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anti-Human Osteopontin Antikörper:
anti-Mouse (Murine) Osteopontin Antikörper:
anti-Rat (Rattus) Osteopontin Antikörper:
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Human Monoclonal Osteopontin Primary Antibody für ICC, IF - ABIN259958
Kon, Yokosaki, Maeda, Segawa, Horikoshi, Tsukagoshi, Rashid, Morimoto, Inobe, Shijubo, Chambers, Uede: Mapping of functional epitopes of osteopontin by monoclonal antibodies raised against defined internal sequences. in Journal of cellular biochemistry 2002
Show all 17 Pubmed References
Human Polyclonal Osteopontin Primary Antibody für IHC (p), WB - ABIN3042688
Shan, Zhou, He, Feng, Chen, Zhong: Expression of both matrix metalloproteinase-2 and its tissue inhibitor-2 in tunica media of radial artery in uremic patients. in Renal failure 2013
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Dog (Canine) Polyclonal Osteopontin Primary Antibody für IHC (p), IP - ABIN5683675
Kim, Shin: Immunohistochemical study of osteopontin in boar testis. in Journal of veterinary science 2007
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Human Polyclonal Osteopontin Primary Antibody für ELISA, ICC - ABIN250537
Alonso, Tracey, Ortiz, Pérez-Gómez, Palacios, Pollán, Linares, Serrano, Sáez-Castillo, Sánchez, Pajares, Sánchez-Aguilera, Artiga, Piris, Rodríguez-Peralto: A high-throughput study in melanoma identifies epithelial-mesenchymal transition as a major determinant of metastasis. in Cancer research 2007
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Human Polyclonal Osteopontin Primary Antibody für IHC, WB - ABIN6711859
Zhao, Chen, Teng, An, Wang, Ma, Xia: The MEK5/ERK5 pathway mediates fluid shear stress promoted osteoblast differentiation. in Connective tissue research 2014
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Human Polyclonal Osteopontin Primary Antibody für ELISA, WB - ABIN3043353
Yin, Cheng, Qin, Yu, Yu, Zhong, Sun, Zhang: Effects of Naringin on Proliferation and Osteogenic Differentiation of Human Periodontal Ligament Stem Cells In Vitro and In Vivo. in Stem cells international 2015
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Mouse (Murine) Polyclonal Osteopontin Primary Antibody für FACS - ABIN4895890
Kuwahara, Suzuki, Tofukuji, Yamada, Kanoh, Matsumoto, Maruyama, Kometani, Kurosaki, Ohara, Nakayama, Yamashita: The Menin-Bach2 axis is critical for regulating CD4 T-cell senescence and cytokine homeostasis. in Nature communications 2014
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Human Polyclonal Osteopontin Primary Antibody für IHC (fp), IHC - ABIN105163
Ashkar, Weber, Panoutsakopoulou, Sanchirico, Jansson, Zawaideh, Rittling, Denhardt, Glimcher, Cantor: Eta-1 (osteopontin): an early component of type-1 (cell-mediated) immunity. in Science (New York, N.Y.) 2000
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Mouse (Murine) Polyclonal Osteopontin Primary Antibody für IF (cc), IF (p) - ABIN723800
Zhang, Men, Fu, Shan, Ye, Wu, Tao, Liu, Jiang: Contribution of SATB2 to the stronger osteogenic potential of bone marrow stromal cells from craniofacial bones. in Cell and tissue research 2013
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Human Polyclonal Osteopontin Primary Antibody für IF (p), IHC (p) - ABIN723695
Liu, Zhang, Wang, Zhang, Chen, Wu: A Strontium-Modified Titanium Surface Produced by a New Method and Its Biocompatibility In Vitro. in PLoS ONE 2015
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Placental osteopontin expression was reduced in cases of placenta percreta.
These results indicate an involvement in very early stages of angiogenesis and a functional distinction of OPN from human osteoblasts derived from different bone entities.
