Recombinant production enables lot-to-lot consistency and is animal-cruelty-free
This product has been cited in peer reviewed publications, see list HERE
Western blot analysis of PCNA on different lysates. Proteins were transferred to a PVDF membrane and blocked with 5% BSA in PBS for 1 hour at room temperature. The primary antibody (ET1605-38, 1/500) was used in 5% BSA at room temperature for 2 hours. Goat Anti-Rabbit IgG - HRP Secondary Antibody (HA1001) at 1:5,000 dilution was used for 1 hour at room temperature.
Lane 1: Hela cell lysate
Lane 2: 293 cell lysate
Lane 3: A431 cell lysate
Predicted band size: 29 kDa
Observed band size: 35 kDa
Phosphorylated. Phosphorylation at Tyr-211 by EGFR stabilizes chromatin-associated PCNA.; Acetylated by CREBBP and p300/EP300; preferentially acetylated by CREBBP on Lys-80, Lys-13 and Lys-14 and on Lys-77 by p300/EP300 upon loading on chromatin in response to UV irradiation. Lysine acetylation disrupts association with chromatin, hence promoting PCNA ubiquitination and proteasomal degradation in response to UV damage in a CREBBP- and EP300-dependent manner. Acetylation disrupts interaction with NUDT15 and promotes degradation.; Ubiquitinated. Following DNA damage, can be either monoubiquitinated to stimulate direct bypass of DNA lesions by specialized DNA polymerases or polyubiquitinated to promote recombination-dependent DNA synthesis across DNA lesions by template switching mechanisms. Following induction of replication stress, monoubiquitinated by the UBE2B-RAD18 complex on Lys-164, leading to recruit translesion (TLS) polymerases, which are able to synthesize across DNA lesions in a potentially error-prone manner. An error-free pathway also exists and requires non-canonical polyubiquitination on Lys-164 through 'Lys-63' linkage of ubiquitin moieties by the E2 complex UBE2N-UBE2V2 and the E3 ligases, HLTF, RNF8 and SHPRH. This error-free pathway, also known as template switching, employs recombination mechanisms to synthesize across the lesion, using as a template the undamaged, newly synthesized strand of the sister chromatid. Monoubiquitination at Lys-164 also takes place in undamaged proliferating cells, and is mediated by the DCX(DTL) complex, leading to enhance PCNA-dependent translesion DNA synthesis. Sumoylated during S phase.; Methylated on glutamate residues by ARMT1/C6orf211.
The proliferating cell nuclear antigen (PCNA), a protein synthesized in early G1 and S phases of the cell cycle, functions in cell cycle progression, DNA replication and DNA repair. In early S phase, PCNA exhibits granular distribution and is absent from the nucleoli; however, in late S phase, it relocates to the nucleoli. PCNA exists in two basic forms: one involved in ongoing DNA replication, which localizes specifically to the nucleus, and a second, soluble form, not implicated in constant synthesis. Interestingly, the latter form degrades in the presence of organic solvents, rendering it undetectable by histological methods in tissues using organic fixatives, and thus also providing a method of visualizing only the synthesizing form.
Quantitative global proteome and lysine succinylome analyses provide insights into metabolic regulation and lymph node metastasis in gastric cancer