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Catalog Number: (10751-108)
Supplier: Prosci
Description: PLAC1 Antibody: PLAC1 was initially identified as a protein expressed specifically in the placenta and other cells derived from the trophoblast lineage during embryonic development, but has also been found to be expressed ectopically in a wide range of human malignancies, particularly breast cancers. PLAC1 is a membrane-associated protein that is thought to serve a receptor-like function modulating cell-cell or ligand receptor interactions unique to the maternal-placental interface. Decreased expression of PLAC1 is associated with decreased expression of cyclin D1 and reduced expression of AKT kinase, which, combined with the fact that PLAC1 is expressed on the surface of cancer cells, suggests that PLAC1 may be an effective candidate for immunotherapeutic treatments of cancer.


Supplier: Diagnostic Biosystems
Description: This MAb recognizes human 17 to 26kDa protein, which is identified as cytokine TNF-α (Tumor Necrosis Factor-alpha). Monomeric human TNF-α is a 157 amino acid protein (non-glycosylated) with a reported molecular weight of 17 kDa and can be expressed as a free molecule, also TNF-α is generated as a precursor form called transmembrane TNF-α can be expressed as a cell surface type II polypeptide consisting of 233 amino acid residues molecular weight 26 kDa. TNF-α is an important cell-signaling component of the immune system. It is a protein secreted by LPS stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF-α is currently being evaluated in treatment of certain cancers and AIDS Related Complex.

Catalog Number: (CA76634-486)
Supplier: Diagnostic Biosystems
Description: This MAb recognizes human 17-26kDa protein, which is identified as cytokine TNF-α (Tumor Necrosis Factor-alpha). Monomeric human TNF-α is a 157 amino acid protein (non-glycosylated) with a reported molecular weight of 17 kDa and can be expressed as a free molecule, also TNF-α is generated as a precursor form called transmembrane TNF-α can be expressed as a cell surface type II polypeptide consisting of 233 amino acid residues molecular weight 26 kDa. TNF-α is an important cell-signaling component of the immune system. It is a protein secreted by LPS stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF-α is currently being evaluated in treatment of certain cancers and AIDS Related Complex.


Catalog Number: (89417-636)
Supplier: Prosci
Description: PLAC1 Antibody: PLAC1 was initially identified as a protein expressed specifically in the placenta and other cells derived from the trophoblast lineage during embryonic development, but has also been found to be expressed ectopically in a wide range of human malignancies, particularly breast cancers. PLAC1 is a membrane-associated protein that is thought to serve a receptor-like function modulating cell-cell or ligand receptor interactions unique to the maternal-placental interface. Decreased expression of PLAC1 is associated with decreased expression of cyclin D1 and reduced expression of AKT kinase, which, combined with the fact that PLAC1 is expressed on the surface of cancer cells, suggests that PLAC1 may be an effective candidate for immunotherapeutic treatments of cancer.


Catalog Number: (21913-194)
Supplier: Berkshire
Description: These extremely clean and pure polyester/rayon non-woven wipers are made from soft, absorbent Dupont™ Sontara® MicroPure LP fabric.

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Supplier: Berkshire
Description: Ideal for absorbing spills of solvents and deionized water in ISO Class 5 (FED-STD-209E Class 100/M3.5) environments.
Supplier: Biotium
Description: This MAb specifically precipitates heterogeneous material of high MW, identified as perlecan, a major heparan-sulfate proteoglycan (HSPG) within all basement membranes and cell surfaces. It does not cross-react with laminin, fibronectin, or dermatran sulfate proteoglycan. Because of perlecan s strategic location and ability to store and protect growth factors, it has been strongly implicated in the control of tumor cell growth and metastatic behavior. Perlecan possesses angiogenic and growth-promoting attributes primarily by acting as a co-receptor for basic fibroblast growth factor (FGF-2). Suppression of perlecan causes substantial inhibition of neoplastic growth and neovascularization. Thus, perlecan is a potent inducer of neoplasm growth and angiogenesis in vivo and therapeutic interventions targeting this key modulator of tumor progression may improve neoplastic treatment.

Supplier: Thermo Fisher Scientific
Description: One-piece 96-well MicroWell™ plates are designed for colorimetric, fluorescent, and luminescent immunoassays and binding assays
Supplier: Thermo Fisher Scientific
Description: These Terasaki-style mini trays are ideal for serotyping, HLA applications, microlymphocytotoxicity, cell cloning studies, protein crystallization, and sequencing reactions.
Supplier: Biotium
Description: This MAb specifically precipitates heterogeneous material of high MW, identified as perlecan, a major heparan-sulfate proteoglycan (HSPG) within all basement membranes and cell surfaces. It does not cross-react with laminin, fibronectin, or dermatran sulfate proteoglycan. Because of perlecan s strategic location and ability to store and protect growth factors, it has been strongly implicated in the control of tumor cell growth and metastatic behavior. Perlecan possesses angiogenic and growth-promoting attributes primarily by acting as a co-receptor for basic fibroblast growth factor (FGF-2). Suppression of perlecan causes substantial inhibition of neoplastic growth and neovascularization. Thus, perlecan is a potent inducer of neoplasm growth and angiogenesis in vivo and therapeutic interventions targeting this key modulator of tumor progression may improve neoplastic treatment.