These data elucidate a better understanding of how total OPN and their splicing isoforms, as well as their associated signaling, may contribute to main aspects of chemoresistance and radioresistance, such as those controlling cell survival, apoptosis, autophagy, stemness, epithelial cell plasticity and associated cell receptors.
The expression of serum OPN was significantly higher in Aortic Dissection patients than in healthy controls.OPN may participate in the formation of Aortic Dissection by activating the Akt and IkappaB signaling pathways.
OPN is essential for maintaining the tight junction complex by allowing occludin to localize at tight junctions. In Caco-2 monolayers, OPN suppression reduced junctional occludin and redistributed it into the intracellular compartment with decreased transepithelial electrical resistance.
OPN was accumulated in CD133+/CD44+ subgroup of HCC cells. Knocking down OPN significantly inhibited the sphere formation and stemness-related genes expression, and delayed tumor initiation of CD133+/CD44+ subgroup of HCC cells.
Particulate matter exposure increased the expression of osteopontin in the bronchial epithelium, serum, and bronchoalveolar lavage fluid of mice. Moreover, particulate matter induced osteopontin expression in human bronchial epithelial cells in a dose and time-dependent manner.
this study demonstrates that Pcsk5 is expressed in bone-forming cells, and that OPN is a novel substrate for PC5/6
OPN, secreted by the vascular smooth muscle cells, is elevated in the circulating plasma and aortic wall of patients with abdominal aortic aneurysms. It can inhibit the induction of the TR1 suppressor cell, leading to an overall proinflammatory state contributing to progressive aortic wall breakdown and dilation.
OPN is a critical component of the antifungal immune response and is essential for effective neutrophil recruitment, inflammatory cytokine production and apoptosis in A. fumigatus keratitis.
Acute-phase plasma OPN could be used as a useful prognostic biomarker in Subarachnoid Hemorrhage.
Results support a role for OPN in mediating pancreatic tumor aggressiveness driven by adipocyte p62 deficiency.
Results provide evidence that OPN facilitates West Nile virus (WNV) neuroinvasion by recruiting WNV-infected polymorphonuclear neutrophils into the brain.
During the interaction of fibroblasts and cancer cells, the increased neoplastic OPN induced by stromal IL-6 accelerated the growth, migration and invasion of cancer cells. More importantly, the authors also showed that soluble OPN could promote head and neck cancer progression via the integrin alphavbeta3-NF-kappa B pathway.
Loss of osteopontin is associated with glioblastoma-promoting microenvironment.
The rare occurrence of antibodies to either osteopontinb or osteopontinc suggests that the breaking of tolerance to fulllength osteopontin is more prevalent in tumor autoimmunity than a reaction to a poorly immunogenic neoepitope.
OPNa is the main contributor to matrix calcification in tested thyroid cancer cells.
Higher SPP1 plasma levels in PMF patients correlate with a more severe fibrosis degree.
Plasma OPN levels were associated with the presence and severity of diabetic retinopathy in Asians with type 2 diabetes.
Study demonstrated that osteopontin exerts an important role in the monocytes/macrophage phenotypic differentiation from hypertensive patients with vascular calcification.
adipocytes progenitor cells from subcutaneous white adipose tissue of lean OPN-deficient mice display an enhanced capacity for differentiating to adipocytes; these alterations may explain the healthy expansion of WAT in the OPN-deficient model which is associated with reduced inflammation and insulin resistance
OPN is essential for maintaining the tight junction complex by allowing occludin to localize at tight junctions. OPN deficiency resulted in an elevated disease activity index, shortened colon length, and aggravated histological signs in mice with DSS-induced acute colitis compared to WT mice. OPN deficiency decreased occludin expression in the colonic mucosa.
Data show that osteopontin (OPN) mediates Na(+)/H(+) exchanger isoform 1 (NHE1)-induced cardiac hypertrophy through p90 ribosomal S6 kinase (p90 RSK).
