Analytical Data
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Gene name
PBLD
- Application
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Alternative Names
PBLD;MAWBP;Phenazine biosynthesis-like domain-containing Protein
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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
P30039
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Expression Region
1-288aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMKLPIFIADAFTARAFRGNPAAVCLLENEL DEDMHQKIAREMNLSETAFIRKLHPTDNFAQSSCFGLRWFTPASEVPLCG HATLASAAVLFHKIKNMNSTLTFVTLSGELRARRAEDGIVLDLPLYPAHP QDFHEVEDLIKTAIGNTLVQDICYSPDTQKLLVRLSDVYNRSFLENLKVN TENLLQVENTGKVKGLILTLKGEPGGQTQAFDFYSRYFAPWVGVAEDPVT GSAHAVLSSYWSQHLGKKEMHAFQCSHRGGELGISLRPDGRVDIRGGAAV VLEGTLTA
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Molecular Weight
34 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
PBLD (Protein-Binding Lipocalin Domain) is an intriguing protein that has garnered significant attention due to its diverse biological roles and potential implications in various diseases. Discovered in the context of kidney health, PBLD is implicated in the transport and binding of small hydrophobic molecules, such as fatty acids and hormones, thereby influencing metabolic and physiological processes. With its lipocalin structure, PBLD exhibits unique features that allow it to interact with multiple ligands, making it a critical player in lipid metabolism and signaling pathways. Research has indicated that dysregulation of PBLD may contribute to pathological conditions, including obesity, diabetes, and cardiovascular diseases. Recent studies employing molecular biology techniques have aimed to elucidate the precise mechanisms by which PBLD operates within cellular environments, providing insights into its functional roles and potential therapeutic applications. Understanding the nuances of PBLD activity and its interactions with various biomolecules could pave the way for novel strategies in disease prevention and management, highlighting the importance of ongoing research in this promising area of protein science.
