Recombinant Human Recq-Like Dna Helicase Blm (BLM) Protein (His)

Name: Recombinant Human Recq-Like Dna Helicase Blm (BLM) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00634P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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

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Product Overview

Description	Recombinant Human Recq-Like Dna Helicase Blm (BLM) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P54132
Target Symbol	BLM
Synonyms	(Bloom syndrome protein)(DNA helicase, RecQ-like type 2)(RecQ2)(RecQ protein-like 3)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	DCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWINQDGCQVICATIAFGMGIDKPDVRFVIHASLPKSVEGYYQESGRAGRDGEISHCLLFYTYHDVTRLKRLIMMEKDGNHHTRETHFNNLY
Expression Range	877-1024aa
Protein Length	Partial
Mol. Weight	23.0 kDa
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	ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction. Participates in DNA replication and repair. Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA. Negatively regulates sister chromatid exchange (SCE). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction. Recruited by the KHDC3L-OOEP scaffold to DNA replication forks where it is retained by TRIM25 ubiquitination, it thereby promotes the restart of stalled replication forks.
Subcellular Location	Nucleus. Note=Together with SPIDR, is redistributed in discrete nuclear DNA damage-induced foci following hydroxyurea (HU) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a RMI complex- and SPIDR-dependent manner.
Protein Families	Helicase family, RecQ subfamily
Database References	HGNC: 1058 OMIM: 210900 KEGG: hsa:641 STRING: 9606.ENSP00000347232 UniGene: PMID: 29523790 Low BLM expression is associated with Colorectal Cancer. PMID: 29386092 BLM is actively recruited to the alternative lengthening of telomeres that are experiencing replication stress and that the recruitment of BLM to these damaged telomeres is interdependent and is regulated by both ATR and Chk1. PMID: 28673972 Our data highlights that BLM helicase and hSSB1 function in a dynamic complex in cells and that this complex is likely required for BLM protein stability and function. PMID: 28506294 In the absence of BLM, sister chromatid exchange events do not occur randomly throughout the genome but are strikingly enriched at coding regions, specifically at sites of guanine quadruplex motifs in transcribed genes. PMID: 29348659 Data show that helicases RHAU, BLM, and WRN exhibit distinct G-quadruplex (GQ) conformation specificity, but use a common mechanism of repetitive unfolding that leads to disrupting GQ structure multiple times in succession. PMID: 27407146 Mutations within the domain VI of BLM detected in human cancer samples demonstrate the functional importance of this domain, suggesting human tumorigenicity resulting from mtBLM may be at least partly attributed to mitigated FANCD2 activation. PMID: 27083049 Sgs1 and BLM regulate R-loop-associated genome instability. PMID: 29042409 These results showed that BLM enters the nucleus via the importin beta1, RanGDP and NTF2 dependent pathway, demonstrating for the first time the nuclear trafficking mechanism of a DNA helicase. PMID: 29017749 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 The authors show that the helicase of hDNA2 functionally integrates with BLM or WRN helicases to promote double-stranded DNA degradation by forming a heterodimeric molecular machine. This collectively suggests that the human DNA2 motor promotes the enzyme's capacity to degrade double-stranded DNA in conjunction with BLM or WRN and thus promote the repair of broken DNA. PMID: 27612385 The BLM-TOP3A-RMI (BTR) dissolvase complex is required for Alternative lengthening of telomeres-mediated telomere synthesis. BLM and SLX4 play opposing roles in recombination-dependent replication at human telomeres. PMID: 28877996 Aberrant BLM cytoplasmic expression associates with DNA damage stress and hypersensitivity to DNA-damaging agents in colorectal cancer. PMID: 27169843 In humans, mutations in BLM give rise to Bloom's syndrome features genomic instability and susceptibity to cancer. PMID: 27238185 in Alternative Lengthening of Telomeres cells, FANCD2 promotes intramolecular resolution of stalled replication forks in telomeric DNA while BLM facilitates their resection and subsequent involvement in the intermolecular exchanges that drive Alternative Lengthening of Telomeres. PMID: 27427384 Results show that BLM-deficient human cells produce hemi-loss of heterozygosity by spontaneous deletion even though they exhibit a high spontaneous frequency of inter-allelic homologous recombination. PMID: 27601585 BLM deficiency enables HeR in human cells PMID: 27100209 these data indicate that carriers of deleterious BLM mutations are at increased risk to develop CRC, albeit with a moderate-to-low penetrance. PMID: 26358404 evidence that BLM is a substrate for Fbw7alpha-dependent ubiquitylation and degradation during mitosis PMID: 26028025 TopBP1 