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anti-Human HBXIP Antibodies:
anti-Mouse (Murine) HBXIP Antibodies:
anti-Rat (Rattus) HBXIP Antibodies:
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Overall, the available data depict a self-inhibitory feedback loop in which HBV, through HBx, increases the expression of miR (show MYLIP Antibodies)-125a, that in turn interferes with expression of HBV surface antigen, thus repressing viral replication.
HBXIP can modulate the etoposide sensitivity of MCF-7 cell lines.
deacetylation of MST1 mediated by HBXIP-enhanced HDAC6 results in MST1 degradation in a CMA manner in promotion of breast cancer growth.
HBXIP up-regulates YAP (show YAP1 Antibodies) expression via activating transcription factor c-Myb (show MYB Antibodies) to facilitate the growth of hepatoma cells.
high level of expression of HBXIP is associated with the progression of non-small-cell lung cancer and may be a useful biomarker for poor prognostic evaluation and a potential molecular therapy target for patients with non-small-cell lung cancer
HBXIP is able to depress the gluconeogenesis in hepatoma cells by suppressing PCK1 (show PCK1 Antibodies) to promote hepatocarcinogenesis, involving miR (show MLXIP Antibodies)-135a/FOXO1 (show FOXO1 Antibodies) axis and PI3K (show PIK3CA Antibodies)/Akt (show AKT1 Antibodies)/p-FOXO1 (show FOXO1 Antibodies) pathway.
we conclude that the oncoprotein HBXIP contributes to the abnormal lipid metabolism in breast cancer
HBXIP can function as a mediator protein for DNA damage response signals to activate the G2/M checkpoint to maintain genome integrity and prevent cell death.
promotes cisplatin resistance and regulates CD147 via Sp1 (show PSG1 Antibodies) in ovarian cancer
The mRNA levels of ACSL1 (show Acsl1 Antibodies) were positively associated with those of HBXIP in clinical breast cancer tissues. Thus, we conclude that the oncoprotein HBXIP is able to up-regulate ACSL1 (show Acsl1 Antibodies) through activating the transcriptional factor Sp1 (show PSG1 Antibodies) in breast cancer.
Data indicate that hepatitis B virus X-interacting protein (HBXIP) over-expression appears to associate with cervical cancer progression, and may potentially be used as a cervical cancer biomarker for the early diagnosis, prognostic evaluation and therapeutic target for cervical cancer.
This gene encodes a protein that specifically complexes with the C-terminus of hepatitis B virus X protein (HBx). The function of this protein is to negatively regulate HBx activity and thus to alter the replication life cycle of the virus.
hepatitis B virus x interacting protein
, hepatitis B virus x-interacting protein
, Hepatitis B virus X-interacting protein
, HBV X-interacting protein homolog
, HBX-interacting protein homolog
, hepatitis B virus X-interacting protein homolog
, late endosomal/lysosomal adaptor and MAPK and MTOR activator 5
, ragulator complex protein LAMTOR5
, HBV X-interacting protein
, HBx-interacting protein
, hepatitis B virus x-interacting protein (9.6kD)
, Hepatitis B virus X-interacting protein homolog