Recombinant Human Dna Polymerase Theta (POLQ) Protein (His-SUMO)

Name: Recombinant Human Dna Polymerase Theta (POLQ) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-06522P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Dna Polymerase Theta (POLQ) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O75417
Target Symbol	POLQ
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	C-6His-SUMO
Target Protein Sequence	SSSESLSIIDVASDQNLFQTFIKEWRCKKRFSISLACEKIRSLTSSKTATIGSRFKQASSPQEIPIRDDGFPIKGCDDTLVVGLAVCWGGRDAYYFSLQKEQKHSEISASLVPPSLDPSLTLKDRMWYLQSCLRKESDKECSVVIYDFIQSYKILLLSCGISLEQSYEDPKVACWLLDPDSQEPTLHSIVTSFLPHELPLLEGMETSQGIQSLGLNAGSEHSGRYRASVESILIFNSMNQLNSLLQKENLQDVFRKVEMPSQYCLALLELNGIGFSTAECESQKHIMQAKLDAIETQAYQLAGHSFSFTSSDDIAEVLFLELKLPPNREMKNQGSKKTLGSTRRGIDNGRKLRLGRQFSTSKDVLNKLKALHPLPGLILEWRRITNAITKVVFPLQREKCLNPFLGMERIYPVSQSHTATGRITFTEPNIQNVPRDFEIKMPTLVGESPPSQAVGKGLLPMGRGKYKKGFSVNPRCQAQMEERAADRGMPFSISMRHAFVPFPGGSILAADYSQLELRILAHLSHDRRLIQVLNTGADVFRSIAAEWKMIEPESVGDDLRQQAKQICYGIIYGMGAKSLGEQMGIKENDAACYIDSFKSRYTGINQFMTETVKNCKRDGFVQTILGRRRYLPGIKDNNPYRKAHAERQAINTIVQGSAADIVKIATVNIQKQLETFHSTFKSHGHREGMLQSDQTGLSRKRKLQGMFCPIRGGFFILQLHDELLYEVAEEDVVQVAQIVKNEMESAVKLSVKLKVKVKIGASWGELKDFDV
Expression Range	1820-2590aa
Protein Length	Partial
Mol. Weight	98.7 kDa
Research Area	Epigenetics And Nuclear Signaling
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	DNA polymerase that promotes microhomology-mediated end-joining (MMEJ), an alternative non-homologous end-joining (NHEJ) machinery triggered in response to double-strand breaks in DNA. MMEJ is an error-prone repair pathway that produces deletions of sequences from the strand being repaired and promotes genomic rearrangements, such as telomere fusions, some of them leading to cellular transformation. POLQ acts as an inhibitor of homology-recombination repair (HR) pathway by limiting RAD51 accumulation at resected ends. POLQ-mediated MMEJ may be required to promote the survival of cells with a compromised HR repair pathway, thereby preventing genomic havoc by resolving unrepaired lesions. The polymerase acts by binding directly the 2 ends of resected double-strand breaks, allowing microhomologous sequences in the overhangs to form base pairs. It then extends each strand from the base-paired region using the opposing overhang as a template. Requires partially resected DNA containing 2 to 6 base pairs of microhomology to perform MMEJ. The polymerase activity is highly promiscuous: unlike most polymerases, promotes extension of ssDNA and partial ssDNA (pssDNA) substrates. Also exhibits low-fidelity DNA synthesis, translesion synthesis and lyase activity, and it is implicated in interstrand-cross-link repair, base excision repair and DNA end-joining. Involved in somatic hypermutation of immunoglobulin genes, a process that requires the activity of DNA polymerases to ultimately introduce mutations at both A/T and C/G base pairs.
Subcellular Location	Nucleus. Chromosome.
Protein Families	DNA polymerase type-A family
Database References	HGNC: 9186 OMIM: 114480 KEGG: hsa:10721 STRING: 9606.ENSP00000264233 UniGene: PMID: 28695890 Data suggest that translesion DNA synthesis mediated by (1) POLI-dependent pathway (2) REV1- and POLN-dependent pathway, or (3) POLtheta-dependent pathway occur in predominantly error-free manner in human cells. (POLI = DNA polymerase iota; REV1 = DNA repair protein-REV1; POLN = DNA polymerase nu; POLtheta = DNA polymerase theta) PMID: 29330301 results suggest that bypass of Tg by Pol theta; results in mutations opposite the lesion, as well as frameshift mutations PMID: 29243925 This article summarizes work on the expression and purification of the full-length protein, and then focus on the design, expression, and purification of an active C-terminal polymerase fragment. Strategies to obtain and improve crystals of a ternary POLQ complex (enzyme:DNA:nucleotide) are also presented, along with key elements of the structure. PMID: 28668117 Our results indicate that there is a synthetic lethal relationship between pol theta;-mediated DNA repair and homologous recombination pathways PMID: 27533083 Data suggest that error-free DNA replication through 3-deaza-3-methyladenine adduct is mediated via three different pathways dependent upon POL-iota/POL-kappa, POL-theta, and POL-zeta. PMID: 28939775 Use fluorescence resonance energy transfer to monitor assembly of the human replicative polymerase holoenzyme. PMID: 23577232 These results suggest that variants in the POLQ gene may be associated with the risk of Luminal breast cancer PMID: 25417172 A DNA repair variant in POLQ (c.