Analytical Data
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Gene name
bHB
- Application
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Alternative Names
bHB；BHLHB2；DEC1；SHARP2；Class E basic helix-loop-helix Protein 40
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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
O14503
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Expression Region
1-412aa
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AA Sequence
MERIPSAQPPPACLPKAPGLEHGDLPGMYPAHMYQVYKSRRGIKRSEDSKETYKLPHRLIEKKRRDRINECIAQLKDLLPEHLKLTTLGHLEKAVVLELTLKHVKALTNLIDQQQQKIIALQSGLQAGELSGRNVETGQEMFCSGFQTCAREVLQYLAKHENTRDLKSSQLVTHLHRVVSELLQGGTSRKPSDPAPKVMDFKEKPSSPAKGSEGPGKNCVPVIQRTFAHSSGEQSGSDTDTDSGYGGESEKGDLRSEQPCFKSDHGRRFTMGERIGAIKQESEEPPTKKNRMQLSDDEGHFTSSDLISSPFLGPHPHQPPFCLPFYLIPPSATAYLPMLEKCWYPTSVPVLYPGLNASAAALSSFMNPDKISAPLLMPQRLPSPLPAHPSVDSSVLLQALKPIPPLNLETKD
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Molecular Weight
45.5 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
The study of bHB (bovine Hemoglobin Binding) recombinant proteins has gained significant attention in the field of biochemistry and molecular biology due to their potential applications in various industries. Bovine hemoglobin, derived from cattle, serves as a model for understanding the structure and function of hemoproteins, which are crucial for oxygen transport and storage in living organisms. Recombinant technology enables the production of modified hemoglobin with specific characteristics, facilitating the exploration of its functionality and interaction with other biomolecules. Research has shown that bHB recombinant proteins can improve oxygen delivery in therapeutic applications, enhance the performance of biopharmaceuticals, and serve as effective agents in various biochemical assays. Additionally, the ability to manipulate bHB at the genetic level allows scientists to investigate the effects of specific mutations on protein stability and activity. The growing interest in sustainable alternatives for blood substitutes also propels research into bHB, as it presents a potential solution for addressing blood shortages and transfusion-related complications. Overall, the investigation of bHB recombinant proteins is essential for advancing our understanding of hemoglobin function, developing innovative biomedical applications, and contributing to the field of synthetic biology.
