Recombinant Saccharomyces Cerevisiae Proliferating Cell Nuclear Antigen (POL30) Protein (His-SUMO)

Name: Recombinant Saccharomyces Cerevisiae Proliferating Cell Nuclear Antigen (POL30) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09100P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Description	Recombinant Saccharomyces Cerevisiae Proliferating Cell Nuclear Antigen (POL30) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P15873
Target Symbol	POL30
Synonyms	POL30; YBR088C; YBR0811; Proliferating cell nuclear antigen; PCNA
Species	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MLEAKFEEASLFKRIIDGFKDCVQLVNFQCKEDGIIAQAVDDSRVLLVSLEIGVEAFQEYRCDHPVTLGMDLTSLSKILRCGNNTDTLTLIADNTPDSIILLFEDTKKDRIAEYSLKLMDIDADFLKIEELQYDSTLSLPSSEFSKIVRDLSQLSDSINIMITKETIKFVADGDIGSGSVIIKPFVDMEHPETSIKLEMDQPVDLTFGAKYLLDIIKGSSLSDRVGIRLSSEAPALFQFDLKSGFLQFFLAPKFNDEE
Expression Range	1-258aa
Protein Length	Full Length
Mol. Weight	44.9kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	This protein is an 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. Involved in DNA repair.
Subcellular Location	Nucleus.
Protein Families	PCNA family
Database References	KEGG: sce:YBR088C STRING: 4932.YBR088C

Gene Functions References

proliferating cell nuclear antigen (PCNA) unloading activity of Elg1 is important for coordinating DNA replication forks with the process of replication-coupled nucleosome assembly to maintain silencing of HML and HMR through S-phase PMID: 29440488
found evidence implicating PCNA in the maintenance of the high-order structure and stability of heterochromatin, which indicates a role of DNA replication in heterochromatin maintenance PMID: 27987109
Srs2 interaction with PCNA allows the helicase activity to unwind fork-blocking CAG/CTG hairpin structures to prevent DNA breaks during DNA replication. Independently of PCNA binding, Srs2 also displaces Rad51 from nascent strands to prevent recombination-dependent repeat expansions and contractions. PMID: 28175398
the various roles of Elg1 in genome stability maintenance involve the unloading of both modified and unmodified PCNA. PMID: 28108661
Pro-recombination Role of Srs2 Protein Requires SUMO (Small Ubiquitin-like Modifier) but Is Independent of PCNA (Proliferating Cell Nuclear Antigen) Interaction. PMID: 26861880
results suggest that Elg1-RLC acts as a general PCNA unloader and is dependent upon DNA ligation during chromosome replication. PMID: 26212319
Elevated levels of PCNA rescue pds5-1 temperature sensitivity and cohesion defects, but do not rescue pds5-1 mutant cell condensation defects. PMID: 25986377
Authors discuss the interplay of POL30 and Srs2 proteins in error-free DNA-damage tolerance in Saccharomyces cerevisiae and show how sumoylated PCNA recruits Srs2 for this mechanism. [Review] PMID: 26041265
In contrast to the "toolbelt" model, which was demonstrated for bacterial and archaeal sliding clamps, our results suggest a mechanism of sequential switching of partners on the eukaryotic PCNA trimer during DNA replication and repair. PMID: 25228764
Cells deficient in PCNA unloading exhibit increased chromosome breaks. PMID: 25449133
Data indicate that the C22Y substitution alters the positions of the alpha-helices lining the central hole of the POL30 (PCNA) ring, whereas the C81R substitution creates a distortion in an extended loop near the PCNA subunit interface. PMID: 23869605
Elg1-replication factor C-like complex functions in unloading of both unmodified and SUMOylated PCNA during DNA replication. PMID: 23499004
The increased dynamics of hPCNA relative to scPCNA may allow it to acquire multiple induced conformations upon binding to its substrates enlarging its binding diversity. PMID: 21364740
show that yeast Elg1 interacts physically and genetically with PCNA, in a manner that depends on PCNA modification, and exhibits preferential affinity for SUMOylated PCNA. PMID: 20571511
High-copy expression of POL30 (PCNA) suppresses the canavanine mutation rate of all the rad27 alleles, including rad27Delta. PMID: 19596905
SUMO-modified PCNA functionally cooperates with Srs2 PMID: 15931174
Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase SRs2p. PMID: 15989970
Mediates the entry of the flap endonuclease and DNA ligase I into the process of Okazaki fragment joining, and this ordered entry is necessary to prevent CAG repeat tract expansions. PMID: 16079237
PCNA acts as a scaffold for consecutive protein-protein interactions that allow for the coordination of mismatch repair steps. PMID: 16303135
An open PCNA clamp in a complex with RFC through fluorescence energy transfer experiments was captured. PMID: 16476998
Diubiquitinated Mcm10 interacts with PCNA to facilitate an essential step in DNA elongation. PMID: 16782870
Mgs1 physically associates with PCNA and that Mgs1 helps suppress the RAD6 DNA damage tolerance pathway in the absence of exogenous DNA damage. PMID: 16809783
role for PCNA in regulating the mutagenic activity of Polzeta separate from its modification at Lys164 PMID: 16957771
The loaded form of yPCNA may play an important effector role in directing yMutLalpha incision to the discontinuous strand of a nicked heteroduplex. PMID: 17951253
Mismatch repair-PCNA interactions are important for repairing mismatches formed during meiotic recombination, but play only a relatively minor role in regulating the fidelity of mitotic recombination. PMID: 18245822
PCNA participates in formation and stability of epigenetically regulated chromatin through a pathway that includes replication factor C, the chromatin assembly factor Asf1p, and the K56-specific acetyltransferase Rtt109p. PMID: 18558650
PCNA modification by SUMO is controlled by DNA PMID: 18701921
the balance between HDR and NHEJ pathways is crucially controlled by genes of the RAD6 pathway through modifications of PCNA PMID: 18722556
While wild-type PCNA stimulates incorporation by Dna polymerase eta opposite an abasic site, the mutant PCNA protein actually inhibits incorporation opposite this DNA lesion. PMID: 19053247
Data suggest that mono-ubiquitination of PCNA is induced by nucleotide misincorporation by DNA polymerase alpha. PMID: 19279190
DNA binding commits Saccharomyces cerevisiae replication factor C to ATP hydrolysis, which is followed by proliferating cell nuclear antigen (PCNA) closure and PCNA.DNA release. PMID: 19285992

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.