Recombinant Human Dna Repair Protein Rad51 Homolog 1 (RAD51) Protein (His)

Name: Recombinant Human Dna Repair Protein Rad51 Homolog 1 (RAD51) Protein (His)
Brand: Beta LifeScience
SKU: BLC-07409P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Dna Repair Protein Rad51 Homolog 1 (RAD51) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q06609
Target Symbol	RAD51
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	AMQMQLEANADTSVEEESFGPQPISRLEQCGINANDVKKLEEAGFHTVEAVAYAPKKELINIKGISEAKADKILAEAAKLVPMGFTTATEFHQRRSEIIQITTGSKELDKLLQGGIETGSITEMFGEFRTGKTQICHTLAVTCQLPIDRGGGEGKAMYIDTEGTFRPERLLAVAERYGLSGSDVLDNVAYARAFNTDHQTQLLYQASAMMVESRYALLIVDSATALYRTDYSGRGELSARQMHLARFLRMLLRLADEFGVAVVITNQVVAQVDGAAMFAADPKKPIGGNIIAHASTTRLYLRKGRGETRICKIYDSPCLPEAEAMFAINADGVGDAKD
Expression Range	2-339aa
Protein Length	Full Length of Mature Protein
Mol. Weight	40.9 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	Plays an important role in homologous strand exchange, a key step in DNA repair through homologous recombination (HR). Binds to single and double-stranded DNA and exhibits DNA-dependent ATPase activity. Catalyzes the recognition of homology and strand exchange between homologous DNA partners to form a joint molecule between a processed DNA break and the repair template. Binds to single-stranded DNA in an ATP-dependent manner to form nucleoprotein filaments which are essential for the homology search and strand exchange. Part of a PALB2-scaffolded HR complex containing BRCA2 and RAD51C and which is thought to play a role in DNA repair by HR. Plays a role in regulating mitochondrial DNA copy number under conditions of oxidative stress in the presence of RAD51C and XRCC3. Also involved in interstrand cross-link repair.
Subcellular Location	Nucleus. Cytoplasm. Cytoplasm, perinuclear region. Mitochondrion matrix. Chromosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Protein Families	RecA family, RAD51 subfamily
Database References	HGNC: 9817 OMIM: 114480 KEGG: hsa:5888 UniGene: PMID: 28067217 RAD51 135G>C polymorphism is not associated with colorectal cancer. PMID: 29893328 Data show that short ssDNA traverses the nuclear membrane, but is drawn into the nucleus by binding to the DNA replication and repair factors replication protein A (RPA) and Rad51 recombinase (Rad51). PMID: 27230542 region in the N terminus of BRCA2 exhibits DNA binding activity and promotes RAD51-mediated homologous recombination PMID: 27628236 We have identified and characterised a novel DNA damage response mechanism in melanoma. Instead of increasing levels of RAD51 on encountering cisplatin-induced interstrand crosslinks during replication, melanoma cells shut down RAD51 synthesis and instead boost levels of translesion synthesis DNA polymerase zeta to allow replication to proceed PMID: 29254481 Twenty-one different deleterious variants were identified in the RAD51 paralogs in 30 patients with ovarian and/or beast cancer. PMID: 29255180 he results of the study indicate that Akt1 seems to be a regulatory component in the homologous recombination (HR) repair of DNA double-strand break in a Rad51-dependent manner. PMID: 29156644 RAD51 135G/C polymorphism was a risk factor for the three common gynecological tumors, especially for endometrial cancer among hospital-based populations. PMID: 29952992 Fanconi anemia-associated RAD51 mutants are defective at stalled fork protection. Mutant RAD51 nucleoprotein filaments are unstable due to aberrant ATP binding and hydrolysis. PMID: 29020621 Inactivation of homologous recombination factors BRCA1, BRCA2, or RAD51 hypersensitizes cells to acetaldehyde treatment, in spite of the Fanconi anemia pathway being functional. PMID: 28729482 DNA sequencing was performed for six single-nucleotide polymorphisms in the GSTP1, RAD51, XRCC1 and XRCC3 genes in BC patients and the control group. Two variants in the 5'-UTR of the XRCC3 and RAD51 genes showed a significant association with susceptibility to breast cancer. Additionally, authors reported 2 mutations in intron 7 of the XRCC3 gene. PMID: 28315507 our data demonstrated for the first time that inhibition of RAD51 suppressed the cervical cancer cell proliferation and the growth of cervical cancer xenografts by attenuating cell cycle transition, which