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Mouse (Murine) Polyclonal SPARC Primary Antibody for CyTOF, FACS - ABIN4899335
Arnold, Rivera, Carbon, Toombs, Chang, Bradshaw, Brekken: Losartan slows pancreatic tumor progression and extends survival of SPARC-null mice by abrogating aberrant TGF? activation. in PLoS ONE 2012
Show all 11 Pubmed References
Human Polyclonal SPARC Primary Antibody for CyTOF, FACS - ABIN4899340
Aguilera, Rivera, Hur, Carbon, Toombs, Goldstein, Dellinger, Castrillon, Brekken: Collagen signaling enhances tumor progression after anti-VEGF therapy in a murine model of pancreatic ductal adenocarcinoma. in Cancer research 2014
Show all 7 Pubmed References
Mouse (Murine) Monoclonal SPARC Primary Antibody for CyTOF, FACS - ABIN4899334
Weaver, Sage, Yan: Absence of SPARC in lens epithelial cells results in altered adhesion and extracellular matrix production in vitro. in Journal of cellular biochemistry 2006
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Human Polyclonal SPARC Primary Antibody for IF (p), IHC (p) - ABIN738141
Chen, Wang, Xi, Xue, He, Zhang, Zhao: SPARC is a key regulator of proliferation, apoptosis and invasion in human ovarian cancer. in PLoS ONE 2012
Show all 3 Pubmed References
Human Monoclonal SPARC Primary Antibody for CyTOF, FACS - ABIN4899338
Moreno, Ball, Andrade, McDermid, Stanimirovic: Insulin-like growth factor binding protein-4 (IGFBP-4) is a novel anti-angiogenic and anti-tumorigenic mediator secreted by dibutyryl cyclic AMP (dB-cAMP)-differentiated glioblastoma cells. in Glia 2006
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Human Polyclonal SPARC Primary Antibody for FACS, WB - ABIN4899336
Xu, Ping, Yin, Xiao, Xiang, Ballantyne, Wu, Li: Elevated plasma SPARC levels are associated with insulin resistance, dyslipidemia, and inflammation in gestational diabetes mellitus. in PLoS ONE 2013
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Human Polyclonal SPARC Primary Antibody for IHC, IHC (fro) - ABIN4355498
Kato, Nicholson, Neiman, Rantalainen, Holmes, Barrett, Uhlén, Nilsson, Spector, Schwenk: Variance decomposition of protein profiles from antibody arrays using a longitudinal twin model. in Proteome science 2011
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Human Monoclonal SPARC Primary Antibody for ELISA, WB - ABIN562974
Piconese, Costanza, Tripodo, Sangaletti, Musio, Pittoni, Poliani, Burocchi, Passafaro, Gorzanelli, Vitali, Chiodoni, Barnaba, Pedotti, Colombo: The matricellular protein SPARC supports follicular dendritic cell networking toward Th17 responses. in Journal of autoimmunity 2011
Cow (Bovine) Polyclonal SPARC Primary Antibody for IHC, WB - ABIN2789396
Boyineni, Tanpure, Gnanamony, Antony, Fernández, Lin, Pinson, Gondi: SPARC overexpression combined with radiation retards angiogenesis by suppressing VEGF-A via miR‑410 in human neuroblastoma cells. in International journal of oncology 2016
SPARC treatment enhances the epithelial mesenchymal transition signaling pathway via activation of AKT (show AKT1 Antibodies), and exogenous SPARC and tumor expressing SPARC might be associated with tumor progression in head and neck cancers.
The epicardial adipose tissue expresses the mRNA of osteopontin (show SPP1 Antibodies), osteoprotegerin (show TNFRSF11B Antibodies), and osteonectin genes that have been implicated in the calcification process; such expression is statistically associated with some components of HDL (show HSD11B1 Antibodies) subclasses in coronary artery disease patients.
detection of SPARC mRNA and protein expression levels may facilitate early diagnosis and prognosis assessment of esophageal squamous cell carcinoma.
SPARC rs17718347 and rs2347128 single nucleotide polymorphisms are associated with progression-free survival in locally advanced and metastatic pancreatic cancer patients.
results demonstrated that loss of miR (show MLXIP Antibodies)-211 expression and thus uncontrolled SPARC overexpression might drive progression of hepatocellular carcinoma (HCC (show FAM126A Antibodies)), which may provide a novel therapeutic strategy for the treatment of HCC (show FAM126A Antibodies).
Data suggest that plasma SPARC levels may be biomarker for vascular complications among Chinese type 2 diabetic patients; patients in lowest SPARC tertile have increased odds of aortic stiffness but reduced odds of peripheral arterial disease.
