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ProteomicsHuman cancer cell MCF-7 IP-PTEN MS
The MCF-7 cells were lysed using RIPA lysis buffer with a high salinity content to break out non-covalent binding of proteins. Then IP under partially denaturing conditions was performed and demonstrated that anti-PTEN precipitates were detected as smear bands, then mass spectrometry analysis of the...
ORGANISM(S): Homo sapiens (Human) 
2022-04-04 | PXD021544 | Pride
Human Breast cancer Pten Ms 
ProteomicsMCF-7 PTEN-Nedd8 IP-MS
We intended to elucidate the underlying mechanism of PTEN-Nedd8 in tumorigenesis. So, we firstly employed affinity purification and mass spectrometry to interrogate PTEN-Nedd8 interactome in nucleus.
ORGANISM(S): Homo sapiens (Human) 
2022-05-20 | PXD011395 | Pride
Human Breast cancer cell Nedd8 Pten Ip-ms 
ProteomicsMCF-7 Flag-need8 IP-MS
To allow the proteomic identification of proteins modified with Nedd8, we firstly employed affinity purification and mass spectrometry to interrogate Nedd8 interactome.
ORGANISM(S): Homo sapiens (Human) 
2022-04-01 | PXD011368 | Pride
Human Breast cancer cell Ip-ms Mcf-7 
ProteomicsLncRNA MAGI2-AS3-encoded polypeptide restrains the proliferation and migration of breast cancer cells
This study was conducted by using Flag tag to IP proteins expressed with fusion small peptides encoding LncRNA MAGI2-AS3 and identified by high resolution mass spectrometry.
ORGANISM(S): Homo Sapiens 
2023-03-06 | PXD040607 |
ProteomicsComparative proteomic Analysis of wheat roots
Root is of vital important in acquiring nutrients and water from soils. Uncovering the regulatory mechanism of wheat root growth is of great help for genetic improvement of roots traits. A comparative proteomic analysis was performed. Expressed proteins were identified under CK and LN conditions. Pr...
ORGANISM(S): Triticum Aestivum 
2018-03-19 | PXD008793 |
ProteomicsCaspase-2 is a condensate-mediated deubiquitinase in protein quality control
When cells encounter proteome stresses, caspase-2 accumulates in a ubiquitin-rich condensate, which functions as a deubiquitinase to cleave the overloaded ubiquitinated proteins.
ORGANISM(S): Homo Sapiens 
2023-09-06 | PXD041964 |
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