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SPARC-associated signaling pathways are associated with lymphangiogenesis and lymph node metastases of hypopharyngeal cancer.
Stromal SPARC expression correlated with the prognosis of patients with resectable biliary carcinoma, and its significance was enhanced in patients treated with adjuvant gemcitabine-based chemotherapy.
Studies revealed that SPARC plays a critical role in regulating bone remodeling and maintaining bone mass and quality. The mechanisms by which SPARC influences bone formation, maintenance, and repair might occur through multiple pathways that include the regulation of procollagen processing and assembly in the bone matrix, crosslinking, mineralization, and/or osteoblast/osteoclast differentiation and activity. [review]
This study indicates that germline PTCH1 (show PTCH1 Proteins) heterozygous mutations play a major role in bone metabolism in patients with NBCCS (show PTCH1 Proteins), in particular in those with PTCH1 (show PTCH1 Proteins) protein truncation mutations. SPARC may represent an important downstream modulator of PTCH1 (show PTCH1 Proteins) mediation of bone metabolism.
The SPARC drives pathological responses in non-small cell lung cancer and idiopathic pulmonary fibrosis by promoting microvascular remodelling and excessive deposition of ECM (show MMRN1 Proteins) proteins.
proCOL11A1, fibroblast-activated protein, secreted protein acidic and rich in cysteine, and periostin (show POSTN Proteins) expression was significantly increased in the intratumoral stroma of pancreatic ductal adenocarcinomas compared to paired non-neoplastic pancreata
The mRNA and protein levels of SPARC were 5.78-fold higher in cancer tissues compared with the case-matched normal epithelium. High expression levels of SPARC in esophageal squamous cell carcinoma parenchyma were related to lymph node metastasis and poor prognosis (p = 0.049 and p = 0.04).
SPARC can serve a dual function role as both predictor for prognosis and potentially biomarker for lymph node metastasis in resected pancreatic cancer patients.
SPARC appears to be an important modulator of the actin cytoskeleton, implicating maintenance of muscular function
that SPARC-mediated degradation of the extracellular matrix, and its possible association with MMPs, might contribute to progression of phyllodes tumors
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 Proteins) blocking antibody suppressed the SPARC-induced collagen I secretion, indicating that SPARC promoted collagen production directly through ADAMTS1 (show ADAMTS1 Proteins) interaction. In conclusion, ADAMTS1 (show ADAMTS1 Proteins) is an important mediator of SPARC-regulated cardiac aging.
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 Proteins) migration.
SPARC levels were not associated with efficacy in patients with MPC. This exploratory analysis does not support making treatment decisions regarding nab-paclitaxel plus gemcitabine or gemcitabine alone in MPC based on SPARC expression.
SPARC is proposed to act as a critical regulator of transglutaminase activity on collagen I with implications for mechanical strength of tissues.
Tumor-produced SPARC and VCAM1 (show VCAM1 Proteins) are regulators of cancer extravasation.
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 Proteins)), fibroblast growth factor 2 (FGF2 (show FGF2 Proteins)) 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 Proteins) in regulating sparc expression in zebrafish embryogenesis.
Results establish a role for an ECM (show MMRN1 Proteins) 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)