Bruker Daltonics introduced its flexImaging 2.0 software for the acquisition and evaluation of MALDI-TOF and TOF/TOF imaging data, late last week. The software allows for color-coded visualization of the distribution of biomarkers or absorbed drugs and their major metabolites with MALDI imaging of tissue samples, Bruker said in a statement.
AnaSpec last week released 12 catalog peptides. CFTR (108-117), Pseudomonas aeruginosa inhibitor, representing amino acids 108-117 of the first CFTR extracellular domain can be purchased here.
Histone H3 (116–136), C116–136, which spans the C-terminius of histone H3, amino acids 116 to 136, can be purchased here.
Histone H3 (1-21), biotinylated, corresponding to the first 21 amino acids of the NH2 terminal of histone H3f followed by a GG linker and biotinylated lysine, can be purchased here.
RS domain derived peptide, a substrate of Clk/Sty, phosphorylated by Clk/Sty protein kinase is available for purchase here.
BTK derived peptide, a substrate for Btk involved in precursor B cell receptor signal, can be purchased here.
Histone H3 (116–136), N15–39, a peptide based on amino acids 15 to 39 of histone H3, is available for purchase here.
Forkhead derived peptide, FAM-labeled, or woodtide, used as a substrate for the DYRK family of kinases in in vitro analysis, can be purchased here.
Forkhead derived peptide, or woodtide, corresponding to residues 324 to 334 of transcription factor FKHR with two lysine residues added at the N-terminus to facilitate binding to phosphocellulose paper, is available for purchase here.
LMP2 (340–350), SSC, an Epstein-Barr virus-encoded oncogene latent membrane protein 2, can be purchased here.
LMP2 (419-427), TYG,an HLA A 2402-restricted Epstein-Bar virus-encoded oncogen latent membrane protein 2, can be purchased here.
HIV QK10, an HLA A3 restricted HIV Nef epitope, can be purchased here.
L1ARSLCD, which has a single amino acid substitution at a critical tyrosine residue compared to L1CD (1173-1185), can be purchased here.
The University of Michigan this week launched its Michigan Molecular Interactions database of protein interactions. The database contains information from well-known protein interaction repositories and merges the data using “novel computational technology. Using MiMI, scientists can efficiently access information about protein processes and rapidly dig down to primary source data,” the university said in a statement.