DNA ligase

Expression system: E. coli
Length: 330-689, Partial
Activity: Not Tested

Expression system: E. coli
Length: 340-679, Partial
Activity: Not Tested

Expression system: P. pastoris (Yeast)
Length: 1-408, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-485, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1-469, Full Length
Activity: Not Tested

Expression system: E. coli
Length: 1881-1992, Partial
Activity: Not Tested

Small Ubiquitin-Related Modifier 2 (SUMO2) is an Ubiquitin-like protein that belongs to the ubiquitin family with SUMO subfamily. It is a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed sumoylation. SUMO2 can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptidebond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins.

p53, also known as Tp53, is a DNA-binding protein which belongs to the p53 family. It contains transcription activation, DNA-binding, and oligomerization domains. p53 protein is expressed at low level in normal cells and at a high level in a variety of transformed cell lines, where it's believed to contribute to transformation and malignancy. p53 (TP53) is a transcription factor whose protein levels and post-translational modification state alter in response to cellular stress (such as DNA damage, hypoxia, spindle damage). Activation of p53 begins through a number of mechanisms including phosphorylation by ATM, ATR, Chk1 and MAPKs. MDM2 is a ubiquitin ligase that binds p53 and targets p53 for proteasomal degradation. Phosphorylation, p14ARF and USP7 prevent MDM2-p53 interactions, leading to an increase in stable p53 tetramers in the cytoplasm. Further modifications such as methylation and acetylation lead to an increase in Tp53 binding to gene specific response elements. Tp53 regulates a large number of genes (>100 genes) that control a number of key tumor suppressing functions such as cell cycle arrest, DNA repair, senescence and apoptosis. Whilst the activation of p53 often leads to apoptosis, p53 inactivation facilitates tumor progression. It is postulated to bind to a p53-binding site and activate expression of downstream genes that inhibit growth and or invasion, and thus function as a tumor suppressor. Mutants of p53 that frequently occur in a number of different human cancers fail to bind the consensus DNA binding site, and hence cause the loss of tumor suppressor activity. Defects in TP53 are a cause of esophageal cancer, Li-Fraumeni syndrome, lung cancer and adrenocortical carcinoma.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy

Expression system: E. coli
Length: 1-130, Full Length
Activity: Not Tested