Recombinant Human Atp-Dependent Dna Helicase Q1 (RECQL)

Name: Recombinant Human Atp-Dependent Dna Helicase Q1 (RECQL)
Brand: Beta LifeScience
SKU: BLC-02857P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Atp-Dependent Dna Helicase Q1 (RECQL) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P46063
Target Symbol	RECQL
Synonyms	RECQL; RECQ1; RECQL1; ATP-dependent DNA helicase Q1; EC 3.6.4.12; DNA helicase; RecQ-like type 1; RecQ1; DNA-dependent ATPase Q1; RecQ protein-like 1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Target Protein Sequence	MASVSALTEELDSITSELHAVEIQIQELTERQQELIQKKKVLTKKIKQCLEDSDAGASNEYDSSPAAWNKEDFPWSGKVKDILQNVFKLEKFRPLQLETINVTMAGKEVFLVMPTGGGKSLCYQLPALCSDGFTLVICPLISLMEDQLMVLKQLGISATMLNASSSKEHVKWVHAEMVNKNSELKLIYVTPEKIAKSKMFMSRLEKAYEARRFTRIAVDEVHCCSQWGHDFRPDYKALGILKRQFPNASLIGLTATATNHVLTDAQKILCIEKCFTFTASFNRPNLYYEVRQKPSNTEDFIEDIVKLINGRYKGQSGIIYCFSQKDSEQVTVSLQNLGIHAGAYHANLEPEDKTTVHRKWSANEIQVVVATVAFGMGIDKPDVRFVIHHSMSKSMENYYQESGRAGRDDMKADCILYYGFGDIFRISSMVVMENVGQQKLYEMVSYCQNISKCRRVLMAQHFDEVWNSEACNKMCDNCCKDSAFERKNITEYCRDLIKILKQAEELNEKLTPLKLIDSWMGKGAAKLRVAGVVAPTLPREDLEKIIAHFLIQQYLKEDYSFTAYATISYLKIGPKANLLNNEAHAITMQVTKSTQNSFRAESSQTCHSEQGDKKMEEKNSGNFQKKAANMLQQSGSKNTGAKKRKIDDA
Expression Range	1-649aa
Protein Length	Full Length
Mol. Weight	73.5 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 helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction.
Subcellular Location	Nucleus.
Protein Families	Helicase family, RecQ subfamily
Database References	HGNC: 9948 OMIM: 600537 KEGG: hsa:5965 STRING: 9606.ENSP00000395449 UniGene: PMID: 29341116 the RECQL:c.1667_1667 + 3delAGTA mutation in Polish women was not correlated to breast cancer susceptibility PMID: 29351780 Study detected five different RECQL mutation in six unrelated breast cancer patients. The identified mutations include one frame-shift deletion, two splicing site mutation and one nonsense mutation. PMID: 27125668 RECQ1 is significantly overexpressed in multiple myeloma cells vs normal plasma cells. Increased RECQ1 expression is associated with poor prognosis. Its knockdown inhibits cell growth, increases apoptosis, and promotes DNA ds-breaks. Its overexpression protects against melphalan and bortezomib. It interacts with PARP1 and its loss sensitizes to PARP inhibitors. PMID: 28186131 Data indicate that RECQL* c.1667_1667+3delAGTA is not a high-risk mutation for breast cancer though it could represent a moderate-risk breast cancer susceptibility allele.[meta-analysis] PMID: 27832498 The authors have discovered a major sub-pathway of conventional long-patch base excision repair that involves formation of a 9-nucleotide gap 5' to the lesion. This new sub-pathway is mediated by RECQ1 DNA helicase and ERCC1-XPF endonuclease in cooperation with PARP1 poly(ADP-ribose) polymerase and RPA. PMID: 28373211 We conclude that RECQL1 has prognostic and predictive significance in breast cancers. PMID: 27837030 Our results indicate that the zinc binding motif in the RQC domain of RECQ1 is a key structural element that is essential for the structure-functions of RECQ1. PMID: 27248010 Knockdown of RECQ1 significantly suppressed lung cancer cell proliferation, migration and invasion. PMID: 27565844 To better understand the roles of RECQ1, two AL mutants (W227A and F231A) in full-length RECQ1 were characterized biochemically and genetically PMID: 26455304 RECQL is a new breast cancer susceptibility gene. PMID: 26125302 RECQL is a DNA helicase in breast cancer [editorial] PMID: 26387136 RECQ1 A159C genotype may be a prognostic or predictive factor for resectable pancreatic cancer patients who are treated with adjuvant 5-FU before and after 5-FU-based chemoradiation. PMID: 26725729 RECQL is a potential breast cancer susceptibility gene; mutations in this gene contribute to familial breast cancer development. PMID: 25945795 RECQL1 is a prognostic factor for epithelial ovarian cancer and contributes to potential malignancy by inhibiting apoptosis. PMID: 25424877 A novel function of RECQ1 is identified: in gene regulation and indicates that RECQ1 contributes to tumor development and progression, in part, by regulating the expression of key genes that promote cancer cell migration, invasion and metastasis. PMID: 25483193 RECQL is a breast cancer susceptibility gene. PMID: 25915596 we show that RECQ1 can form what appears to