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Human CACYBP Protein expressed in Escherichia coli (E. coli) - ABIN667003
Filipek, Jastrzebska, Nowotny, Kwiatkowska, Hetman, Surmacz, Wyroba, Kuznicki: Ca2+-dependent translocation of the calcyclin-binding protein in neurons and neuroblastoma NB-2a cells. in The Journal of biological chemistry 2002
Show all 2 references for ABIN667003
The biological characteristics a (show SIAH1 Proteins)nd target proteins of CacyBP/SIP and its exact role in various cancers are discussed. Re (show S100A6 Proteins)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 Proteins).
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 Proteins)) metastasis and also sheds light on the underlying molecular mechanism by which CacyBP promotes CRC (show CALR Proteins) metastasis.
CacyBP enhances multidrug resistance of pancreatic cancer cells by regulation of P-gp (show ABCB4 Proteins) and Bcl-2 (show BCL2 Proteins).
These findings reveal a novel function for SNRK (show SNRK Proteins) in the regulation of colon cancer cell proliferation and beta-catenin (show CTNNB1 Proteins) signaling.
different activity of CacyBP/SIP in neuroblastoma (show ARHGEF16 Proteins) NB2a and colon cancer HCT116 cells might affect the ERK1/2 pathway in the differentiation or proliferation processes
Calcyclin-binding protein/Siah-1 (show SIAH1 Proteins)-interacting protein (CacyBP/SIP) was initially described as a binding partner of S100A6 (show S100A6 Proteins) in the Ehrlich ascites tumor cells and later as a Siah-1 (show SIAH1 Proteins)-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.
new insight into the interaction between S100 proteins and CacyBP/SIP
SIP (-/-) embryonic fibroblasts have increased levels of cytosolic p27 (show CDKN1B Proteins) 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 Proteins) mutant does not.
Cacybp is associated with acute lung injury
Data indicated that CacyBP/SIP could simultaneously interact with tubulin (show TUBB Proteins) and actin, suggesting that CacyBP/SIP might link actin and tubulin (show TUBB Proteins) cytoskeletons.
binds EF-hand proteins of the S100 family [CacyBP/SIP]
Structural details of multiple sites of protein-protein interactions on SIP provide insight into the mechanism that drives the formation of the Siah-1 E3 ubiquitin ligase complex [SIP]
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