Recombinant Human PCNA Protein Standard (His tag)
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Recombinant Human PCNA Protein Standard (His tag) is a Human Full Length protein, expressed in Escherichia coli, with >80%, suitable for sELISA, SDS-PAGE.
View Alternative Names
Proliferating cell nuclear antigen, PCNA, Cyclin
- sELISA
Lab
Sandwich ELISA - Recombinant Human PCNA Protein Standard (His tag) (AB316635)
Sandwich ELISA with the capture antibody dilution at 2 µg/mL and detector antibody dilution at 0.5 µg/mL.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human PCNA Protein Standard (His tag) (AB316635)
SDS-PAGE analysis of ab316635 under reducing conditions for 2ug protein.
Reactivity data
Product details
While the standard is the same as the one provided in the corresponding SimpleStep ELISA Kit, it cannot be treated as the consumable provided with our SimpleStep ELISA Kit due to differences in its concentration calibration.
Abcam guarantee that this protein standard is suitable for use in a sandwich ELISA. Individual results may vary due to differences in technique, laboratory equipment, buffers, and other experimental factors. The detection range provided for this protein standard is based on initial sandwich ELISA validation data.
The protein concentration is the concentration after validation on our sandwich ELISA platform. This Standard protein is guaranteed to work with our Capture and Detector antibodies in sELISA. Please contact our Scientific Support team to know which antibody pair is suitable for this protein.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
This protein serves a core function in cell cycle regulation and DNA repair. PCNA acts as a scaffold for the assembly of numerous proteins involved in DNA processing forming part of the replication fork complex. It interacts with cyclins and cyclin-dependent kinases (CDKs) linking DNA synthesis to cell cycle progression. Furthermore PCNA partners with proteins involved in DNA mismatch repair base excision repair and nucleotide excision repair.
Pathways
PCNA is integral in the DNA replication and repair pathways. It closely associates with the p21 protein which regulates the cell cycle by inhibiting cyclin-CDK complexes upon DNA damage. PCNA also plays a part in the ubiquitin-proteasome pathway where its modification by ubiquitin impacts how cells respond to DNA damage. This modification recruits specific proteins for DNA repair highlighting its central role in maintaining genomic stability.
Specifications
Form
Liquid
General info
Function
Auxiliary protein of DNA polymerase delta and epsilon, is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand (PubMed : 35585232). Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA repair and DNA damage tolerance pathways (PubMed : 24939902). Acts as a loading platform to recruit DDR proteins that allow completion of DNA replication after DNA damage and promote postreplication repair : Monoubiquitinated PCNA leads to recruitment of translesion (TLS) polymerases, while 'Lys-63'-linked polyubiquitination of PCNA is involved in error-free pathway and employs recombination mechanisms to synthesize across the lesion (PubMed : 24695737).
Sequence similarities
Belongs to the PCNA family.
Post-translational modifications
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 (PubMed:19419956, PubMed:24939902). 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 (PubMed:24939902). Acetylation disrupts interaction with NUDT15 and promotes degradation (PubMed:19419956).. Ubiquitinated (PubMed:20227374, PubMed:24939902). 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.
Subcellular localisation
Nucleus
Target data
Product promise
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