Amphiregulin-epidermal growth factor receptor (EGFR)-mediated signaling reprogram eosinophils to an inflammatory state with enhanced production of osteopontin, a key profibrotic immunomodulatory protein. The analysis of polyps from patients with eosinophilic chronic rhinosinusitis reveals fibrosis with accumulation of amphiregulin-producing memory T helper 2 cells and osteopontin-producing eosinophils.
we unveil a new role for Opn in setting up a tolerogenic milieu boosting antigenic tolerance induction, thus leading to prevention of allergic airway inflammation
Osteopontin overexpression in non-alcoholic steatohepatitis enhances leptin-mediated fibrogenesis via PI3K/Akt.
The data of this study suggest that OPN is essential for proper astrocytic generation in vitro culture prepared from mouse cerebral cortex.
Study shows that potent pro-inflammatory and pro-fibrotic molecules, osteopontin and galectin-3, are not major disease modulators of laminin alpha2 chain-deficient muscular dystrophy.
Osteopontin activates the NF-kappaB pathway and accelerates the transfer and phosphorylation of p-NF-kappaB P65 from the cytoplasm to the nucleus. In the nucleus, p-NF-kappaB P65 regulates the transcription of genes encoding bone transcription factors, affecting osteogenesis and osteoclast synthesis and the secretion of bone-damaging factors, and ultimately leading to bone destruction.
Study demonstrates that osteopontin has an essential role in modulating macrophage immunological profile and their ability to resist pathogenic forms of amyloid beta-protein.
BSP and pyrophosphates work in concert to direct mineralization in cementum and likely other mineralized tissues.
OPN deficiency has a protective effect against the progressive lipid deposition and glomerulosclerosis elicited by hypercholesterolemia.
The present study demonstrated that OPN deficiency reduced intestinal absorption of cholesterol by suppressing the expression of NPC1L1, thus protecting mice from cholesterol gallstone formation.
OPN regulates CYP7A1 levels and the metabolic fate of liver acetyl-CoA as a result of CHOL and PC metabolism interplay
These results demonstrate that OPN expressed by fatigue-resistant/slow motor neurons is involved in the second-wave neurodegeneration by up-regulating MMP-9 through alphavbeta3 integrin in the mouse model of amyotrophic lateral sclerosis.
Osteopontin is highly induced in carbon nanotube-exposed lungs and plays critical roles in TGF-beta1 signaling activation and myofibroblast differentiation to promote fibrosis development.
study first addressed in detail the LF/fOPN interaction and proposed a LF:fOPN 4/1 maximal stoichiometry.
This implies that a majority of the acidic residues within OPN must be engaged in calcium interaction under physiological conditions.
Genetic variations in the SPP1 promoter affect gene expression and the level of osteopontin secretion into bovine milk.
Osteopontin, osteocalcin and OB-cadherin expression in Synthetic nanohydroxyapatite vs bovine hydroxyapatite cultured Osteoblastic-like cells.
osteopontin (OPN) can serve as a process-directing agent for the intrafibrillar mineralization of collagen.
Results suggest a mechanism of the interaction of UO2(2+) with bone metabolism and a new role for osteopontin (OPN) as a metal transporter.
Upon induction of luteolysis, SPP1 serves as a signaling molecule to recruit or activate immune cells to facilitate luteal regression and tissue degradation.
OPN strongly reduces the amount of biofilm formed in a well-defined laboratory model of acidogenic dental biofilm.
This study demonstrates that adhesion of isolated neonatal rat osteoclasts in vitro was augmented on bovine milk osteopontin (bmOPN) with post-translational modifications (PTMs) compared to human Escherichia-coli-derived recombinant OPN without PTMs.
topographical distribution of both the in vivo and in vitro phosphorylation sites of bone sialoprotein
the bovine osteopontin gene has two functionally distinct clusters of haplotypes within the QTL region on chromosome 6
The relationship between polymorphisms in SPP1 and several factors affecting growth and development in beef cattle was studied.
findings show significant association of osteoponitin variants with milk composition traits
In this study, we have expressed bovine osteopontin in a prokaryotic system and identified the seven amino acid residues phosphorylated in vitro by CKII.
