Analytical Data
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Gene name
BLM
- Application
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Alternative Names
BLM;RECQ2;RECQL3;RecQ-like DNA helicase BLM
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P54132
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Expression Region
877-1024aa
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AA Sequence
DCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWINQDGCQVICATIAFGMGIDKPDVRFVIHASLPKSVEGYYQESGRAGRDGEISHCLLFYTYHDVTRLKRLIMMEKDGNHHTRETHFNNLY
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Molecular Weight
23.0 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The study of BLM (Bloom syndrome helicase) recombinant proteins has garnered significant interest due to the pivotal role that BLM plays in maintaining genomic stability and preventing cancer. BLM is a member of the RecQ helicase family and is crucial for DNA replication, repair, and homologous recombination. Mutations in the BLM gene lead to Bloom syndrome, a rare genetic disorder characterized by growth deficiencies, immunodeficiency, and a markedly increased risk of various cancers. Understanding the biochemical properties and functional mechanisms of BLM through recombinant protein studies allows researchers to elucidate its specific roles in DNA metabolism and repair pathways. By producing recombinant BLM proteins, scientists can investigate their enzymatic activities, interactions with other proteins, and the effects of specific mutations. These studies are essential not only for comprehending the basic cellular processes governed by BLM but also for developing potential therapeutic strategies to tackle disorders linked to genomic instability and cancer. As such, the investigation of BLM recombinant proteins continues to be a rich area of research with important implications for both basic science and clinical applications in oncology and genetics.











