Recombinant Human PCNA Protein (His Tag)

Name: Recombinant Human PCNA Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-3662
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	P12004
Synonym	ATLD2
Background	Proliferating Cell Nuclear Antigen (PCNA) is a protein only expresse in nomal proliferate cells and cancer cells. It is central to both DNA replication and repair. One of the well-established functions for PCNA is its role as the processivity factor for DNA polymerase delta and epsilon. PCNA tethers the polymerase catalytic unit to the DNA template for rapid and processive DNA synthesis. Two forms of PCNA exist in cells: (i) a detergent-insoluble trimeric form stably associated with the replicating forks during S phase and (ii) a soluble form in quiescent cells in G1 and G2 phases. PCNA forms a toroidal trimer in S phase with replication factor-C (RF-C) and DNA in an ATP-dependent manner and enables the loading of DNA polymerase delta and epsilon onto the complex. The close association of PCNA with kinase complexes involved in cell cycle machinery indicates that PCNA has a regulatory role in cell cycle progression. PCNA also participates in the processing of branched intermediates that arise during the lagging strand DNA synthesis.
Description	A DNA sequence encoding the mature form of human PCNA (P12004) (Met 1-Ser 261) was expressed, with a His tag at the N-terminus.
Source	Baculovirus-Insect Cells
Predicted N Terminal	Met
AA Sequence	Met 1-Ser 261
Molecular Weight	The recombinant human PCNA consists of 280 a.a. and has a calculated molecular mass of 31 kDa. It migrates as an approximately 36 kDa band in SDS-PAGE under reducing conditions.
Purity	>90% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile 50mM Na3PO4, 300mM NaCl, 10% glycerol, pH 7.0, 2mM DTT.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. 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. 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.
Subcellular Location	Nucleus.
Protein Families	PCNA family
Database References	HGNC: 8729 OMIM: 176740 KEGG: hsa:5111 STRING: 9606.ENSP00000368438 UniGene: Hs.147433
Associated Diseases	Ataxia-telangiectasia-like disorder 2 (ATLD2)

Gene Functions References

PCNA recognizes the DNA structure through a set of basic residues within the ring channel organized to match the pitch of B-DNA, establishing short-lived polar interactions with consecutive DNA phosphates. PMID: 28071730
Results show that HECW2 interacts with PCNA mediating its ubiquitination and proteasomal degradation. PMID: 29753763
It has been shown that conjugation of SUMO2, but not SUMO1 or SUMO3, to the essential replication factor PCNA is induced on transcribed chromatin by the RNAPII-bound helicase RECQ5. PMID: 30006506
This study identified PCNA-peptide interactions formed in the peptide bound simulation that play a crucial role in complex formation. The calculated binding energies correlate well with the measured binding affinities of various peptides to PCNA. PMID: 29095607
Results suggest that CDK-mediated phosphorylation of Cdt2 inactivates its ubiquitin ligase activity by reducing its affinity to PCNA, an important strategy for regulating the levels of key proteins in the cell cycle. PMID: 29424068
CHAF1A and PCNA are highly expressed in cervical squamous cell carcinoma and associated with the malignancy PMID: 29382432
DDB2-PCNA interaction may contribute to a correct DNA damage response for maintaining genome integrity PMID: 29604309
this study shows that cytoplasmic PCNA connects glycolysis and cell survival in acute myeloid leukemia PMID: 27759041
The results revealed that PCNA is predominantly localized in the cytoplasm, while hAng is distributed both in the nucleus and in the cytoplasm. hAng and PCNA colocalize in the cytoplasm, suggesting that they may interact in this compartment. PMID: 28777577
PCNA and E-cadherin may have roles in prognosis of patients with gastric cancer PMID: 28611525
PCNA and MutLalpha interact specifically but weakly in solution to form a complex of approximately 1:1 stoichiometry that depends on PCNA interaction with the C-terminal endonuclease domain of the MutLalpha PMS2 subunit. PMID: 28439008
