Analytical Data
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Gene name
SELPLG
- Application
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Alternative Names
SELPLG;P-selectin glycoProtein ligand 1
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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
SELPLG (selectin P ligand) is a glycoprotein that plays a crucial role in the adhesion of leukocytes to the endothelial cells during inflammation and immune response. Its primary function involves binding to selectins, which are specialized proteins expressed on the surface of activated endothelial cells, aiding in the rolling and migration of white blood cells to sites of injury or infection. Research on SELPLG has gained considerable attention due to its potential implications in various pathological conditions, including autoimmune diseases, cancer metastasis, and cardiovascular disorders. Understanding the structural and functional properties of SELPLG, particularly its interactions with selectins, is vital for developing therapeutic strategies aimed at modulating immune responses. The recombinant production of SELPLG provides a valuable tool for studying its biological functions, elucidating the mechanisms of leukocyte trafficking, and exploring its potential as a biomarker or therapeutic target. Moreover, advancements in protein engineering and expression systems facilitate the generation of SELPLG variants with enhanced functionalities, paving the way for innovative treatments in inflammatory and immune-related diseases.











