Analytical Data
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Gene name
BMF
- Application
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Alternative Names
Bcl 2 modifying factor; Bcl-2-modifying factor; Bcl2 modifying factor; Bmf; BMF_HUMAN; FLJ00065
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96LC9
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Expression Region
1-184aa
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Molecular Weight
47.5 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
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Protein Description
Alpha 1-Microglobulin (A1M) is a protein that has gained attention due to its potential roles in various physiological and pathological processes. It is primarily produced in the liver and has been implicated in antioxidant defense, immune modulation, and tissue protection. Research has revealed that A1M acts as a scavenger of free radicals and can bind to heme, thereby preventing oxidative damage in tissues. Its involvement in renal and cardiovascular diseases, as well as its potential as a biomarker for inflammation, has sparked considerable interest in this protein. Recombinant human A1M has been engineered to explore its therapeutic potential, particularly in diseases characterized by oxidative stress and inflammation. As a result, studies focusing on the production, purification, and functional characterization of recombinant A1M have emerged, aiming to unlock its possible applications in regenerative medicine and drug development. Furthermore, understanding the molecular mechanisms governing A1M's protective functions could pave the way for novel therapeutic strategies against oxidative stress-related disorders. Overall, the exploration of recombinant A1M represents a promising avenue for therapeutic intervention and underscores the significance of this protein in health and disease.