Catalog Number: (75981-216)
Supplier: Biotium
Description: This MAb specifically precipitates heterogeneous material of high MW, identified as perlecan, a major heparan-sulfate proteoglycan (HSPG) within all basement membranes and cell surfaces. It does not cross-react with laminin, fibronectin, or dermatran sulfate proteoglycan. Because of perlecan s strategic location and ability to store and protect growth factors, it has been strongly implicated in the control of tumor cell growth and metastatic behavior. Perlecan possesses angiogenic and growth-promoting attributes primarily by acting as a co-receptor for basic fibroblast growth factor (FGF-2). Suppression of perlecan causes substantial inhibition of neoplastic growth and neovascularization. Thus, perlecan is a potent inducer of neoplasm growth and angiogenesis in vivo and therapeutic interventions targeting this key modulator of tumor progression may improve neoplastic treatment.


Catalog Number: (75793-636)
Supplier: Prosci
Description: ANGPTL4 (Angiopoietin-like protein 4) mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorigenesis and directly regulates lipid, glucose, and energy metabolism. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. ANGPTL4 is a protein consisting of an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain (FLD). Both domains have distinct biological functions. The coiled-coil domain is responsible for the inhibitory effects on lipoprotein lipase (LPL) converting the active form of LPL into an inactive form, and the FLD domain mediates its antiangiogenic functions. The coiled coil and the FLD domains are separated by a short linker that can be cleaved after secretion. ANGPTL4 appears on the cell surface as the full-length form, where it can be released by heparin treatment. ANGPTL4 protein is then proteolytically cleaved by proprotein convertases (PCs), including furin, PC5/6, paired basic amino acid-cleaving enzyme 4, and PC7.


Catalog Number: (75793-634)
Supplier: Prosci
Description: ANGPTL4 (Angiopoietin-like protein 4) mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorigenesis and directly regulates lipid, glucose, and energy metabolism. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. ANGPTL4 is a protein consisting of an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain (FLD). Both domains have distinct biological functions. The coiled-coil domain is responsible for the inhibitory effects on lipoprotein lipase (LPL) converting the active form of LPL into an inactive form, and the FLD domain mediates its antiangiogenic functions. The coiled coil and the FLD domains are separated by a short linker that can be cleaved after secretion. ANGPTL4 appears on the cell surface as the full-length form, where it can be released by heparin treatment. ANGPTL4 protein is then proteolytically cleaved by proprotein convertases (PCs), including furin, PC5/6, paired basic amino acid-cleaving enzyme 4, and PC7.


Catalog Number: (75793-656)
Supplier: Prosci
Description: ANGPTL4 (Angiopoietin-like protein 4) mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorigenesis and directly regulates lipid, glucose, and energy metabolism. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. ANGPTL4 is a protein consisting of an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain (FLD). Both domains have distinct biological functions. The coiled-coil domain is responsible for the inhibitory effects on lipoprotein lipase (LPL) converting the active form of LPL into an inactive form, and the FLD domain mediates its antiangiogenic functions. The coiled coil and the FLD domains are separated by a short linker that can be cleaved after secretion. ANGPTL4 appears on the cell surface as the full-length form, where it can be released by heparin treatment. ANGPTL4 protein is then proteolytically cleaved by proprotein convertases (PCs), including furin, PC5/6, paired basic amino acid-cleaving enzyme 4, and PC7.


Catalog Number: (75793-364)
Supplier: Prosci
Description: ANGPTL4 mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorgenesis and directly regulates lipid, glucose, and energy metabolism. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. ANGPTL4 is a protein consisting of an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain (FLD). Both domains have distinct biological functions. The coiled-coil domain is responsible for the inhibitory effects on lipoprotein lipase (LPL) converting the active form of LPL into an inactive form, and the FLD domain mediates its antiangiogenic functions. The coiled coil and the FLD domains are separated by a short linker that can be cleaved after secretion. ANGPTL4 appears on the cell surface as the full-length form, where it can be released by heparin treatment. ANGPTL4 protein is then proteolytically cleaved by proprotein convertases (PCs), including furin, PC5/6, paired basic amino acid-cleaving enzyme 4, and PC7.


Catalog Number: (75793-654)
Supplier: Prosci
Description: ANGPTL4 (Angiopoietin-like protein 4) mainly expressed in endothelial cells (hypoxia-induced). Regulates angiogenesis and modulates tumorigenesis and directly regulates lipid, glucose, and energy metabolism. Inhibits proliferation, migration, and tubule formation of endothelial cells and reduces vascular leakage. ANGPTL4 is a protein consisting of an N-terminal coiled-coil domain and a C-terminal fibrinogen-like domain (FLD). Both domains have distinct biological functions. The coiled-coil domain is responsible for the inhibitory effects on lipoprotein lipase (LPL) converting the active form of LPL into an inactive form, and the FLD domain mediates its antiangiogenic functions. The coiled coil and the FLD domains are separated by a short linker that can be cleaved after secretion. ANGPTL4 appears on the cell surface as the full-length form, where it can be released by heparin treatment. ANGPTL4 protein is then proteolytically cleaved by proprotein convertases (PCs), including furin, PC5/6, paired basic amino acid-cleaving enzyme 4, and PC7.


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