Analytical Data
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Gene name
UPP1
- Application
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Alternative Names
UDRPASE; UP; UPASE
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q16831
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Expression Region
Asn45~Tyr235
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Molecular Weight
25kDa
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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
Surfactant Protein D (SP-D) is a member of the collectin family of proteins, which play a critical role in the innate immune response, particularly in the lung and alveolar spaces. SP-D is involved in surfactant homeostasis, modulation of inflammation, and pathogen recognition, making it crucial for respiratory health. Research on SP-D has intensified due to its potential implications in various pulmonary diseases, including asthma, chronic obstructive pulmonary disease (COPD), and pulmonary infections. The study of recombinant SP-D (rSP-D) involves the production of this protein using recombinant DNA technology, allowing for detailed examination of its structure-function relationships, immunological properties, and therapeutic potentials. Recent advances in recombinant protein expression systems have facilitated the production of rSP-D, enabling researchers to investigate its ability to enhance pathogen clearance, regulate immune responses, and restore lung function in disease models. Given the increasing burden of respiratory diseases worldwide, understanding the biological functions of SP-D and the therapeutic applications of rSP-D holds promise for innovative strategies in treating lung disorders and improving patient outcomes.
