Sf9, Insect cells.
Nectin-2, Herpes virus entry mediator B, Herpesvirus entry mediator B, HveB, Nectin cell adhesion molecule 2, Poliovirus receptor-related protein 2, CD112, HVEB, PRR2, PVRL2.
Greater than 90.0% as determined by SDS-PAGE.
NECTIN2 Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 337 amino acids (32-360a.a.) and having a molecular mass of 36.3kDa (Molecular size on SDS-PAGE will appear at approximately 40-57kDa).
NECTIN2 is expressed with an 8 amino acids His tag at C-Terminus and purified by proprietary chromatographic techniques.
Nectin-2, Herpes virus entry mediator B, Herpesvirus entry mediator B, HveB, Nectin cell adhesion molecule 2, Poliovirus receptor-related protein 2, CD112, HVEB, PRR2, PVRL2.
Sf9, Insect cells.
QDVRVQVLPE VRGQLGGTVE LPCHLLPPVP GLYISLVTWQ RPDAPANHQN VAAFHPKMGP SFPSPKPGSE RLSFVSAKQS TGQDTEAELQ DATLALHGLT VEDEGNYTCE FATFPKGSVR GMTWLRVIAK PKNQAEAQKV TFSQDPTTVA LCISKEGRPP ARISWLSSLD WEAKETQVSG TLAGTVTVTS RFTLVPSGRA DGVTVTCKVE HESFEEPALI PVTLSVRYPP EVSISGYDDN WYLGRTDATL SCDVRSNPEP TGYDWSTTSG TFPTSAVAQG SQLVIHAVDS LFNTTFVCTV TNAVGMGRAE QVIFVRETPN TAGAGATGGL EHHHHHH.
Nectin Cell Adhesion Molecule 2 (Nectin-2), also known as CD112, is a single-pass type I membrane glycoprotein that plays a crucial role in cell-cell adhesion. It is a member of the nectin family, which includes four members: Nectin-1, Nectin-2, Nectin-3, and Nectin-4. Nectin-2 is involved in the formation of adherens junctions, which are essential for maintaining the structural integrity of tissues .
The preparation of human recombinant Nectin-2 involves several steps. Initially, the gene encoding Nectin-2 is cloned into an appropriate expression vector. This vector is then introduced into a host cell line, such as HEK293 or CHO cells, which are commonly used for protein expression. The host cells are cultured under optimal conditions to promote the expression of Nectin-2. Once the protein is expressed, it is purified using affinity chromatography, which exploits the specific binding properties of Nectin-2 to isolate it from other cellular components. The final purification step often involves gel filtration chromatography to achieve high purity .
Nectin-2 forms homo-cis dimers on the cell surface via its Ig2-domain. These dimers can interact in a heterophilic or homophilic manner with other nectins or nectin-like molecules. The interaction between Nectin-2 and DNAM-1 (CD226) is particularly significant in immune regulation. The binding of DNAM-1 to Nectin-2 can either stimulate or inhibit T-cell proliferation and cytokine production, depending on the receptor it binds to . Mutational analysis has shown that disruption of the homodimeric interface of Nectin-2 leads to a failure of homodimer formation and loss of binding to DNAM-1 .