Sf9, Baculovirus cells.
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E
Sterile filtered colorless solution.
Greater than 95.0% as determined by SDS-PAGE.
SELE Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 541 amino acids (22-556 a.a) and having a molecular mass of 59.4kDa.
SELE is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
E-selectin, also known as SELE, is a cell adhesion molecule found on endothelial cells. It plays a crucial role in the inflammatory response by facilitating the binding of leukocytes and platelets to the endothelium. This protein is a glycoprotein that binds to carbohydrates in a calcium-dependent manner. The human E-selectin gene is located on chromosome 1 and consists of 14 exons.
This recombinant SELE protein is produced in Sf9 insect cells using a baculovirus expression system. It is a single polypeptide chain with a molecular weight of 59.4 kDa. The protein sequence includes amino acids 22 to 556 of the human SELE protein, with a 6-amino acid His-tag added to the C-terminus to facilitate purification. The protein is purified using proprietary chromatographic techniques and is glycosylated, meaning it has sugar molecules attached.
The product is a colorless solution that has been sterilized by filtration.
This SELE protein is supplied in a solution containing 0.5 mg/ml SELE, Phosphate-Buffered Saline (pH 7.4), and 10% glycerol.
For short-term storage (up to 4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to store the product frozen at -20°C. To ensure stability during long-term storage, adding a carrier protein such as HSA or BSA (0.1%) is recommended. Repeated freezing and thawing of the product should be avoided.
The purity of this SELE protein is greater than 95% as determined by SDS-PAGE analysis.
The biological activity of this SELE protein is measured by its ability to support the adhesion of U937 cells (a human histiocytic lymphoma cell line) to a surface coated with the protein. When used at a concentration of 2 µg/ml, the immobilized SELE protein promotes U937 cell adhesion by more than 40%.
E-selectin, Endothelial leukocyte adhesion molecule 1, ELAM-1, Leukocyte-endothelial cell adhesion molecule 2, LECAM2, CD62E antigen, SELE, ELAM1, ELAM, ESEL, CD62E
Sf9, Baculovirus cells.
WSYNTSTEAM TYDEASAYCQ QRYTHLVAIQ NKEEIEYLNS ILSYSPSYYW IGIRKVNNVW VWVGTQKPLT EEAKNWAPGE PNNRQKDEDC VEIYIKREKD VGMWNDERCS KKKLALCYTA ACTNTSCSGH GECVETINNY TCKCDPGFSG LKCEQIVNCT ALESPEHGSL VCSHPLGNFS YNSSCSISCD RGYLPSSMET MQCMSSGEWS APIPACNVVE CDAVTNPANG FVECFQNPGS FPWNTTCTFD CEEGFELMGA QSLQCTSSGN WDNEKPTCKA VTCRAVRQPQ NGSVRCSHSP AGEFTFKSSC NFTCEEGFML QGPAQVECTT QGQWTQQIPV CEAFQCTALS NPERGYMNCL PSASGSFRYG SSCEFSCEQG FVLKGSKRLQ CGPTGEWDNE KPTCEAVRCD AVHQPPKGLV RCAHSPIGEF TYKSSCAFSC EEGFELHGST QLECTSQGQW TEEVPSCQVV KCSSLAVPGK INMSCSGEPV FGTVCKFACP EGWTLNGSAA RTCGATGHWS GLLPTCEAPT ESNIPHHHHH H
E-Selectin is a member of the selectin family of cell adhesion molecules, which also includes P-Selectin and L-Selectin. These molecules are characterized by their calcium-dependent binding to specific carbohydrate ligands on the surfaces of leukocytes. E-Selectin is a heavily glycosylated transmembrane protein expressed by activated endothelial cells in microvascular linings .
The structure of E-Selectin includes:
Recombinant human E-Selectin, produced in Sf9 insect cells, is a 58.6 kDa protein containing 535 amino acid residues, corresponding to the extracellular portion of the full-length protein. Due to glycosylation, E-Selectin migrates at an apparent molecular weight of approximately 65-85 kDa by SDS-PAGE analysis under reducing conditions .
E-Selectin is primarily involved in the initial steps of leukocyte recruitment during inflammation. It mediates the rolling of leukocytes on the endothelial surface, a critical step that precedes firm adhesion and transmigration into tissues. This interaction is facilitated by the binding of E-Selectin to specific carbohydrate determinants on leukocytes, such as sialyl-Lewisx.
The recombinant form of E-Selectin is produced using the baculovirus expression system in Sf9 insect cells. This system is advantageous for producing glycosylated proteins that are similar to their native forms. The recombinant E-Selectin is purified to a high degree of purity, typically greater than 95% as determined by SDS-PAGE and HPLC analyses .
Recombinant human E-Selectin is widely used in research to study the mechanisms of leukocyte adhesion and migration. It is also used in assays to measure the adhesion of leukocytes to endothelial cells, which can provide insights into inflammatory processes and potential therapeutic targets for inflammatory diseases.