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The oncogene BCL2 is a membrane protein that blocks a step in a pathway leading to apoptosis or programmed cell death.
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The BAG-1 stabilizes F508del-CFTR by direct binding, probably competing out ubiquitin to partially avoid its proteasomal degradation.
The membrane form of heparin binding EGF-like growth factor (show HBEGF Proteins) (ProHB-EGF (show EGF Proteins)) is most likely able to trigger the nuclear translocation of BAG-1 in keeping its level high.
Hemoxygenase (show HMOX1 Proteins) 1 deficiency provoked diminished Bag-1 level upon LPS (show TLR4 Proteins) treatment
this study first reported the solution structure of mBAG-1 (show LRRC4 Proteins)-UBH and the growth factor precursor-interacting motif on the protein.
Bag-1 proteins function as regulators of the action of selective transcription factors.
during development of mouse autopods, BAG-1 expression is downregulated upon the initiation of interdigital apoptosis (BAG-1)
Bag1 is a regulator and marker of neuronal differentiation
BAG1 displays potent neuroprotective activity in vivo against stroke.
Since, BAG-1 is essential for cell survival, its association with tNhtt aggregates might disrupt its normal function and thereby promote polyglutamine-expanded tNhtt-induced cell death.
Bag1 is essential for differentiation and survival of hematopoietic and neuronal cells.
Taken together, these data indicate that Bag-1 up-regulation is required to maintain apoptosis resistance in human cytomegalovirus-infected cells.
the combined effects of BAG-1 and XPD (show ERCC2 Proteins) polymorphisms on chemotherapy sensitivity and survival in patients with advanced non-small-cell lung cancer, which might be the important predictive markers for platinum-based chemotherapy efficacy.
Bag-1 indirectly affects cell survival through c-Myc (show MYC Proteins) activated signalling that causes elevation of ornithine decarboxylase (show ODC1 Proteins) levels, leading to an increase of the polyamine content.
Overexpression of miR (show MLXIP Proteins)-138 inhibited cell proliferation by directly suppressing the expression of Bag-1.
The expression of BAG-1 was upregulated in chronic non-eosinophilic rhinosinusitis.
BAG-1 expression was high in esophageal carcinoma tissues compared to normal esophagus. After Eca109 cells were transfected with BAG-1-siRNA, the proliferation and invasive capabilities of the cells were decreased while the apoptosis rate was enhanced.
BAG-1M mediates Hsp70 (show HSP70 Proteins) inhibition downstream of NF-kappaB (show NFKB1 Proteins).
distinct isoforms of BAG-1 had different anti-apoptotic ability in breast cancer cells treated with the 4-OH TAM (show CCNA1 Proteins).
BAG-1M and HspBP1 (show HSPBP1 Proteins) had differential impacts on the dynamic composition of steroid receptor (show ESR2 Proteins) folding complexes
The results present that the constructed shRNA plasmids significantly inhibited the expression of mRNA and protein of Lo Vo cell BAG-1, and can maintain the effect for a long term
The oncogene BCL2 is a membrane protein that blocks a step in a pathway leading to apoptosis or programmed cell death. The protein encoded by this gene binds to BCL2 and is referred to as BCL2-associated athanogene. It enhances the anti-apoptotic effects of BCL2 and represents a link between growth factor receptors and anti-apoptotic mechanisms. Multiple protein isoforms are encoded by this mRNA through the use of a non-AUG (CUG) initiation codon, and three alternative downstream AUG initiation codons. A related pseudogene has been defined on chromosome X.
BAG family molecular chaperone regulator 1
, Bcl-2-binding protein
, bcl-2-associated athanogene 1
, Bcl-2 associating athanogene-1 protein
, glucocortoid receptor-associated protein RAP46
, receptor-associated protein, 46-KD