Analytical Data
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Gene name
hlgB
- Application
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Alternative Names
hlgB；RNF45；E3 ubiquitin-Protein ligase AMFR
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Species
E.coli
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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
P0A075
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Expression Region
26-325aa
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AA Sequence
AEGKITPVSVKKVDDKVTLYKTTATADSDKFKISQILTFNFIKDKSYDKD TLVLKATGNINSGFVKPNPNDYDFSKLYWGAKYNVSISSQSNDSVNVVDY APKNQNEEFQVQNTLGYTFGGDISISNGLSGGLNGNTAFSETINYKQESY RTTLSRNTNYKNVGWGVEAHKIMNNGWGPYGRDSFHPTYGNELFLAGRQS SAYAGQNFIAQHQMPLLSRSNFNPEFLSVLSHRQDGAKKSKITVTYQREM DLYQIRWNGFYWAGANYKNFKTRTFKSTYEIDWENHKVKLLDTKETENNK
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Molecular Weight
38 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 hlgB gene, found in various bacteria, encodes a protein that plays a crucial role in the synthesis of heme-like compounds and the metabolism of reactive oxygen species. Understanding the functions and mechanisms of hlgB is vital due to its implications in bacterial pathogenesis and survival. Previous studies have shown that hlgB is involved in the production of virulence factors, influencing the pathogenicity of certain bacterial strains. Additionally, proteins encoded by hlgB can contribute to antibiotic resistance, making them significant targets for therapeutic intervention. Recent advancements in recombinant protein expression techniques have facilitated the production of HlgB in heterologous systems, enabling detailed structural and functional analyses. These studies aim to elucidate the biochemical pathways associated with HlgB, providing insights into its role in microbial physiology and potential applications in biotechnology and medicine. In summary, research on hlgB recombinant proteins not only enhances our understanding of bacterial biology but also offers promising avenues for the development of new antimicrobial agents.
