Analytical Data
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Gene name
CD162/PSGL-1
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简介
CD162/PSGL-1 Protein is a sialomucin expressed on leukocytes, which through high affinity, calcium-dependent interactions with E- and P-selectins, mediates rapid rolling of leukocytes over vascular surfaces during the initial steps in inflammation[1]. CD162/PSGL-1 Protein, Human (HEK293, mFc) is the recombinant human-derived CD162/PSGL-1 protein, expressed by HEK293 , with C-mFc labeled tag.
- Application
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Alternative Names
P-selectin glycoprotein ligand 1; PSGL-1; Selectin P ligand; CD162; SELPLG
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Species
Human
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Source
HEK293
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Tag
C-mFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
AAC50061.1
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Expression Region
L18-V295
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Protein Length
Partial
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Molecular Weight
55.4 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
CD162, also known as P-selectin glycoprotein ligand-1 (PSGL-1), is a key adhesion molecule predominantly expressed on leukocytes, playing a crucial role in the regulation of immune responses and inflammation. The interaction between CD162 on leukocytes and P-selectin on activated endothelial cells is essential for the adhesion and rolling of leukocytes, facilitating their migration to sites of injury or infection. Research into CD162/PSGL-1 has gained significant attention due to its implications in various pathological conditions, including autoimmune diseases, chronic inflammation, and cancer metastasis. Understanding the structural and functional aspects of this molecule could provide insights into therapeutic targets for modulating immune responses. Recombinant CD162/PSGL-1 proteins have been developed to study these interactions in vitro, enabling investigations into their role in leukocyte trafficking and functional assays. By using these recombinant proteins, researchers can explore the signaling pathways activated upon CD162 engagement, assess the effects of mutations or post-translational modifications, and evaluate potential inhibitors that may disrupt the CD162-P-selectin interaction, which is a promising strategy for developing novel anti-inflammatory therapies. Thus, the study of CD162/PSGL-1 not only enhances our understanding of cellular adhesion mechanisms but also opens avenues for targeted immunotherapy in various diseases characterized by dysregulated immune responses.