could be a functional link between RAD51 and cyclin D1 and p21. PMID: 28627709 Low RAD51 gene expression is associated with breast cancer. PMID: 28058614 (-)-Guaiol is involved in cell autophagy to regulate the expression of RAD51, leading to double-strand breaks triggered cell apoptosis PMID: 27566579 Report a requirement for PARP2 in stabilizing replication forks that encounter base excision repair (BER) intermediates through Fbh1-dependent regulation of Rad51. Whereas PARP2 is dispensable for tolerance of cells to single stranded breaks or homologous recombination dysfunction, it is redundant with PARP1 in BER. PMID: 29467415 Histone deacetylases 1 and 2 cooperate in regulating BRCA1, CHK1, and RAD51 expression in acute myeloid leukemia cells. PMID: 28030834 BRCA1-BARD1 mutants with weakened RAD51 interactions show compromised DNA joint formation and impaired mediation of homologous recombination and DNA repair in cells; results identify a late role of BRCA1-BARD1 in homologous recombination, an attribute of the tumour suppressor complex that could be targeted in cancer therapy PMID: 28976962 Our data suggest that in both BRCA1-mutant and BRCA1-wild-type TNBCs, CSCs are relatively resistant to PARP inhibition. This resistance is mediated by RAD51, suggesting that strategies aimed at targeting RAD51 may increase the therapeutic efficacy of PARPi PMID: 28034904 Data show that the combination of targeting RAD51 and p38 inhibits cell proliferation both in vitro and in vivo, which was further enhanced by targeting of PARP1. PMID: 27507046 Data suggest that oleandrin may be a potential anti-tumor agent by suppressing the expression of RAD51 recombinase. PMID: 27449097 we demonstrated that Y54 phosphorylation enhances the RAD51 recombinase activity by at least two different mechanisms, modifies the RAD51 nucleoprotein filament formation, and allows RAD51 to compete efficiently with ssDNA binding protein RPA. PMID: 27671650 Mutations F86L & E258A affect the multimerization/BRCA2 binding region of RAD51.Both variants exhibit altered thermal stability,reduced DNA binding affinity,reduced ATPase activity compared to wild-type. F86L efficiently catalyzes DNA strand exchange reactions,whereas strand exchange activity of E258A is severely reduced.Mixtures of either variant with wild-type RAD51 exhibit strong defects in DNA strand exchange activity PMID: 29100040 Data indicate that lupus autoantibody 3E10 directly binds to the N-terminus of RAD51 recombinase, sequesters RAD51 in the cytoplasm, and impedes RAD51 binding to DNA. PMID: 29036688 Study suggested that RAD51, XRCC1, and XRCC3 polymorphisms may be predictive factors for radiation-induced acute toxicity in rectal cancer patients treated with preoperative combined therapy. PMID: 25811296 n metastatic high grade clear cell carcinoma, this expression was more pronounced. Though we could not demonstrate direct correlation, we showed that epigenetic modification by methylation is associated with decreased genomic translation of Rad51. PMID: 27170370 our study provides a strong rationale for targeting RAD51-mediated repair to specifically radiosensitize GSCs. PMID: 28076755 The anti-recombinase activity of BLM is of general importance for normal retention of RAD51 at DNA double strand break sites and regulation of homologous recombination. PMID: 28912125 Results showed that the expression of RAD51 is both nuclear and cytoplasmic and it varies among breast cancer (BC) phenotypes. Lack of RAD51 nuclear expression is associated with poor prognostic parameters and shorter survival in invasive BC patients suggesting that RAD51 might play a role in BC development and progression. PMID: 27464795 USP21 interacts with, deubiquitinates and stabilizes BRCA2 to promote efficient RAD51 loading at DNA double-strand breaks. PMID: 28743957 CTC1/STN1/TEN1 (CST) deficiency diminishes HU-induced RAD51 foci formation. PMID: 27487043 These results underscore the importance of RAD51 in radioresistance of glioblastoma stem cells PMID: 27495836 PLAUR to be essential for activation of Checkpoint kinase 1 (CHK1); maintenance of cell cycle arrest after DNA damage in a TP53-dependent manner; expression, nuclear import and recruitment to DNA-damage foci of RAD51 recombinase, the