FAN1 interaction with ubiquitylated PCNA alleviates replication stress and preserves genomic integrity independently of BRCA2 PMID: 29051491
Treatment with 240 mg/l matrine reduced the protein expression levels of PCNA and eIF4E. Matrine also reduced the migration ability of A549 cells and inhibited their proliferation, which may be associated with the overexpression of p53 and p21, and the reduction of PCNA and eIF4E expression levels. PMID: 28447756
The here presented evidence that the PCNA inner surface is highly regulated to control DNA damage resistance represents a new concept that offers new opportunities to develop tools to manipulate the DNA damage response in cancer treatment. [review] PMID: 28814116
Data suggest that, as part of DNA repair in nucleus of embryonic stem cells, IGF1R interacts with and phosphorylates PCNA at tyrosine residues 60, 133, and 250; this is followed by mono- and polyubiquitination of PCNA by RAD18 and SHPRH. (IGF1R = insulin-like growth factor 1 receptor; PCNA = proliferating cell nuclear antigen; RAD18 = E3 ubiquitin-protein ligase RAD18; SHPRH = E3 ubiquitin-protein ligase SHPRH) PMID: 28924044
Here, we report the complex structure of PCNA and the peptide ((784)NEILQTLLDLFFPGYSK(800)) derived from UHRF2 that contains a PIP box. Structural analysis combined with mutagenesis experiments provide the molecular basis for the recognition of UHRF2 by PCNA via PIP-box. PMID: 28951215
The complex between p15PAF and trimeric PCNA is of low affinity, forming a transient complex that is difficult to characterize at a structural level due to its inherent polydispersity. We have determined the structure, conformational fluctuations, and relative population of the five species that coexist in solution by combining small-angle X-ray scattering (SAXS) with molecular modelling. PMID: 28180305
Dynamic binding of the PARG non-canonical PIP-box to PCNA. PMID: 28934471
PCNA expression significantly associated with clinical stage, histological grade, and poor prognosis of Osteosarcoma, which could evaluate tumor cell proliferation, and predict its biological behavior and prognosis. PMID: 29019895
These results propose a mechanism for progerin-induced genome instability and accelerated replicative senescence in Hutchinson-Gilford progeria syndrome. PMID: 28515154
High PCNA expression is associated with lung adenocarcinoma. PMID: 28423618
Eco1 mediated acetylation regulates PCNA sliding on DNA in the presence of DNA damage, favoring homologous recombination linked to sister-chromatid cohesion. PMID: 27916662
Damage-induced fork reversal in mammalian cells requires PCNA ubiquitination, UBC13, and K63-linked polyubiquitin chains, previously involved in error-free damage tolerance. Fork reversal in vivo also requires ZRANB3 translocase activity and its interaction with polyubiquitinated PCNA, pinpointing ZRANB3 as a key effector of error-free DNA damage tolerance. PMID: 28886337
Multiple studies provide evidence that PCNA lies at the center of the faithful duplication of eukaryotic genomes and therefore genome integrity. [review] PMID: 28157503
Human CTF18-RFC clamp-loader complexed with non-synthesising POLE efficiently loads the PCNA sliding clamp. PMID: 28199690
Results suggest that the UNG2 N-terminus may serve as a flexible scaffold to tether PCNA and RPA at the replication fork, and that post-translational modifications on the UNG2 N-terminus disrupt formation of the PCNA-UNG2-RPA protein complex. PMID: 28746850
ECRG2 in combination with cisplatin (DDP) can inhibit viability and induce apoptosis in esophageal cancer DDP-resistant cells, possibly via upregulation of p53 expression and downregulation of PCNA expression. PMID: 28348485
Reduced affinity of PCNA(S228I) for specific clients causes subtle cellular defects in undamaged cells which likely contribute to the etiology of PCNA-associated DNA repair disorder (PARD). Analysis of the binding between PCNA and PCNA-interacting proteins (PIPs) shows that the S228I change dramatically impairs the majority of these interactions, including that of Cdt1, DNMT1, PolD3(p66) and PolD4(p12). PMID: 28073635
