Analytical Data
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Gene name
PSGL1
- Application
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Alternative Names
PSGL1；ELAM1；E-selectin
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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
Q14242
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Expression Region
18-320aa
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AA Sequence
MASMTGGQQMGRGHHHHHHENLYFQGGTRLQLWDTWADEAEKALGPLLAR DRRQATEYEYLDYDFLPETEPPEMLRNSTDTTPLTGPGTPESTTVEPAAR RSTGLDAGGAVTELTTELANMGNLSTDSAAMEIQTTQPAATEAQTTQPVP TEAQTTPLAATEAQTTRLTATEAQTTPLAATEAQTTPPAATEAQTTQPTG LEAQTTAPAAMEAQTTAPAAMEAQTTPPAAMEAQTTQTTAMEAQTTAPEA TEAQTTQPTATEAQTTPLAAMEALSTEPSATEALSMEPTTKRGLFIPFSV SSVTHKGIPMAASNLSVNYPVGAPDHISVKQC
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Molecular Weight
35 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
PSGL-1 (P-selectin glycoprotein ligand-1) is a critical adhesion molecule primarily expressed on the surfaces of leukocytes. It plays a pivotal role in the immune response by mediating the interaction between leukocytes and endothelial cells during inflammation, particularly through binding to P-selectin, which is upregulated on activated endothelial cells. Understanding the structure and function of PSGL-1 is vital for unraveling its mechanisms in various pathophysiological conditions, including autoimmune disorders, cardiovascular diseases, and cancer progression. Recent studies have focused on the recombinant expression of PSGL-1 to investigate its molecular interactions and therapeutic potential. By producing recombinant PSGL-1, researchers aim to analyze its binding characteristics, elucidate the signaling pathways it activates, and explore its potential as a target for drug development. The ability to generate large quantities of functional PSGL-1 protein through recombinant techniques facilitates high-throughput studies and may lead to novel therapeutic strategies that leverage this molecule's role in modulating immune responses. This research is particularly relevant in the context of developing interventions to mitigate excessive inflammation or enhance immune responses against tumors. Overall, the study of PSGL-1 recombinant proteins represents a promising avenue for improving our understanding of immune mechanisms and developing innovative treatments for various diseases.