principal protein involved in the homologous recombination repair pathway. PMID: 27685627 By antagonizing RAD51 at forks, RADX allows cells to maintain a high capacity for homology-directed repair while ensuring that replication functions of RAD51 are properly regulated. Thus, RADX is essential to achieve the proper balance of RAD51 activity to maintain genome stability. PMID: 28735897 E3 ligase RFWD3 functions in timely removal and degradation of RPA and RAD51 to allow homologous recombination progression to subsequent steps following mitomycin C damage. PMID: 28575658 In the absence of RAD51, the unprotected newly replicated genome is degraded by the exonuclease activity of MRE11, and the fragmented nascent DNA accumulates in the cytosol, initiating an innate immune response. PMID: 28334891 Architectural plasticity of human BRCA2-RPA-RAD51 complexes in DNA break repair has been described. PMID: 28168276 cyclin D1 and other cyclins such as cyclin A regulates DNA integrity through RAD51 interaction with the BRCA2 C-terminal domain PMID: 26387543 Upregulation of RAD51 and overexpression of Ki67 may be associated with the progression of thyroid cancer. PMID: 28502582 Data suggest that RAD51, BRCA2, and BRCA1 promote stability of nascent DNA at replication forks; RAD51 prevents MRE11 nuclease-mediated degradation of nascent ssDNA; BRCA2 displaces RPA (replication protein A) complex by recruiting RAD51 to protect ssDNA; BRCA1 promotes repair foci following DNA damage and is essential for cell survival. (BRCA = breast cancer recombination protein; RAD51 = Rad51 recombinase) [REVIEW] PMID: 28079255 Data suggest RAD52 binds tightly to RPA/ssDNA complex in presynaptic complex and inhibits RPA turnover; during presynaptic complex assembly, most of RPA and RAD52 is displaced from ssDNA, but some RAD52/RPA/ssDNA complexes persist as interspersed clusters surrounded by RAD51 filaments. (RAD52 = Rad52 DNA repair/recombination protein; RPA = replication protein A; ssDNA = single-stranded DNA; RAD51 = Rad51 recombinase) PMID: 28551686 High RAD51 expression is associated with drug Resistance in Malignant Melanoma. PMID: 26980768 Cryo-EM analyses of human RAD51 in different states of the DNA-strand-exchange process and structures of presynaptic and postsynaptic complexes of RAD51 at near-atomic resolution. PMID: 27941862 By specifically regulating RAD51 activity at uncoupled replication forks, MMS22L-TONSL stabilizes perturbed replication forks by promoting replication fork reversal and stimulating their homologous recombination-mediated restart in vivo. PMID: 27797818 S100A11 is involved in homologous recombination by regulating the appearance of RAD51 in double strand break repair sites. PMID: 27590262 HsRAD51 NPF which may form on nucleosome bound dsDNA can have profound effects on the dynamic nature of nucleosomes, and may even facilitate the recruitment of other factors such as homologous HsRAD51-ssDNA NPFs or HsRAD54. PMID: 27738136 ubiquitination of RAD51 hinders RAD51-BRCA2 interaction, while deubiquitination of RAD51 facilitates RAD51-BRCA2 binding and RAD51 recruitment and thus is critical for proper homologous recombination PMID: 27941124 NEK8 plays a critical role in replication fork stability through its regulation of the DNA repair and replication fork protection protein RAD51. PMID: 27892797 we demonstrate that BCCIPbeta induces a conformational change within the RAD51 filament that promotes release of ADP to help maintain an active presynaptic filament. Our findings reveal a functional role for BCCIPbeta as a RAD51 accessory factor in HR. PMID: 27694622 It has been concluded that stable binding and/or the melting of secondary DNA structures by RPA1 is required for DNA repair, including RAD51-mediated DNA strand exchange, but is dispensable for DNA replication. PMID: 27131385 Results suggest that cell cycle progression and proliferation of HeLa cells can be tightly controlled by the abundance of RAD51 and RAD54 proteins, which are essential for the rapid response to postreplicative stress and DNA damage stress. PMID: 28190324

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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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