Analytical Data
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Gene name
dltA
- Application
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Alternative Names
dltA；D-alanine--D-alanyl carrier Protein ligase
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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
P10515
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Expression Region
93-640aa
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AA Sequence
KVPLPSLSPTMQAGTIARWEKKEGDKINEGDLIAEVETDKATVGFESLEECYMAKILVAEGTRDVPIGAIICITVGKPEDIEAFKNYTLDSSAAPTPQAAPAPTPAATASPPTPSAQAPGSSYPPHMQVLLPALSPTMTMGTVQRWEKKVGEKLSEGDLLAEIETDKATIGFEVQEEGYLAKILVPEGTRDVPLGTPLCIIVEKEADISAFADYRPTEVTDLKPQVPPPTPPPVAAVPPTPQPLAPTPSAPCPATPAGPKGRVFVSPLAKKLAVEKGIDLTQVKGTGPDGRITKKDIDSFVPSKVAPAPAAVVPPTGPGMAPVPTGVFTDIPISNIRRVIAQRLMQSKQTIPHYYLSIDVNMGEVLLVRKELNKILEGRSKISVNDFIIKASALACLKVPEANSSWMDTVIRQNHVVDVSVAVSTPAGLITPIVFNAHIKGVETIANDVVSLATKAREGKLQPHEFQGGTFTISNLGMFGIKNFSAIINPPQACILAIGASEDKLVPADNEKGFDVASMMSVTLSCDHRVVDGAVGAQWLAEFRKYLE
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Molecular Weight
62.2 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
The DltA protein, a significant component of the d-alanylation pathway, plays a crucial role in bacterial cell wall biosynthesis by transferring d-alanine to teichoic acids, which are critical for maintaining cell wall stability and integrity. This modification impacts the surface charge and overall structure of the bacterial cell wall, influencing interactions with host immune systems and antibiotic susceptibility. Research on DltA has gained prominence due to its potential implications in understanding bacterial resistance mechanisms and virulence. In gram-positive bacteria, the d-alanylation process is pivotal for the viability and pathogenicity of strains such as Staphylococcus aureus and Streptococcus pneumoniae. The examination of DltA has also prompted investigations into its structural and functional properties, enabling insights into its enzymatic mechanisms. Given the rising concerns regarding antibiotic resistance, targeting the biosynthetic pathways involving DltA could present a novel strategy for developing new antimicrobial therapies. As such, the study of DltA and its recombinant forms could provide valuable information for both basic research and therapeutic applications, further underlining its significance in microbiology and infectious disease research.
