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Search results for: Anti bone sialoprotein II Monoclonal

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#21876355   2011/08/26 To Up

Increased matrix metalloproteinase-2 and bone sialoprotein response to human coronal caries.

It has been suggested that host matrix metalloproteinase-2 (MMP-2) present in dentin may be involved in caries progression, however, its response to caries is not known. Bone sialoprotein (BSP) has been implicated in dentin mineralization and MMP-2 modulation.
L W Boushell, H Nagaoka, H Nagaoka, M Yamauchi

2120 related Products with: Increased matrix metalloproteinase-2 and bone sialoprotein response to human coronal caries.

100 96 wells (1 kit)20 200ug100 20 20 100 96T20 20

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#21703845   2011/06/06 To Up

Long-period gratings in photonic crystal fiber as an optofluidic label-free biosensor.

Using long-period gratings (LPG) inscribed in photonic crystal fiber (PCF) and coupling this structure with an optically aligned flow cell, we have developed an optofluidic refractive index transduction platform for label-free biosensing. The LPG-PCF scheme possesses extremely high sensitivity to the change in refractive index induced by localized binding event in different solution media. A model immunoassay experiment was carried out inside the air channels of PCF by a series of surface modification steps in sequence that include adsorption of poly(allylamine hydrochloride) monolayer, immobilization of anti-rat bone sialoprotein monoclonal primary antibody, and binding interactions with non-specific goat anti-rabbit IgG (H+L) and specific secondary goat anti-mouse IgG (H+L) antibodies. These adsorption and binding events were monitored in situ using the LPG-PCF by measuring the shift of the core-to-cladding mode coupling resonance wavelength. Steady and significant resonance changes, about 0.75 nm per nanometer-thick adsorbed/bound bio-molecules, have been observed following the sequence of the surface events with monolayer sensitivity, suggesting the promising potential of LPG-PCF for biological sensing and evaluation.
Zonghu He, Fei Tian, Yinian Zhu, Nina Lavlinskaia, Henry Du

1531 related Products with: Long-period gratings in photonic crystal fiber as an optofluidic label-free biosensor.

100 μg48 samples900 tests0.1ml (1mg/ml)100 μg100 μg250 1 mg100 μg100 μg96 tests100 μg

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#16778210   // To Up

Bone sialoprotein mediates the tumor cell-targeted prometastatic activity of transforming growth factor beta in a mouse model of breast cancer.

Transforming growth factor betas (TGF-beta) play a dual role in carcinogenesis, functioning as tumor suppressors early in the process, and then switching to act as prometastatic factors in late-stage disease. We have previously shown that high molecular weight TGF-beta antagonists can suppress metastasis without the predicted toxicities. To address the underlying mechanisms, we have used the 4T1 syngeneic mouse model of metastatic breast cancer. Treatment of mice with a monoclonal anti-TGF-beta antibody (1D11) significantly suppressed metastasis of 4T1 cells to the lungs. When metastatic 4T1 cells were recovered from lungs of 1D11-treated and control mice, the most differentially expressed gene was found to be bone sialoprotein (Bsp). Immunostaining confirmed the loss of Bsp protein in 1D11-treated lung metastases, and TGF-beta was shown to regulate and correlate with Bsp expression in vitro. Functionally, knockdown of Bsp in 4T1 cells reduced the ability of TGF-beta to induce local collagen degradation and invasion in vitro, and treatment with recombinant Bsp protected 4T1 cells from complement-mediated lysis. Finally, suppression of Bsp in 4T1 cells reduced metastasis in vivo. We conclude that Bsp is a plausible mediator of at least some of the tumor cell-targeted prometastatic activity of TGF-beta in this model and that Bsp expression in metastases can be successfully suppressed by systemic treatment with anti-TGF-beta antibodies.
Jeong-Seok Nam, Adam M Suchar, Mi-Jin Kang, Christina H Stuelten, Binwu Tang, Aleksandra M Michalowska, Larry W Fisher, Neal S Fedarko, Alka Jain, Jan Pinkas, Scott Lonning, Lalage M Wakefield

2036 related Products with: Bone sialoprotein mediates the tumor cell-targeted prometastatic activity of transforming growth factor beta in a mouse model of breast cancer.

