Analytical Data
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Gene name
PGRP-SC2
- Application
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Alternative Names
PGRP-SC2；Peptidoglycan-recognition Protein SC2
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Species
E.coli
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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
Q9V4X2
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Expression Region
21-184aa
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AA Sequence
VTIISKSEWGGRSATSKTSLANYLSYAVIHHTAGNYCSTKAACITQLQNIQAYHMDSLGWADIGYNFLIGGDGNVYEGRGWNVMGAHATNWNSKSIGISFLGNYNTNTLTSAQITAAKGLLSDAVSRGQIVSGYILYGHRQVGSTECPGTNIWNEIRTWSNWKA
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Molecular Weight
25.2 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
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Protein Description
PGRP-SC2 (Peptidoglycan Recognition Protein-SC2) is a crucial component of the innate immune system in various organisms, particularly in insects such as Drosophila melanogaster. These proteins are known for their role in detecting peptidoglycan, a major component of bacterial cell walls, thereby serving as essential players in the host's defense mechanism against bacterial infections. Research into PGRP-SC2 has grown in importance as scientists seek to understand its structural characteristics, binding affinities, and mechanism of action in immune signaling pathways. Previous studies have shown that PGRP-SC2 not only recognizes and binds to bacterial cell wall components but also plays a significant role in modulating immune responses, influencing the activity of immune cells, and regulating the production of antimicrobial peptides. Furthermore, the versatility of PGRP-SC2 extends to its ability to interact with other immune-modulating proteins, indicating a complex network of interactions that are pivotal for maintaining immune homeostasis. With the rise of antibiotic resistance and the re-emergence of bacterial infections, investigating the functional properties of PGRP-SC2 could provide insights into novel therapeutic strategies and enhance our understanding of innate immunity. Thus, research on recombinant PGRP-SC2 proteins not only sheds light on fundamental immunological processes but also holds potential for applications in biotechnology and medicine.