The binding of bovine seminal proteins A1, A2, and 30 kDa and osteopontin to spermatozoa and the effects of oviductal fluid on protein binding are reported.
Results of this study confirm for the first time, the expression of Opn in the ileum and ileocecal lymph node of cattle with paratuberculosis.
Opn may be a key regulator against Mycobacterium avium ssp. paratuberculosis infection
The role of OPN phosphate groups in adsorption to, incorporation into and inhibition of calcium oxalate monohydrate crystals was studied by comparing OPN isoforms differing in phosphorylation.
SPP1 (also known as osteopontin) has a significant role in the modulation of milk protein gene expression.
OPN may act as a carrier protein for LF in milk, and modulate the potent antimicrobial and immunostimulatory activities of the LF protein.
These data suggested that methylation in the OPN promoter plays a crucial role in the regulation of OPN expression that we found in cloned pigs genome.
The striking breed differences between hyperprolific Large White and Meishanin pigs of secreted phospoprotein 1 expression in endometrium suggest that SPP1 may be associated with placental efficiency.
Microglia incubated in vitro with different concentrations (0.1 fM-1 nM) of recombinant osteopontin showed increased proliferation at 10 fM.
results of this study reveal faster growth rate and differences in pig productivity according to genotypes of the SPP1 gene
Osteopontin could play an important role in the development of neointimal hyperplasia in venous conduits after coronary artery bypass grafting.
A different MSSCP pattern was shown in osteopontin which indicates that mutation is located in promotor region; the A --> G transitions was identified in two positions -617 and -608
The 3' terminal end of the first intron of porcine SPP1 harbors a C/EBPbeta binding site and this binding site is negatively affected by the mutant G allele.
in pregnant pigs SPP1 is induced by conceptus estrogen in uterine luminal epithelium and is regulated in a manner coincident with placental progesterone production
osteopontin promotes pathologic mineralization via calcium pyrophosphate dihydrate crystal formation in articular cartilage.
Osteopontin is detected in the majority of germ cells and is involved in spermatogenesis in boar testis.
Infection of urinary tract by Escherichia coli caused higher than normal expression of promoter protein osteopontin and mucosal damage at renal tubular cells.
The SPP1 was principally expressed in motor neurons in lamina IX of the macaque spinal cord.The expression level varied among different spinal segments and correlated positively with neuron size.
results demonstrate that SPP1 is expressed in corticospinal tract neurons in M1 and several other sensorimotor cortices
The protein encoded by this gene is involved in the attachment of osteoclasts to the mineralized bone matrix. The encoded protein is secreted and binds hydroxyapatite with high affinity. The osteoclast vitronectin receptor is found in the cell membrane and may be involved in the binding to this protein. This protein is also a cytokine that upregulates expression of interferon-gamma and interleukin-12. Several transcript variants encoding different isoforms have been found for this gene.
, early T-lymphocyte activation 1
, osteopontin/immunoglobulin alpha 1 heavy chain constant region fusion protein
, secreted phosphoprotein 1 (osteopontin, bone sialoprotein I, early T-lymphocyte activation 1)
, urinary stone protein
, 44 kDa bone phosphoprotein
, bone sialoprotein 1
, calcium oxalate crystal growth inhibitor protein
, early T-lymphocyte activation 1 protein
, osteopontin-like protein
, Sialoprotein (osteopontin)
, bone sialoprotein I
, spp1 protein
, secreted phosphoprotein-1
, LOW QUALITY PROTEIN: osteopontin
, Bone sialoprotein 1