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CacyBP/SIP nuclear localization, dependent on S100 protein, suppresses gastric cancer tumorigenesis through beta-catenin (show CTNNB1 Antibodies) degradation and the dephosphorylation of ERK1/2 during the G2 phase.
Our data have shown for the first time the regulation of CacyBP/SIP gene expression by NFAT1 (show NFAT1 Antibodies). Since NFAT (show NFATC1 Antibodies) transcription factors are involved in processes related to immune response, these results indicate potential involvement of CacyBP/SIP in the immune system.
These results suggest that CacyBP/SIP may be promoting growth of colon cancer cells by enhancing ubiquitin-mediated degradation of p27kip1 (show CDKN1B Antibodies).
The biological characteristics a (show SIAH1 Antibodies)nd target proteins of CacyBP/SIP and its exact role in various cancers are discussed. Re (show S100A6 Antibodies)view.
CacyBP/SIP nuclear translocation contributes to the proliferation of gastric cancer cells, and CacyBP/SIP exerts this effect, at least in part, by stimulating ubiquitin-mediated degradation of p27Kip1 (show CDKN1B Antibodies).
CacyBP/SIP plays an important role in inhibiting apoptosis of glioma cells which might be mediated by ERK1/2 signaling pathway.
CacyBP/SIP is a useful indicator of dis processes in Chronic Lymphocytic Leukemia (CLL) and plays an important role in sustaining the balance of cell proliferation and apoptosis.
CacyBP/SIP nuclear translocation promotes the proliferation and cell cycle progression of gastric cancer cells.
Overexpression of CacyBP is associated with glioma.
This study presents CacyBP as a promising candidate biomarker for colorectal cancer (CRC (show CALR Antibodies)) metastasis and also sheds light on the underlying molecular mechanism by which CacyBP promotes CRC (show CALR Antibodies) metastasis.
involvement of CacyBP/SIP in the regulation of p38 (show CRK Antibodies) kinase activity, in addition to that of ERK1/2, might point to the function of CacyBP/SIP in pro-survival and pro-apoptotic pathways.
In undifferentiated and differentiated tumor cells, CacyBP level has an effect on the ERK1/2-CREB (show CREB1 Antibodies)-BDNF (show BDNF Antibodies) pathway.
Calcyclin-binding protein/Siah-1 (show SIAH1 Antibodies)-interacting protein (CacyBP/SIP) was initially described as a binding partner of S100A6 (show S100A6 Antibodies) in the Ehrlich ascites tumor cells and later as a Siah-1 (show SIAH1 Antibodies)-interacting protein. Its role has been studied in various mouse tumors and cell lines. Review.
sumoylated CacyBP/SIP is present in the cytoplasmic and not in the nuclear fraction. We have also established that lysine 16 is the residue which undergoes sumoylation in the CacyBP/SIP protein.
different activity of CacyBP/SIP in neuroblastoma (show ARHGEF16 Antibodies) NB2a and colon cancer HCT116 cells might affect the ERK1/2 pathway in the differentiation or proliferation processes
new insight into the interaction between S100 proteins and CacyBP/SIP
SIP (-/-) embryonic fibroblasts have increased levels of cytosolic p27 (show CDKN1B Antibodies) and exhibit increased cell motility compared to wild-type cells.
CacyBP/SIP exhibits a phosphatase activity toward ERK1/2 kinases while its E217K (show Ube2g1 Antibodies) mutant does not.
Cacybp is associated with acute lung injury
Data indicated that CacyBP/SIP could simultaneously interact with tubulin (show TUBB Antibodies) and actin, suggesting that CacyBP/SIP might link actin and tubulin (show TUBB Antibodies) cytoskeletons.
The protein encoded by this gene is a calcyclin binding protein. It may be involved in calcium-dependent ubiquitination and subsequent proteosomal degradation of target proteins. It probably serves as a molecular bridge in ubiquitin E3 complexes and participates in the ubiquitin-mediated degradation of beta-catenin. Two alternatively spliced transcript variants encoding different isoforms have been found for this gene.
, calcyclin binding protein
, Calcyclin binding protein
, S100A6-binding protein
, Siah-interacting protein (SIP)
, growth-inhibiting gene 5 protein
, siah-interacting protein