100.00 ug100.00 ug100.00 ug0.1ml (1mg/ml)100.00 ug100.00 ug100.00 ug100.00 ug

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#16465361   // To Up

Treatment of bone metastasis induced by MDA-MB-231 breast cancer cells with an antibody against bone sialoprotein.

The extracellular bone matrix protein bone sialoprotein (BSP) is considered to play an important role in the pathogenesis of lytic skeletal lesions which are associated with severe morbidity in breast, prostate or lung cancer patients. In addition to in vitro studies, nude rats were implanted with 10(5) MDA-MB-231 cells transfected with GFP into a small branch of the femoral artery. Osteolytic lesions of the respective hind leg were detected by X-ray and CT analysis as well as by immunohistochemistry. Exposure of MDA-MB-231GFP cells in vitro to an antibody against BSP (0-400 microg/ml) decreased proliferation, colony formation and migration of these cells by up to 95, 83 and 89 T/C%, respectively. In nude rats, pre-incubation of MDA-MB-231GFP cells prior to inoculation (25-100 microg/ml) reduced the mean osteolytic lesion size to 22 T/C% after 90 days of observation (p<0.05). Treatment of overt lytic metastasis with the anti-BSP antibody (10 mg/kg) resulted in a significantly smaller mean lesion size of 57 T/C% at the end of the observation period (p<0.05) as well as in new bone formation. Immunohistochemical analysis revealed the presence of BSP in MDA-MB-231GFP cells and in vessel endothelium cells during processes such as migration and invasion. In conclusion, an anti-BSP antibody decreased proliferation, colony formation and migration of MDA-MB-231GFP cells in vitro and reduced osteolysis besides inducing bone formation in a nude rat model.
Tobias Bäuerle, Jenny Peterschmitt, Heidegard Hilbig, Fabian Kiessling, Franz P Armbruster, Martin R Berger

2689 related Products with: Treatment of bone metastasis induced by MDA-MB-231 breast cancer cells with an antibody against bone sialoprotein.

100ug Lyophilized100ug Lyophilized100ul100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized

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#15642592   // To Up

Enamel matrix derivative is a potent inhibitor of breast cancer cell attachment to bone.

This study examined whether enamel matrix derivative (EMD) inhibits the adhesion of cancer cells to bone. A typical breast cancer cell line, MCF-7, was used. Conditioned human osteosarcoma cell (Saos-2) medium was used as extracellular bone matrix (ECBM) to measure cell attachment. MCF-7 cells were incubated on ECBM-coated culture plates with or without soluble EMD, Arg-Gly-Asp (RGD) sequence blocking peptides, recombinant bone sialoprotein (rBSP), or specific integrin antibodies, and the attached cells were quantified using toluidine blue staining. EMD markedly reduced the attachment of MCF-7 cells to ECBM in a dose-dependent manner. An RGD peptide (GRGDSP) and recombinant BSP inhibited cell attachment to the same degree as EMD. Similarly, anti-alphavbeta3 integrin antibody strongly reduced cell attachment, whereas anti-alphavbeta5 and anti-beta1 integrin antibodies had less marked effects on cell attachment. These results show that EMD inhibits MCF-7 cell attachment to a bone matrix and that it might be useful as an anti-adhesive agent for breast cancer cells to bone in vivo.
Tadahiro Takayama, Naoto Suzuki, Masataka Narukawa, Harvey A Goldberg, Kichibee Otsuka, Koichi Ito

1278 related Products with: Enamel matrix derivative is a potent inhibitor of breast cancer cell attachment to bone.

