TGF-beta receptor complex. This protein has been found on endothelial cells, activated macrophages, fibroblasts, and smooth-muscle cells. Endoglin has a role in the development of the cardiovascular system and in vascular remodeling. Its expression is regulated during heart development. CD105 is highly expressed in endothelial cells during tumor angiogenesis and inflammation, with weak or negative expression in vascular endothelium of normal tissues. Angiogenesis is a promising prognostic marker in a variety of tumors. Endoglin is a more specific and sensitive marker for tumor angiogenesis than CD31 or CD34, as it labels only newly-formed blood vessels and may serve as a prognostic marker for Prostate Adenocarcinoma, and cancers of the lung, stomach, breast, and brain. (Shipping Cost: €200.00) Host Mouse Application Immunohistochemistry (IHC), Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Rat -
CD15/FUT4 [FUT4&815]
Description CD15 is expressed on Reed-Sternberg cells of Hodgkin’s disease and by various other cell types including myeloid cells and epithelial cells. Antibodies to CD15 recognize a pentasaccharide sequence occurring in lacto-N-fucopentaose III ceramide (also referred to as X hapten of Lex) found in higher glycolipids and glycoproteins. A review by Arber et al. has reported that antibodies to CD15 demonstrate positive staining in 87% of Hodgkin’s disease including nodular sclerosing, mixed cellularity, and lymphocyte depletion, wherea s the lymphocyte predominant variant exhibits a lower rate of positivity (37%). Among non-Hodgkin’s lymphoma, 13% express CD15 including 4.1% B-cell, 21% T-cell, and 17% null-cell. CD15 expression has also been demonstrated in acute myeloid leukemia (65%) and chronic myelogenous leukemia (96% chronic phase and 54% blast phase). A relatively low level of CD15 expression has been reported in acute lymphoblastic leukemia (5.7% overall) with positivity observed in 7.7% Host Mouse Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC) Reactivity Human, Mouse, Rat -
CD15/FUT4 [FUT4&815]
Description CD15 is expressed on Reed-Sternberg cells of Hodgkin’s disease and by various other cell types including myeloid cells and epithelial cells. Antibodies to CD15 recognize a pentasaccharide sequence occurring in lacto-N-fucopentaose III ceramide (also referred to as X hapten of Lex) found in higher glycolipids and glycoproteins. A review by Arber et al. has reported that antibodies to CD15 demonstrate positive staining in 87% of Hodgkin’s disease including nodular sclerosing, mixed cellularity, and lymphocyte depletion, wherea s the lymphocyte predominant variant exhibits a lower rate of positivity (37%). Among non-Hodgkin’s lymphoma, 13% express CD15 including 4.1% B-cell, 21% T-cell, and 17% null-cell. CD15 expression has also been demonstrated in acute myeloid leukemia (65%) and chronic myelogenous leukemia (96% chronic phase and 54% blast phase). A relatively low level of CD15 expression has been reported in acute lymphoblastic leukemia (5.7% overall) with positivity observed in 7.7% Host Mouse Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC) Reactivity Human, Mouse, Rat -
CD171/NCAM-L1 [C2]
Description Cell adhesion molecules are a family of closely related cell surface glycoproteins involved in cell-cell interactions during growth and are thought to play an important role in embryogenesis and development. Neuronal cell adhesion molecule (NCAM) expression is observed in a variety of human tumors, including neuroblastomas, rhabdomyosarcomas, Wilm's tumors, Ewing's sarcomas and some primitive myeloid malignancies. The NCAM-L1 adhesion molecule (CD171) plays an important role in axon guidance and cell migration in the nervous system. The presence of NCAM-L1 might contribute to tumor progression by promoting cell adhesion and migration and is known to be expressed by neurons, neuroblastomas and other malignant tumors. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat, Rabbit, Chicken, Fish -
CD171/NCAM-L1 [C2]
Description Cell adhesion molecules are a family of closely related cell surface glycoproteins involved in cell-cell interactions during growth and are thought to play an important role in embryogenesis and development. Neuronal cell adhesion molecule (NCAM) expression is observed in a variety of human tumors, including neuroblastomas, rhabdomyosarcomas, Wilm's tumors, Ewing's sarcomas and some primitive myeloid malignancies. The NCAM-L1 adhesion molecule (CD171) plays an important role in axon guidance and cell migration in the nervous system. The presence of NCAM-L1 might contribute to tumor progression by promoting cell adhesion and migration and is known to be expressed by neurons, neuroblastomas and other malignant tumors. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
CD284/Toll-like Receptor 4 [25]
Description This antibody reacts with human Toll-like receptor 4 (TLR4). It is a member of the Toll-like receptor (TLR) family, which plays a fundamental role in pathogen recognition and activation of innate immunity. TLRs are highly conserved from Drosophila to humans and share structural and functional similarities. They recognize pathogen-associated molecular patterns that are expressed on infectious agents, and mediate the production of cytokines necessary for the development of effective immunity. The various TLRs exhibit different patterns of expression. This receptor has been implicated in signal transduction events induced by lipopolysaccharide (LPS) found in most gram-negative bacteria. Mutations in this gene have been associated with differences in LPS responsiveness. Multiple transcript variants encoding different isoforms have been found for this gene. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC) Reactivity Human, Monkey, Dog (Canine),Pig (Porcine), Rat, Guinea Pig