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anti-Mouse (Murine) SH3GLB1 Anticorps:
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Human Monoclonal SH3GLB1 Primary Antibody pour ICC, IF - ABIN4308128
Karbowski, Jeong, Youle: Endophilin B1 is required for the maintenance of mitochondrial morphology. dans The Journal of cell biology 2004
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Human Polyclonal SH3GLB1 Primary Antibody pour IF, WB - ABIN541271
Oltvai, Milliman, Korsmeyer: Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programmed cell death. dans Cell 1993
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Human Polyclonal SH3GLB1 Primary Antibody pour ELISA, WB - ABIN257365
Takahashi, Karbowski, Yamaguchi, Kazi, Wu, Sebti, Youle, Wang: Loss of Bif-1 suppresses Bax/Bak conformational change and mitochondrial apoptosis. dans Molecular and cellular biology 2005
Human Polyclonal SH3GLB1 Primary Antibody pour ICC, ELISA - ABIN1001869
Lockshin, Osborne, Zakeri: Cell death in the third millennium. dans Cell death and differentiation 2000
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Human Monoclonal SH3GLB1 Primary Antibody pour ICC, IF - ABIN4269695
Cho, Xiao, Wang, Gao, Rafikov, Black, Huang, Ding, Yoon, Kirken, Yin, Wang, Dong: Bif-1 Interacts with Prohibitin-2 to Regulate Mitochondrial Inner Membrane during Cell Stress and Apoptosis. dans Journal of the American Society of Nephrology : JASN 2019
Human Polyclonal SH3GLB1 Primary Antibody pour ICC, IF - ABIN441165
Mir, George, Zahoor, Harms, Guinn, Sarvetnick: Inhibition of Autophagic Turnover in ?-Cells by Fatty Acids and Glucose Leads to Apoptotic Cell Death. dans The Journal of biological chemistry 2015
SH3GLB1 controls nicotinic acetylcholine receptors endocytic trafficking in a phosphorylation- and RAB5-dependent manner at steps upstream of autophagosome formation.
These findings thus identify Bif-1 as a novel regulator of lipid homeostasis to prevent the pathogenesis of obesity and its associated metabolic complications.
these data reveal an Irgm1-dependent mechanism that promotes the tumorigenesis of melanoma via dual regulation of apoptosis and Bif-1-dependent autophagy
Our findings suggest that endophilin-B1 is a key mediator of a feed-forward mechanism of Alzheimer's disease pathogenesis
selective autophagy regulates the basal and atrophy-induced turnover of the pentameric transmembrane protein, CHRN, and that TRIM63, together with SH3GLB1 and SQSTM1 regulate this process.
these data suggest that Bif-1 is essential for the maintenance of mitochondrial morphology and function in neurons
Bif-1 haploinsufficiency attenuates mitophagy and results in the promotion of chromosomal instability, which enables tumor cells to efficiently bypass the oncogenic/metabolic pressures for apoptosis.
findings not only establish Cdk5 as a critical regulator of autophagy induction, but also reveal a role for Cdk5 and EndoB1 in the pathophysiology of Parkinson's disease through modulating autophagy
These findings suggest that Bif-1 acts as a critical regulator of Atg9 puncta formation presumably by mediating Golgi fission for autophagosome biogenesis during starvation.
characterization of and function at intracellular membranes [endophilin B1b]
Bif-1 is an important component of the mitochondrial pathway for apoptosis as a novel Bax/Bak activator, and loss of this proapoptotic molecule may contribute to tumorigenesis.
A potential role for endophilin B1t in mammalian spermatogenesis is discussed within the context of the PP1c gamma knockout testis phenotype.
Bif-1 interacts with Beclin 1 through ultraviolet irradiation resistance-associated gene (UVRAG) and functions as a positive mediator of the class III PI(3) kinase (PI(3)KC3).
Src phosphorylation of Bif-1 suppresses the interaction between Bif-1 and Bax, resulting in the inhibition of Bax activation during anoikis.
Here the authors report that Endophilin B2, similarly to Endophilin B1, plays an indispensable role in mitochondria sequestration and inner mitochondrial membrane (IMM) protein degradation during mitophagy.
endophilin B1 participates in dynamin 2-dependent formation of a population of transport vesicles distinct from those generated by A-type endophilins
Bif-1 is involved in prostate cancer tumorigenesis and acts as a suppressor in prostate cancer progression.
endophilin B1 mediated the biological function of EGFR in cancer cell proliferation through regulating the EGFR endocytic trafficking and downstream signaling.
Data suggest that activated autophagy is associated with the progression of pancreatic ductal adenocarcinoma and that the overexpression of autophagy-related proteins Atg5, Ambra1, beclin-1, LC3B and Bif-1 is significantly correlated with poor outcome.
these data suggest a novel function for Bif-1 as a suppressor of breast cancer cell migration by promoting EGFR degradation through the regulation of endosome maturation
The expression of Bif-1 is downregulated in a subset of pancreatic ductal adenocarcinoma. This novel finding is in agreement with the tumor suppressor function of Bif-1.
GSK-3beta promotes cell survival by modulating Bif-1-dependent autophagic response and cell death.
Double knockdown of endophilin B1 and Drp1 leads to a mitochondrial phenotype identical to that of the Drp1 single knockdown, a result consistent with Drp1 acting upstream of endophilin B1 in the maintenance of morphological dynamics of mitochondria.
BAR domain of endophilin-A1 drives membrane curvature by coordinate action of the crescent's scaffold mechanism and the ridge's membrane insertion in addition to membrane binding via amino-terminal amphipathic helix.
The decreased expression of Bif-1 in malignant gastric epithelial cells compared with the normal mucosal cells suggests that loss of Bif-1 expression may play a role in gastric tumorigenesis, possibly by inhibiting the apoptosis mediated by Bif-1.
Bif-1 expression might play a role in tumorigenesis in both urinary bladder (UB) and gallbladder (GB) cancer
The loss of Bif-1 expression in a subset of prostate cancer samples is in agreement with the proapoptotic function of Bif-1.
down-regulation of Bif-1 during the transition from normal colorectal mucosa to colorectal adenocarcinoma
DLP1 also caused global morphological changes in mitochondrial outer membrane-like liposomes, but DLP1 did not stimulate BAX-permeabilizing function in the absence or presence of Bif-1.
This gene encodes a SRC homology 3 domain-containing protein. The encoded protein interacts with the proapoptotic member of the Bcl-2 family, Bcl-2-associated X protein (Bax) and may be involved in regulating apoptotic signaling pathways. This protein may also be involved in maintaining mitochondrial morphology. Alternate splicing results in multiple transcript variants.
SH3-domain GRB2-like endophilin B1
, SH3 domain-containing GRB2-like protein B1
, Bax-interacting factor 1
, SH3-containing protein SH3GLB1
, protein phosphatase 1, regulatory subunit 70
, SH3-domain GRB2-like B1 (endophilin)
, SH3 domain GRB2-like protein B1