100ug Lyophilized200 ug100ug Lyophilized100ug Lyophilized

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#15619669   2004/10/18 To Up

Immortalization of cementoblast progenitor cells with Bmi-1 and TERT.

A cementoblast progenitor cell line designated BCPb8 was successfully isolated from dental follicle cells immortalized with Bmi-1 and hTERT. BCPb8 showed the potential to differentiate into cementoblasts on implantation into immunodeficient mice. BCPb8 was confirmed to be the first established cementoblast progenitor cell line and will provide a useful model for investigating cementogenesis.
Masahiro Saito, Keisuke Handa, Tohru Kiyono, Shintaro Hattori, Takamasa Yokoi, Takanori Tsubakimoto, Hidemitsu Harada, Toshihide Noguchi, Minoru Toyoda, Sadao Sato, Toshio Teranaka

2646 related Products with: Immortalization of cementoblast progenitor cells with Bmi-1 and TERT.

100ul100ml2.5 mg 100 G10ml1 mg10 mg 25 G100ml 25 G25 mg25 mg

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#11759863   // To Up

Attachment of human periodontal ligament cells to enamel matrix-derived protein is mediated via interaction between BSP-like molecules and integrin alpha(v)beta3.

Although enamel matrix-derived protein (EMD) can stimulate attachment of human periodontal ligament (HPDL) cells to the root surface, the biological mechanism of this phenomenon is unclear. The purpose of this study was to determine which molecules in EMD are involved in the attachment of HPDL cells, and which types of integrins on the cell surface mediate the interaction between the cells and EMD.
N Suzuki, M Ohyama, M Maeno, K Ito, K Otsuka

1725 related Products with: Attachment of human periodontal ligament cells to enamel matrix-derived protein is mediated via interaction between BSP-like molecules and integrin alpha(v)beta3.

1mg5100ug Lyophilized10 100.00 ug10100ug Lyophilized5ug55020100ug Lyophilized

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#10785511   // To Up

Bone sialoprotein mediates human endothelial cell attachment and migration and promotes angiogenesis.

Bone sialoprotein (BSP) is a secreted glycoprotein primarily found in sites of biomineralization. Recently, we demonstrated that BSP is strongly upregulated in osteotropic cancers and particularly those that exhibit microcalcifications. BSP contains an Arg-Gly-Asp (RGD) motif found in other adhesive molecules that interact with cellular integrins. In bone, BSP has been shown to mediate the attachment of osteoblasts and osteoclasts via alpha(v)beta(3) integrin receptors. Ligands for alpha(v)beta(3) integrin are considered to play a central role during angiogenesis. Therefore, we used human umbilical vein endothelial cells (HUVECs) to study the potential role of BSP in angiogenesis. We found that purified eukaryotic recombinant human BSP (rhBSP) is able to promote both adhesion and chemotactic migration of HUVECs in a dose-dependent manner. These interactions involve HUVEC alpha(v)beta(3) integrin receptors and the RGD domain of BSP. Indeed, HUVECs attach to a recombinant BSP fragment containing the RGD domain, whereas this response is not observed with the same fragment in which RGD has been mutated to Lys-Ala-Glu (KAE). A cyclic RGD BSP peptide inhibits both adhesion and migration of HUVECs to rhBSP. Moreover, anti-alpha(v)beta(3) but not anti-alpha(v)beta(5) monoclonal antibodies also prevent BSP-mediated adhesion and migration of HUVECs. We observed that both rhBSP and the RGD BSP recombinant fragment stimulated ongoing angiogenesis on the chorioallantoic chick membrane assay. BSP angiogenic activity was inhibited by anti-alpha(v)beta(3) antibody, and the KAE BSP fragment was inactive. Our findings represent the first report implicating BSP in angiogenesis. BSP could play a critical role in angiogenesis associated with bone formation and with tumor growth and metastatic dissemination.
A Bellahcène, K Bonjean, B Fohr, N S Fedarko, F A Robey, M F Young, L W Fisher, V Castronovo

1822 related Products with: Bone sialoprotein mediates human endothelial cell attachment and migration and promotes angiogenesis.

