Analytical Data
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Gene name
E-Selectin/CD62E
- Application
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Alternative Names
CD62 antigen-like family member EEndothelial leukocyte adhesion molecule 1 ;ELAM-1Leukocyte-endothelial cell adhesion molecule 2 ;LECAM2;; CD62E
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Species
Pig
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P98110
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Expression Region
23-429aa
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Molecular Weight
44.4 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
E-Selectin, also known as CD62E, is a cell adhesion molecule predominantly expressed on activated endothelial cells. It plays a crucial role in the inflammatory response by mediating the tethering and rolling of leukocytes on the endothelium during the early stages of immune response. E-Selectin binds to specific carbohydrate ligands on leukocytes, facilitating their migration from the bloodstream to sites of inflammation or injury. Given its significant role in various pathological conditions, including atherosclerosis, chronic inflammatory diseases, and cancer metastasis, E-Selectin has become a target for therapeutic interventions. The study of E-Selectin at the molecular level, particularly through the development of recombinant protein forms, allows for a better understanding of its structure-function relationships and interaction dynamics with ligands. This research can pave the way for novel anti-inflammatory therapies and drug delivery systems that can selectively target activated endothelial cells, thereby enhancing treatment efficacy while minimizing side effects. The generation and characterization of E-Selectin/CD62E recombinant proteins enable detailed investigations into its role in immune responses, and potential applications in diagnostic and therapeutic settings are being explored as researchers aim to translate these findings into clinical applications.