Data suggest that, during human DNA replication, restricting PCNA (proliferating cell nuclear antigen) to the vicinity of its DNA target site is important; PCNA can be maintained at or near primer/template junctions during DNA synthesis by RPA (replication protein A) or SSB (single-stranded DNA-binding protein); here, the SSB used was from Escherichia coli. PMID: 28590137
Studies demonstrated that POLH interaction with PCNA plays an indispensable role in the recruitment of pol-eta to UV-induced cyclobutane pyrimidine dimers site to carry out translesion synthesis (TLS), and the dissociation of pol-eta from PCNA after TLS is essential for maintaining high fidelity DNA replication. PMID: 26988343
PCNA is a substrate of the HSV-1 deubiquitinase UL36USP, which has previously been shown to be involved mainly in virus uptake and maturation PMID: 28348081
Disruption of PCNA-lamins A/C interactions by prelamin A induces DNA replication fork stalling PMID: 27676213
PCNA plays a critical role in preventing CAG repeat expansions by modulating the structures of dynamic DNA via cooperation with base excision repair enzymes. PMID: 27793507
Replication protein A binds tightly to the single-stranded DNA adjacent to a blocked primer/template junction and restricts PCNA to the upstream duplex region by physically blocking diffusion of PCNA along ssDNA. PMID: 28177605
These findings offer new insights into the determinants of PIP box for PCNA binding. PMID: 27084448
collectively, this study uncovers a new role for CRL4CDT2 in protecting genomic integrity against replication stress via regulated proteolysis of PCNA-associated SDE2 and provides insights into how an integrated UBL domain within linear polypeptide sequence controls protein stability and function. PMID: 27906959
The aim of this study is to analyze the immunoexpression of Ki67, p53, MCM3 and PCNA markers in epithelial remnants of dental follicles of impacted teeth and to identify a possible correlation between the immunoexpression of these markers in dentigerous cysts and keratocystic odontogenic tumors. PMID: 27516012
REV1 promote PCNA monoubiquitylation after UV radiation through interacting with ubiquitylated RAD18. PMID: 26795561
USP7 suppresses H2O2-induced mutagenesis involving cell-cycle-independent processes such as DNA repair. PMID: 26673319
Effect of Fenugreek seed extract (FCE) was studied using HepG2 cell line; evaluated apoptosis effect and changes in expression of PCNA and tp53 due to FCE. PMID: 26557712
The authors describe the structure of the disease-causing S228I variant, which reveals a large conformational change that dramatically transforms the binding pocket for PCNA client proteins. PMID: 26688547
Studies show that acidic residue methyltransferase 1 (Armt1) has a vital role in regulation of the DNA damage response likely through its ability to O-methylate glutamyl residues of the DNA repair factor proliferating cell nuclear antigen (PCNA). PMID: 26450907
Hydrophobic pocket of PCNA is the key domain mediating ALKBH2/PCNA interaction. PCNA association with ALKBH2 increases significantly during DNA replication, suggesting that ALKBH2 forms a cell-cycle dependent complex with PCNA. PMID: 26408825
Report PCNA expression in giant cell tumor of bones. PMID: 26339416
p15PAF acts as a flexible drag that regulates PCNA sliding along the DNA and facilitates the switch from replicative to translesion synthesis polymerase binding. PMID: 25762514
14-3-3zeta reduces DNA damage by interacting with and stabilizing proliferating cell nuclear antigen PMID: 25169136
data indicated that IncRNA-PCNA-AS1 may participate in the gastric cancer carcinogenesis and development and may serve as a new biomarker for patients with gastric cancer PMID: 26731993
Bub1 in complex with LANA recruits PCNA to regulate Kaposi's sarcoma-associated herpesvirus latent replication and DNA translesion synthesis. PMID: 26223641
Results revealed that mutation of lysine K164 in PCNA disrupts mono-ubiquitination of the multiple units within a homo-trimer complex as well as a DNA damage tolerance pathway. PMID: 25692884
A reverse PIP Box interaction occurs with PCNA. Small-molecule ligand binding at the PIP Box interaction site confirmed the adaptive nature of the protein in dictating overall shape and implicates allosterism in transmitting biological effects. PMID: 25036435

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