1.00 flask1.00 flask0.5 ml1.00 flask1.00 flask1.00 flask1000 20 1.00 flask1.00 flask1.00 flask

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#10773110   // To Up

Bone sialoprotein (BSP) is a crucial factor for the expression of osteoblastic phenotypes of bone marrow cells cultured on type I collagen matrix.

In this study, we demonstrated that type I collagen matrix induced the expression of osteoblastic phenotypes of bone marrow cells, and that antibone sialoprotein (BSP) monoclonal antibody suppressed the expression of these phenotypes. On the other hand, BSP accelerated the expression of osteoblastic phenotypes of bone marrow cells. The adherent bone marrow cells were harvested from rat femur and cultured on type I collagen matrix gels in medium containing 15% fetal calf serum, neither beta-glycerophosphate nor glucocorticoid. Cells showed osteoblastic phenotypes (high alkaline phosphatase activity, osteocalcin synthesis, and responsiveness against parathyroid hormone) on collagen matrix gels at week 3 after the inoculation, and simultaneously, BSP was detected in the conditioned medium by Western blotting using an anti-BSP monoclonal antibody. However, cells in the conventional culture dishes did not show osteoblastic phenotypes during the experimental period. To investigate the physiological function of BSP in osteoblastic differentiation, bone marrow cells were cultured on collagen matrix with an anti-BSP monoclonal antibody for 3 weeks. This treatment suppressed the expression of the osteoblastic phenotypes, and the effect of the antibody was abolished by the addition of bovine bone BSP. Furthermore, bovine bone BSP stimulated the expression of osteoblastic phenotypes of bone marrow cells. Our results indicate that BSP plays a crucial role in the expression of osteoblastic phenotypes of bone marrow cells.
M Mizuno, T Imai, R Fujisawa, H Tani, Y Kuboki

1098 related Products with: Bone sialoprotein (BSP) is a crucial factor for the expression of osteoblastic phenotypes of bone marrow cells cultured on type I collagen matrix.

100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized

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#7666059   // To Up

Expression of bone-related protein messenger RNA in human meningiomas: possible involvement of osteopontin in development of psammoma bodies.

Meningiomas often contain concentric calcified foci, referred to as psammoma bodies. Since calcium phosphate deposits in both psammoma bodies and bone tissues, we examined whether messenger (m) RNA of bone-related extracellular matrix proteins and bone morphogenetic proteins (BMP) were expressed in human meningioma tissues. Northern blotting demonstrated the expression of osteopontin (OPN), matrix Gla protein (MGP), osteonectin (ON) and BMP-4 mRNA but not bone sialoprotein, osteocalcin and BMP-2 mRNA. In situ hybridization revealed that most OPN mRNA-expressing cells were located around the psammoma bodies in meningothelial whorls. Moreover, combination of in situ hybridization and immunohistochemistry on serial sections showed that the OPN mRNA-expressing cells were CD68-positive, suggesting they were macrophages. Immunohistochemistry with anti-OPN antibody and von Kossa staining on the adjacent section showed that the deposition site of OPN protein was consistent with that of calcium phosphate. Neither MGP nor ON mRNA expression appeared to correlate with the calcification. The present result suggests that OPN produced by CD68-positive macrophages may play a significant role for development of psammoma bodies in meningiomas.
S Hirota, Y Nakajima, T Yoshimine, K Kohri, S Nomura, M Taneda, T Hayakawa, Y Kitamura

2784 related Products with: Expression of bone-related protein messenger RNA in human meningiomas: possible involvement of osteopontin in development of psammoma bodies.

1mg2ug100 μg5ug100 μg5ug100ug Lyophilized1mg50 1mg2ug100ug Lyophilized

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