be a flat, homotetrameric complex and propose that RECQ1 tetramers are involved in Holliday junction recognition PMID: 25831490 our results provide first indication of nonredundant participation of WRN and RECQ1 in protection from the potentially carcinogenic effects PMID: 25228686 results indicate that RECQL1 plays an important regulatory role in cancer cell proliferation and tumor progression PMID: 24854846 The stimulation of helicase-catalyzed protein displacement is observed with the DNA helicase RECQ1, suggesting a conserved functional interaction of RPA-interacting helicases. PMID: 24895130 RECQL1 may participate in the same pathway as WRN, probably in telomere replication. PMID: 24623817 a crucial role for RECQ1 at naturally occurring fork stalling sites and implicate RECQ1 in mechanisms underlying common fragile site instability in cancer. PMID: 23601052 RECQL1 expression was exceptionally high in rapidly growing ovarian cancer cells. PMID: 23951333 An interaction of RECQ1 with Ku70/80 and a role of the human RecQ helicase in double-strand break repair through nonhomologous end-joining. PMID: 23650516 RECQ1 might have a similar role to that of WRN in helping cells deal with stalled replication forks. PMID: 23095637 RECQ1 promotes restart of DNA replication forks reversed by DNA topoisomerase I inhibition. PMID: 23396353 The data suggested that HomolD-containing promoters require the RNA polymerase II machinery and the proteins DDB1 and RECQL for accurate transcription. PMID: 22705827 Data show that RECQ1 associates with PARP-1 in nuclear extracts and exhibits direct protein interaction in vitro. PMID: 22542292 RAD54 that lacks helicase activity is more efficient in DNA heterology bypass than BLM or REQ1 helicases. PMID: 22356911 RECQ1 might represent a new suitable target for anti cancer therapies aimed to arrest cell proliferation in brain gliomas. PMID: 21752281 The beta-hairpin is a key structural element that controls not only the enzymatic activity of RECQ1, but also the balance between the multiple oligomeric states of the protein. PMID: 21059676 Histological data reveal the potential of RecQL1 as a biological marker predicting the malignancy and progression of liver cancer. PMID: 20198302 These results indicate that RECQ1 and RECQ4 are integral components of the human replication complex and play distinct roles in DNA replication initiation and replication fork progression in vivo. PMID: 20065033 Molecular cloning of a splicing variant of human RECQL helicase. PMID: 12419324 characterization of DNA-unwinding activity PMID: 12419808 RECQ1 alone is able to unwind short DNA duplexes (<110 bp), whereas considerably longer substrates (501 bp) can be unwound only in the presence of human replication protein A (hRPA) PMID: 15096578 RECQ1 has a role in a pathway involving mismatch repair factors PMID: 15886194 analysis of enzymatic properties of the RECQ1 helicase and DNA unwinding and strand annealing activities PMID: 15899892 Identification of RecQL1 as a predominant ATP-dependent, Holliday junction branch migrator present in human nuclear extracts. PMID: 16260474 Our findings suggest that higher-order oligomers are associated with DNA strand annealing, and lower-order oligomers with DNA unwinding. PMID: 17227144 RecQ DNA helicase resolves genetic recombination and suppressive aberrant recombination. PMID: 17483412 Results support that endogenous DNA damage that occurs during DNA replication and remains unrepaired in cancer cells due to RecQL1 silencing induces cancer cell-specific mitotic catastrophe through a less-strict checkpoint in cancer than in normal cells. PMID: 17953710 results provide the first evidence for a role of human RECQ1 in the response to DNA damage and chromosomal stability maintenance and point to the vital importance of RECQ1 in genome homeostasis PMID: 18074021 Human RecQ helicases, BLM and RECQ1, display distinct DNA substrate specificities PMID: 18448429 properties of the RECQ1 helicase may have important implications for the function of RECQ1 in maintenance of genomic stability PMID: 18495662 A crystal structure of a truncated form of the human RECQ1 protein with Mg-ADP, is presented. PMID: 19151156 Topoisomerase I and RecQL1 promote the lytic reactivation of Epstein-Barr virus. PMID: 19494003

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.