Analytical Data
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Gene name
PLDN
- Application
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Alternative Names
BLOC1S6;PA;PLDN;Biogenesis of lysosome-related organelles complex 1 subunit 6
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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
Q9UL45
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Expression Region
1-172aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MSVPGPSSPD GALTRPPYCL EAGEPTPGLS DTSPDEGLIE DLTIEDKAVE QLAEGLLSHY LPDLQRSKQA LQELTQNQVV LLDTLEQEIS KFKECHSMLD INALFAEAKH YHAKLVNIRK EMLMLHEKTS KLKKRALKLQ QKRQKEELER EQQREKEFER EKQLTARPAK RM
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Molecular Weight
22 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
PLDN (Pegylated L-asparaginase) is a recombinant enzyme that plays a vital role in the treatment of acute lymphoblastic leukemia (ALL) and other malignancies by targeting and depleting asparagine, an amino acid critical for the growth of asparagine-dependent tumor cells. Traditional forms of L-asparaginase derived from microbial sources are associated with significant immunogenicity and a short half-life, leading to potential therapeutic challenges. To address these limitations, research has focused on the development of PLDN, which is engineered to improve its pharmacokinetic properties through pegylation—an innovative process that involves attaching polyethylene glycol (PEG) chains to the protein. This modification not only enhances the stability and solubility of L-asparaginase but also reduces its immunogenicity and prolongs its circulation time in the bloodstream, thereby allowing for more effective and sustained therapeutic effects. Clinical studies have begun to demonstrate that PLDN can improve patient outcomes with reduced side effects compared to traditional L-asparaginase formulations. Consequently, ongoing research aims to optimize PLDN's formulation and administration protocols while investigating its efficacy in diverse patient populations. The continued exploration of PLDN and other recombinant proteins underscores the importance of biopharmaceutical advancements in providing targeted and individualized cancer therapies.











