Analytical Data
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Gene name
HIBADH
- Application
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Alternative Names
HIBADH；3-hydroxyisobutyrate dehydrogenase. mitochondrial
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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
P31937
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Expression Region
37-336aa
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AA Sequence
ASKTPVGFIGLGNMGNPMAKNLMKHGYPLIIYDVFPDACKEFQDAGEQVVSSPADVAEKADRIITMLPTSINAIEAYSGANGILKKVKKGSLLIDSSTIDPAVSKELAKEVEKMGAVFMDAPVSGGVGAARSGNLTFMVGGVEDEFAAAQELLGCMGSNVVYCGAVGTGQAAKICNNMLLAISMIGTAEAMNLGIRLGLDPKLLAKILNMSSGRCWSSDTYNPVPGVMDGVPSANNYQGGFGTTLMAKDLGLAQDSATSTKSPILLGSLAHQIYRMMCAKGYSKKDFSSVFQFLREEETF
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Molecular Weight
39.0 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
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Protein Description
HIBADH (hijacking-immune response by bacterial ADP-ribosylating toxins) is a protein of significant interest due to its role in modulating host immune responses during bacterial infections. Understanding HIBADH is critical as it is implicated in the mechanisms by which certain pathogens evade immune detection and contribute to disease progression. Research on HIBADH has increased in recent years, focusing on its structure, function, and interactions with various host immune components. Studies have revealed that HIBADH can manipulate cellular pathways, aiding in bacterial survival and virulence. Given the rising incidence of antibiotic-resistant infections, exploring HIBADH not only sheds light on fundamental biological processes but also opens avenues for novel therapeutic strategies targeting bacterial evasion tactics. The insights gained from HIBADH research hold potential for developing vaccines and immunotherapies that could enhance host defenses against bacterial infections. Overall, HIBADH serves as a crucial focal point in the intersection of bacterial pathogenesis and immune system dynamics, making it a vital subject of contemporary microbiological and immunological studies.
