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anti-Human SIVA1 Anticorps:
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Human Polyclonal SIVA1 Primary Antibody pour ELISA - ABIN564613
Diegmann, Junker, Loncarevic, Michel, Schimmel, von Eggeling: Immune escape for renal cell carcinoma: CD70 mediates apoptosis in lymphocytes. dans Neoplasia (New York, N.Y.) 2006
Show all 3 Pubmed References
Loss of SIVA1 expression is associated with nasopharyngeal carcinoma.
These findings collectively reveal a novel role for the p53 target gene SIVA both in regulating metabolism and in enabling tumorigenesis, independently of p53.
Functional test demonstrated that Siva1 significantly inhibited the invasion and migration of HCT116 cells.
electrical stimulation -inducible SIVA1 modulates p53 activities in proliferating keratinocytes, and exogenous electrical stimulation affects p53/HDM2/SIVA1 axis leading to increased proliferation during re-epithelialization
SIVA1 interacts with RAD18 and serves as a molecular bridge between RAD18 and PCNA, thus targeting the E3 ligase activity of RAD18 onto PCNA.
Siva1 promotes the ubiquitination and degradation of ARF, which in turn affects the stability of p53.
Upon stimulation of thromboxane A2, degradation of Siva1 is impeded, resulting in an accumulation of the protein, which translocates from the nucleus to the cytosol.
negative regulator of IL-2 gene expression in Treg cells
Data show that low levels of Siva1 and Ser16-phosphorylated stathmin correlate with high metastatic states of breast cancer cells.
These findings suggest that the caspase-dependent pathway for induction of apoptosis is involved in Siva-1-mediated influenza A virus replication.
These results suggest that Siva-mediated unprovoked apoptosis is not likely to be involved in the pathogenesis of Familial Mediterranean fever.
Siva-1 forms a functional complex with Tyk2 and participates in the transduction of signals that inhibit B lymphocyte growth.
Siva-1 putative amphipathic helical region (SAH) binds BCL-XL and sensitizes cells to UV radiation induced apoptosis
Overexpression of Siva-1 in T lymphocytes triggers the activation of a caspase-dependent death pathway including a pivotal mitochondrial step. Both N- and C-terminal domains of Siva proteins display the ability to induce a cell death process in T cells.
Siva-1 has a role, through its inhibitory effect on NF-kappaB activity, in TCR-mediated AICD with implications in peripheral tolerance, T-cell homeostasis and cancer
determined the N-terminal part of Siva as the binding region for CD27; the peroxisomal membrane protein PMP22 is a new interaction partner of Siva and may be involved in the host response against CVB3.
Confirming the anti-apoptotic role of HPV-16 E7 in the HaCaT cellular model, evaluated by nuclear morphology, it was also found that Siva-1 expression produced a significant increase of the apoptotic rate in UV radiation-exposed HaCaT cells.
Results suggest that Siva-1 might participate in the CD4-initiated signaling apoptotic pathway induced by the HIV-1 envelope in T-lymphoid cells.
lysophosphatidic acid 2 receptor mediates down-regulation of Siva-1 to promote cell survival
Data show that Siva and pyrin are co-expressed, and that pyrin modulates the apoptotic response to oxidative stress mediated by Siva.
This gene encodes a protein with an important role in the apoptotic (programmed cell death) pathway induced by the CD27 antigen, a member of the tumor necrosis factor receptor (TFNR) superfamily. The CD27 antigen cytoplasmic tail binds to the N-terminus of this protein. Two alternatively spliced transcript variants encoding distinct proteins have been described.
CD27-binding (Siva) protein
, apoptosis regulatory protein Siva
, CD27-binding protein
, Cd27 binding protein