interacts with BLM to maintain genome stability but is dispensable for preventing BLM degradation.Crucial residues mediating BLM-TOP3A/RMI interactions identified. PMID: 25794620 BLM mRNA and BLM protein levels independently influenced BCSS. This is the first and the largest study to provide evidence that BLM is a promising biomarker in breast cancer. PMID: 25673821 These findings indicate that the BLM p.Q548X mutation is not a strong risk factor for ovarian cancer. PMID: 25182961 The binding model of BLM RQC to a HJ offers the structural insights into the branch migration mechanism of BLM, in which DNA unwinding and annealing might be coordinated. PMID: 24257077 this is the first genetic association study to show the significant association between BLM gene and Prostate cancer susceptibility in Chinese population. PMID: 25472581 RecQ-like helicase BLM subcellular localization is regulated by SUMO-targeted ubiquitin ligase RNF4 in response to DNA damage, presumably to prevent illegitimate recombination events. PMID: 25588990 Chk1 phosphorylates BLM-S502 to inhibit cullin-3-mediated BLM degradation during interphase. PMID: 25015292 Findings indicate that BLM functions in 2 distinct pathways. In one, BLM functions to suppress sister chromatid exchanges formation; in the second one, T99 and T122 phosphorylations are essential for suppression of chromosomal radial formation. PMID: 25766002 A novel frameshift mutation in BLM gene associated with high sister chromatid exchanges (SCE) in heterozygous family members. PMID: 25129257 The data highlight the importance of Mus81 and Blm in DNA double-strand repair pathways, fertility, development and cancer. PMID: 24858046 Mutational analysis by direct DNA sequencing revealed a novel frameshift mutation (c.1980-1982delAA) in exon 8 of BLM gene, resulting in a truncated protein (p.Lys662fsX5). PMID: 24118499 BLM protein crystal structure provides detailed information on the interactions of the protein with DNA and helps to explain the mechanism coupling ATP hydrolysis and DNA unwinding. PMID: 24816114 Results suggest that BRCA1 participates in ALT through its interactions with RAD50 and BLM. PMID: 25084169 WRN and BLM act epistatically with DNA2 to promote the long-range resection of double strand break ends in human cells. PMID: 25122754 identified mRNA and miRNA expression differences in Bloom syndrome patient and BLM-depleted cells PMID: 24958861 Data highlight a dual role for BLM that influences the DSB repair pathway choice: protection against CtIP/MRE11 long-range deletions associated with A-EJ and promotion of DNA resection. PMID: 24095737 BLM was ubiquitinated by E3 ligase MIB1 and degraded in G1 cells but was stabilized by TopBP1 in S phase cells. PMID: 24239288 two proteins that interact with BLM, RMI1 and RMI2, are phosphorylated upon SAC activation, and, like BLM, RMI1, and RMI2, are phosphorylated in an MPS1-dependent manner. PMID: 24108125 Case-control study to check an association between the genotypes of the c.-61 G>T and the g.38922 C>G polymorphisms of the RAD51 gene and the g.96267 A>C and the g.85394 A>G polymorphisms of the BLM gene and breast cancer occurrence. PMID: 23404160 The BLM Q548X mutation does not predispose patients to prostate cancer or affect prostate cancer survival. PMID: 24096176 FE65 interactions with BLM and MCM proteins may contribute to the neuronal cell cycle re-entry observed in brains affected by Alzheimer's disease. PMID: 23572515 DNA topoisomerase I stimulates BLM helicase activity on a nucleolar-relevant RNA:DNA hybrid. PMID: 23261817 Consistent with its role as a scaffolding protein for the assembly of BLM and RAD51 foci, cells depleted of SPIDR show increased rate of sister chromatid exchange and defects in homologous recombination repair. PMID: 23509288 BLM helicase is major player in recombination-mediated telomere maintenance PMID: 23268311 an important biochemical link between the UbS-DDR and BLM-dependent pathways involved in maintaining genome stability. PMID: 23708797 Nonsense mutation p.Q548X in BLM protein is associated with breast cancer in Slavic populations. PMID: 23225144 BLM depletion compromises replication fork recovery and leads to extensive delay of cell division after hydroxyurea-induced stalling. PMID: 23253856 Eighteen polymorphisms in four DNA repair genes were genotyped in 789 age related cataract patients and 531 normal controls from the Jiangsu Eye Study. PMID: 23322570 27 BLM alleles that are not currently known to be associated with Bloom syndrome, are identified. PMID: 23129629 Depleting BLM increased the mutation frequency at telomeres and at the MS32 minisatellite, which is a marker of Alternative Lengthening of Telomeres. PMID: 22989712 we identified faults in two genes, Fanconi C and Bloom helicase( FANCC and BLM), in six families. Faults in these genes appear to increase the risk of developing breast cancer PMID: 23028338

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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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