Analytical Data
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Gene name
BSA
- Application
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Alternative Names
BSA；BAT5；G5；NG26；Phosphatidylserine lipase ABHD16A
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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
O95870
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Expression Region
1-558aa
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AA Sequence
MAKLLSCVLGPRLYKIYRERDSERAPASVPETPTAVTAPHSSSWDTYYQPRALEKHADSILALASVFWSISYYSSPFAFFYLYRKGYLSLSKVVPFSHYAGTLLLLLAGVACLRGIGRWTNPQYRQFITILEATHRNQSSENKRQLANYNFDFRSWPVDFHWEEPSSRKESRGGPSRRGVALLRPEPLHRGTADTLLNRVKKLPCQITSYLVAHTLGRRMLYPGSVYLLQKALMPVLLQGQARLVEECNGRRAKLLACDGNEIDTMFVDRRGTAEPQGQKLVICCEGNAGFYEVGCVSTPLEAGYSVLGWNHPGFAGSTGVPFPQNEANAMDVVVQFAIHRLGFQPQDIIIYAWSIGGFTATWAAMSYPDVSAMILDASFDDLVPLALKVMPDSWRGLVTRTVRQHLNLNNAEQLCRYQGPVLLIRRTKDEIITTTVPEDIMSNRGNDLLLKLLQHRYPRVMAEEGLRVVRQWLEASSQLEEASIYSRWEVEEDWCLSVLRSYQAEHGPDFPWSVGEDMSADGRRQLALFLARKHLHNFEATHCTPLPAQNFQMPWHL
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Molecular Weight
63.2 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
Bovine serum albumin (BSA) is a widely studied globular protein, primarily derived from the serum of cows, and serves as an essential component in various biochemical and biophysical applications. Its robust stability, solubility, and ability to bind a range of molecules make it an ideal standard protein in laboratory research. Research on recombinant BSA has gained momentum due to the ethical and economic concerns surrounding the use of animal-derived products, as well as the need for consistent quality and supply in scientific experiments. Recombinant techniques enable the production of BSA with specific modifications, enhancing its functionality and broadening its applications in areas such as drug delivery, biochemical assays, and vaccine development. Furthermore, recombinant BSA can be produced in controlled environments, minimizing the risk of contamination and variability associated with natural sources. This advancement in recombinant protein technology not only addresses safety and reliability issues but also allows researchers to explore the protein's structural and functional properties in greater detail. As a result, ongoing studies focus on optimizing production methods, characterizing the molecular properties of recombinant BSA, and investigating its potential therapeutic uses, highlighting its significance in both basic and applied research.
