Analytical Data
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Gene name
ddl
- Application
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Alternative Names
ddl；FHA domain-containing Protein DDL
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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
P63891
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Expression Region
1-356aa
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AA Sequence
MTKENICIVFGGKSAEHEVSILTAQNVLNAIDKDKYHVDIIYITNDGDWRKQNNITAEIKSTDELHLENGEALEISQLLKESSSGQPYDAVFPLLHGPNGEDGTIQGLFEVLDVPYVGNGVLSAASSMDKLVMKQLFEHRGLPQLPYISFLRSEYEKYEHNILKLVNDKLNYPVFVKPANLGSSVGISKCNNEAELKEGIKEAFQFDRKLVIEQGVNAREIEVAVLGNDYPEATWPGEVVKDVAFYDYKSKYKDGKVQLQIPADLDEDVQLTLRNMALEAFKATDCSGLVRADFFVTEDNQIYINETNAMPGFTAFSMYPKLWENMGLSYPELITKLIELAKERHQDKQKNKYKID
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Molecular Weight
47.7 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
Ddl (D-alanyl-D-alanine ligase) is an essential enzyme involved in the biosynthesis of bacterial cell wall peptidoglycan. It catalyzes the formation of D-alanyl-D-alanine dipeptide, a critical building block for bacterial cell wall structure and integrity. Research on Ddl and its related protein structures has gained significant attention due to the rise of antibiotic-resistant bacteria, which threaten global health. Understanding the mechanisms of Ddl and its enzymatic action could provide insights into novel antibacterial strategies. The study of Ddl's protein structure and function is particularly crucial as it may enable the development of new antibiotic agents targeting this enzyme, offering a promising avenue for overcoming resistance. Furthermore, the structural characterization of Ddl can unveil the intricacies of its catalytic mechanism and provide a framework for designing inhibitors. Advances in techniques such as X-ray crystallography and cryo-electron microscopy have enhanced our understanding of Ddl and its interactions with other cellular components. As the global challenge of antibiotic resistance escalates, concerted research efforts focusing on Ddl and similar enzymes are pivotal for enhancing our arsenal against pathogenic bacteria.