-1060A > G) is associated to hereditary breast cancer patients. PMID: 25409685 Polymerase theta; uses a specialized thumb subdomain to establish unique upstream contacts to the primer DNA strand. PMID: 25775267 Microhomology-mediated end-joining is dependent on Poltheta; in human cells. PMID: 25643323 depletion of Poltheta; has a synergistic effect on cell survival in the absence of BRCA genes, suggesting that the inhibition of this mutagenic polymerase represents a valid therapeutic avenue for tumours carrying mutations in homology-directed repair genes PMID: 25642960 results reveal a synthetic lethal relationship between the homologous-recombination pathway and Poltheta;-mediated repair in epithelial ovarian cancers, and identify Poltheta; as a novel druggable target for cancer therapy PMID: 25642963 A role for DNA polymerase theta; in promoting replication through oxidative DNA lesion, thymine glycol, in human cells. PMID: 24648516 POLQ possesses a DNA polymerase activity that appears to be template independent and allows efficient extension of single-stranded DNA as well as duplex DNA with either protruding or multiply mismatched 3'-OH termini. PMID: 22135286 overexpression in breast cancer confers an adverse prognosis and is associated with key cancer pathways PMID: 20700469 Data show that POLQ overexpression may be a promising genetic instability and prognostic marker for breast cancer. PMID: 20624954 DNA polymerase theta purified from human cells is a high-fidelity enzyme. PMID: 12051913 the isolation of the full-length human DNA POLQ gene, and an initial characterization of its gene product, DNA polymerase theta PMID: 14576298 DNA Pol theta has a specialized function in lymphocytes and in tumor progression PMID: 14735462 POLQ has a high efficiency in by-passing DNA damage. PMID: 15496986 analysis of human DNA polymerase eta error-prone synthesis on DNA deoxyadenosine adducts PMID: 16188888 The results demonstrate that activation of a UV-induced DNA damage response pathway, involving phosphorylation of RPA p34 by DNA-PK, is enhanced in cells lacking poleta. PMID: 16520097 Pol eta can play an important role in determining the cellular sensitivity to therapeutic agents. PMID: 16603639 DNA polymerase eta (Poleta) is responsible for efficient translesion synthesis (TLS) past cis-syn cyclobutane thymine dimers (TT dimers), the major DNA lesions induced by UV irradiation. PMID: 16824193 Human DNA polymerase eta selectively produces a two-base deletion in copying the N2-guanyl adduct of 2-amino-3-methylimidazo[4,5-f]quinoline but not the C8 adduct at the NarI G3 site PMID: 16835218 The enzymatic reactions with human DNA polymerase eta on oxidative products of guanine and 8-oxoG, is investigated. PMID: 17150533 Evolutionary conservation of efficient T[CPD]T bypass by HsPoleta and AtPoleta may reflect a high degree of exposure of human skin and plants to solar UV-B radiation PMID: 18366182 When copying undamaged DNA, DNA polymerase theta generates single base errors at rates 10- to more than 100-fold higher than for other family A members. PMID: 18503084 Domain mapping of the 98-kDa enzyme by limited proteolysis and NaBH(4) cross-linking with a base excision repair intermediate revealed that the dRP lyase active site resides in a 24-kDa domain of Pol theta. PMID: 19188258

FAQs

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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.