Recombinant Mouse Bloom Syndrome Protein Homolog (BLM) Protein (His&MYC)

Beta LifeScience SKU/CAT #: BLC-02782P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Mouse Bloom Syndrome Protein Homolog (BLM) Protein (His&MYC)

Beta LifeScience SKU/CAT #: BLC-02782P
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Product Overview

Description Recombinant Mouse Bloom Syndrome Protein Homolog (BLM) Protein (His&MYC) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb O88700
Target Symbol BLM
Synonyms BlmBloom syndrome protein homolog; mBLM; EC 3.6.4.12; RecQ helicase homolog
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-10His&C-MYC
Target Protein Sequence INAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTIVISPLRSLIVDQVQKLTSFDIPATYLTGDKTDSEAANIYLQLSKKDPIIKLLYVTPEKVCASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQ
Expression Range 684-859aa
Protein Length Partial
Mol. Weight 24.7kDa
Research Area Neuroscience
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 KHDC3-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.
Protein Families Helicase family, RecQ subfamily
Database References

KEGG: mmu:12144

STRING: 10090.ENSMUSP00000127995

UniGene: PMID: 29348659

  • 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
  • BLM helicase facilites telomere replication by resolving G4 structures formed during copying of the G-rich strand by leading strand synthesis. PMID: 26195664
  • Data suggest that BLM suppresses homologous recombination, while full-length BRCA1 promotes this process. PMID: 21709021
  • Although interhomolog recombination is slightly decreased in the absence of BLM, loss of heterozygosity is increased by fivefold or more, implying significantly increased interhomolog crossing over. PMID: 21730139
  • Blm has roles both upstream and downstream of the Rad54 protein, a core HR factor. Disruption of Rad54 in the Blm-mutant background reduced the elevated level of gene targeting and of sister chromatid exchanges. PMID: 20531307
  • the characterization of Hprt mutations in vivo in Blm hypomorphic mice PMID: 20299287
  • there was no dramatic qualititative difference in the basal cell carcionoma or rhabdomyosarcoma tumors associated with the mutant Blm genotype PMID: 19995795
  • Data show that BLM-deficient mouse and human cells suppress homeologous recombination to a similar extent as wild-type cells. PMID: 20154148
  • observations indicate that Blm is a modifier of tumor formation in the mouse and that Blm haploinsufficiency is associated with tumor predisposition PMID: 12242442
  • Bone marrow cells from mice heterozygous for BLM mutation, BLM(Cin/+), transfected with BCR/ABL display increased sensitivity to cisplatin. PMID: 15750625
  • Blm gene mutation produces this instability, strengthening a role for CIN in the development of human cancer. PMID: 16914751
  • Blm serves a vital role for development, maintenance, and function of T lymphocytes, suggesting a basis for the immune deficiency in Bloom's syndrome. PMID: 17210642
  • BLM, the RecQ DNA helicase mutated in Bloom syndrome, is preferentially modified by SUMO-2/3 both in vitro and in vivo PMID: 18708356
  • A vital role is reported for RecQ family helicase Blm in all major aspects of the B cell life cycle, manifest in disturbed B cell immunity and tumor development in its absence. PMID: 19109166
  • The sister chromatid exchange events stimulated by Tim reduction were largely mediated via a Brca2/Rad51-dependent mechanism and were additively increased by deletion of the Blm helicase. PMID: 19112184
  • 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.

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