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The domains of SETD2, a known histone methyltransferase were investigated for specific interaction partners and function using a number of biochemical assays and affinity purification mass spectrometry. The C-terminal domain, named SETD2C, was identified to interact with hnRNP-L through a previousl...
ORGANISM(S): Homo sapiens (Human) 
2021-02-01 | PXD019538 | Pride
The domains of SETD2, a known histone methyltransferase were investigated for specific interaction partners and function using a number of biochemical assays and affinity purification mass spectrometry. The C-terminal domain, named SETD2C, was identified to interact with hnRNP-L through a previousl...
ORGANISM(S): Homo sapiens (Human) 
2021-02-01 | PXD022946 | Pride
The domains of SETD2, a known histone methyltransferase were investigated for specific interaction partners and function using a number of biochemical assays and affinity purification mass spectrometry. The C-terminal domain, named SETD2C, was identified to interact with hnRNP-L through a previousl...
ORGANISM(S): Homo sapiens (Human) 
2021-02-01 | PXD019376 | Pride
we determined the sensitivity of the Lumos mass spectrometer using the NIST monoclonal antibody reference material at various concentrations to detect its peptides in a background of S. cerevisiae whole cell lysate, which was kept at a constant concentration.
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2018-09-12 | PXD009441 | Pride
To identify proteins interacting with Pof8, cell-free extracts of strains FP1547 harboring 3xFLAG epitope-tagged Pof8 and untagged control (FP1546) were diluted to 5 mg/ml in 8 ml of lysis buffer (50 mM Tris-HCl pH 7.5, 150 mM sodium chloride, 0.1% (v/v) NP40 and 10% (v/v) glycerol) plus complete ED...
ORGANISM(S): Schizosaccharomyces Pombe (ncbitaxon:4896) 
2021-05-24 | MSV000087493 | MassIVE
PROJECT DESCRIPTION The Orbitrap Fusion Lumos mass spectrometer has recently been shown to have better fragmentation and detection than its predecessors. Previous studies using a HeLa digest analyzed on the Lumos mass spectrometer have reported the number of peptides and proteins identified by rever...
ORGANISM(S): Saccharomyces Cerevisiae (ncbitaxon:4932) 
2018-04-19 | MSV000082296 | MassIVE
Thermococcus kodakarensis is a thermophilic archaea used in this study to determine how changes in growth temperature affect protein expression. This organism was chosen, in part, due to the simplified proteome and potential protein stability gained when analyzing proteins at room temperature. Two t...
ORGANISM(S): Thermococcus kodakarensis KOD1 
2020-02-17 | PXD014814 | Pride
N-terminally Halo-tagged deletions of human SETD2 were constructed such as SETD2 ABCN1, A, B, C, CN, and CC consisted of amino acids 1-1692, 1-503, 504-1403, 1404-2564, 1404-1963, and 1964-2564, respectively. Deletion mutants were expressed in HEK293T cells and affinity purified, each in biological ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-06-08 | MSV000087587 | MassIVE
We used a reverse chromatin immunoprecipitation (ChIP) method that takes advantage of the RNA-mediated DNA-targeting capability of Cas9 to efficiently and adaptably isolate specific genomic regions and their associated protein factors. By using purified recombinant catalytically-dead Cas9 (dCas9) co...
ORGANISM(S): Drosophila Melanogaster (ncbitaxon:7227) 
2017-10-25 | MSV000081643 | MassIVE
We used a reverse chromatin immunoprecipitation (ChIP) method that takes advantage of the RNA-mediated DNA-targeting capability of Cas9 to efficiently and adaptably isolate specific genomic regions and their associated protein factors. By using purified recombinant catalytically-dead Cas9 (dCas9) co...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-10-25 | MSV000081645 | MassIVE
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