Recombinant Human PCNA Protein

Name: Recombinant Human PCNA Protein
Brand: Beta LifeScience
SKU: BL-1263SG
Availability: InStock

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Accession	NM_002592
Synonym	MGC8367
Background	PCNA is a nuclear protein whose appearance correlates with the proliferative state of the cells and is a cofactor of DNA polymerase delta. PCNA is a homotrimer and helps increase the processivity of leading strand synthesis during DNA replication. In response to DNA damage, PCNA is ubiquitinated and is involved in the RAD6-dependent DNA repair pathway. Immunofluorescence studies have shown that p300 may play a role in DNA repair synthesis through its interaction with PCNA. In vitro and in vivo p300 forms a complex with PCNA that does not depend on the S phase of the cell cycle and stimulates DNA synthesis in vitro (1). PCNA interacts with the Williams syndrome transcription factor (WSTF) allowing it to target to DNA replication foci, that then allows recruitment of SNF2H (2).
Description	Recombinant full-length human PCNA was produced by E. coli system, fused with a His tag at N-terminus.
Source	E.coli
AA Sequence	Full Length
Molecular Weight	~37 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human PCNA Protein should be stored should be stored at < -70°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: 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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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