The profiled circulating tumour cells also expressed elevated levels of stem cell markers, and the extracellular matrix protein, SPARC. The expression of SPARC might correspond to an epithelial-mesenchymal transition in pancreatic circulating tumour cells
Data suggest that both osteonectin and FGF21 (show FGF21 Antibodies) levels in serum are associated with early nephropathy in type 2 diabetes, albeit with different patterns; persistent hyperglycemia may inhibit bone formation leading to osteoporosis. (FGF21 (show FGF21 Antibodies) = fibroblast growth factor 21 (show FGF21 Antibodies))
These results suggest that increased SPARC expression may be an indicator of greater aggressiveness, and may serve as a prognostic factor for triple-negative breast cancer.
High expression of SPARC is related to worse prognosis in rectal cancer patients.
Sparc levels in tendons are critical for proper collagen fibril maturation.
miR (show MLXIP Antibodies)-29 directly targeted SPARC, resulting in degradation of SPARC-encoding mRNA and reduction in the SPARC protein level.
SPARC plays a crucial role in the proliferation and differentiation of C2C12 and may be involved in the link between the ECM (show MMRN1 Antibodies) remodeling and mitochondrial func
SPARC is regulating the interplay between myeloid-derived suppressor cells and the extracellular matrix to drive the induction of epithelial-to-mesenchymal transition in tumor cells.
The results demonstrate for the first time a functional role of the N-propeptide in regulating collagen fiber assembly and cell behavior and suggest that SPARC and the N-propeptide of collagen I have distinct activities in regulating collagen fiber assembly and fibroblast function.
SPARC plays a key role in influencing the spatial organization of the anterior segment, potentially via modulation of collagen properties, while Hevin is not likely to be involved.
An ADAMTS1 (show ADAMTS1 Antibodies) blocking antibody suppressed the SPARC-induced collagen I secretion, indicating that SPARC promoted collagen production directly through ADAMTS1 (show ADAMTS1 Antibodies) interaction. In conclusion, ADAMTS1 (show ADAMTS1 Antibodies) is an important mediator of SPARC-regulated cardiac aging.
SPARC appears to be an important modulator of the actin cytoskeleton, implicating maintenance of muscular function
resistivity measurements were taken on 22 mice, 11 wild-type and 11 sparc-/- (knock out for the protein SPARC: secreted protein acidic and rich in cysteine), bearing mammary carcinomas.
SPARC isoforms, acting on Adipose stromal cells through distinct mechanisms, have an additive effect in inducing ASC (show STS Antibodies) migration.
findings indicate that secreted protein acidic cysteine-rich (SPARC) is intricately regulated by pro-angiogenic and other growth factors together with components of the extracellular matrix during the follicle-luteal transition
This study reports the temporal changes in vascular endothelial growth factor A (VEGFA (show VEGFA Antibodies)), fibroblast growth factor 2 (FGF2 (show FGF2 Antibodies)) and osteonectin during the follicular-luteal transition and corpus luteum development in the cow.
these data identify a contributory role for DNA methylation (show HELLS Antibodies) in regulating sparc expression in zebrafish embryogenesis.
Results establish a role for an ECM (show MMRN1 Antibodies) protein (Sparc) as an important regulator of embryonic haematopoiesis during early development in zebrafish.
Data show that Sparc (Osteonectin) functions in morphogenesis of the pharyngeal skeleton and inner ear in zebrafish.
Sparc is directly required for normal otolith growth
data suggest that SPARC might modulate angiogenesis during wound healing in the horse, which could protect against the disproportionate fibroplasia commonly afflicting limb wounds and leading to the development of exuberant granulation tissue
Data suggest a critical requirement for SPARC during post-gastrula development in Xenopus embryos and that SPARC, directly or indirectly, promotes cell-cell adhesion in vivo.
This gene encodes a cysteine-rich acidic matrix-associated protein. The encoded protein is required for the collagen in bone to become calcified but is also involved in extracellular matrix synthesis and promotion of changes to cell shape. The gene product has been associated with tumor suppression but has also been correlated with metastasis based on changes to cell shape which can promote tumor cell invasion.
, basement-membrane protein 40
, cysteine-rich protein
, secreted protein acidic and rich in cysteine
, Secreted acidic cystein-rich glycoprotein (osteonectin)
, secreted acidic cysteine rich glycoprotein
, secreted protein, acidic, cysteine-rich (osteonectin) S homeolog
, secreted protein, acidic, cysteine-rich (osteonectin)