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Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD. Additionally we are shipping Regulation of Nuclear Pre-MRNA Domain Containing 1B Proteins (7) and and many more products for this protein.
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Aberrant overexpression of CREPT contributes to tumorigenesis of colorectal cancer by promoting cell proliferation and accelerating the cell cycle, and confers sensitivity to 5-fluorouracil.
Ccisplatin-induced peripheral neuropathy(isIPN) is associated with age, modifiable risk factors, and genetically determined expression level of RPRD1B Further study of implicated genes could elucidate the pathophysiologic underpinnings of CisIPN.
CREPT is closely relevant to the proliferation of NSCLC cells.
Altogether, our results provided a novel insight into CREPT in regulating gastric cancer progression through apoptosis regulated by ROS/p53 pathways.
Mechanistically, CREPT regulated beta-catenin/TCF4/cyclin D1 pathway in BC. In conclusion, the data suggested that miR-138/CREPT involved BC progression, providing potential therapeutic targets for BC.
Consistently, samples from oral squamous cell carcinoma (OSCC) patients exhibited a noticeably stronger CREPT expression than noncancerous samples. In contrast, knocking down of CREPT in OSCC cell lines significantly reduced proliferation, colony formation and migration as well as the expression of cyclin D1 and c-Myc, but promoted apoptosis.
In addition, CREPT overexpression significantly promoted tumor growth in vivo. Mechanism study showed that CREPT may regulate cell proliferation and cell cycle through the regulation on cyclin D3, CDK4 and CDK6.
a detailed description of proteins associating with K-H/RPRD1B in higher-order protein complexes is required to further elucidate its role in various cellular processes
CREPT displays unique immunostaining for retroperitoneal leiomyosarcoma tissue and can be used to supplement other currently available markers.
study suggests that CREPT acts as an activator to promote transcriptional activity of the beta-catenin.TCF4 complex in response to Wnt signaling.
RPRD1A and RPRD1B associate directly with RPAP2 phosphatase and coordinate the dephosphorylation of RNAPII phospho-S5 by RPAP2.
RPRD1B overexpression promotes tumor growth and accelerates cell cycle progression.
This study reports that K-H functions in RNAPII regulation, and aids in stabilizing interactions between transcription termination factors, localizing Xrn2 to the 3'-end of genes and ultimately suppressing R-loop formation.
CREPT increases cyclin D1 transcription during tumorigenesis.
Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD. Transcriptional regulator which enhances expression of CCND1. Promotes binding of RNA polymerase II to the CCDN1 promoter and to the termination region before the poly-A site but decreases its binding after the poly-A site. Prevents RNA polymerase II from reading through the 3' end termination site and may allow it to be recruited back to the promoter through promotion of the formation of a chromatin loop. Also enhances the transcription of a number of other cell cycle-related genes including CDK2, CDK4, CDK6 and cyclin-E but not CDKN1A, CDKN1B or cyclin-A. Promotes cell proliferation (By similarity).
regulation of nuclear pre-mRNA domain-containing protein 1B
, unm hi3400
, un-named hi3400
, regulation of nuclear pre-mRNA domain containing 1B
, regulation of nuclear pre-mRNA domain containing 1B a
, Regulation of nuclear pre-mRNA domain containing 1B
, cell cycle-related and expression-elevated protein in tumor
, cell-cycle related and expression-elevated protein in tumor