Analytical Data
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Gene name
Bb
- Application
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Alternative Names
Bb；EIF2BB；Translation initiation factor eIF2B subunit beta
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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
P49770
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Expression Region
1-351aa
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AA Sequence
MPGSAAKGSELSERIESFVETLKRGGGPRSSEEMARETLGLLRQIITDHRWSNAGELMELIRREGRRMTAAQPSETTVGNMVRRVLKIIREEYGRLHGRSDESDQQESLHKLLTSGGLNEDFSFHYAQLQSNIIEAINELLVELEGTMENIAAQALEHIHSNEVIMTIGFSRTVEAFLKEAARKRKFHVIVAECAPFCQGHEMAVNLSKAGIETTVMTDAAIFAVMSRVNKVIIGTKTILANGALRAVTGTHTLALAAKHHSTPLIVCAPMFKLSPQFPNEEDSFHKFVAPEEVLPFTEGDILEKVSVHCPVFDYVPPELITLFISNIGGNAPSYIYRLMSELYHPDDHVL
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Molecular Weight
66.0 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 research background of Bb recombinant proteins primarily revolves around the exploration of their potential applications in biotechnology and medicine. Bb, derived from the pathogenic bacterium *Borrelia burgdorferi*, is known to cause Lyme disease, a tick-borne illness affecting millions worldwide. Understanding the structure and function of Bb proteins is crucial for developing diagnostic tools, vaccines, and therapeutic strategies against this disease. Recombinant protein technology allows for the expression of Bb proteins in host systems, facilitating the study of their immunogenic properties and biological interactions. The ability to produce these proteins in a controlled manner enables researchers to investigate their roles in the immune response and identify potential targets for drug development. Additionally, advances in genetic engineering and protein purification techniques have significantly enhanced the efficiency and yield of Bb recombinant proteins, making it feasible to conduct large-scale studies. This research is vital not only for combating Lyme disease but also for gaining insights into similar vector-borne diseases, thereby contributing to broader public health initiatives. The ongoing exploration of Bb recombinant proteins is a promising frontier in infectious disease research, with the potential to improve diagnostics and treatment options for Lyme disease and potentially other related illnesses.
