Recombinant Rat Dipeptidyl peptidase 4(Dpp4),partial
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| Amount : | 100 µg |
| Purification : | Greater than 90% as determined by SDS-PAGE. |
| Content : | Tris-based buffer50% glycerol |
| Storage condition : | The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C,-80°C. The shelf life of lyophilized form is 12 months at -20°C,-80°C. Notes:Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
| AA sequence : | Expression Region:638-767aa ; N-terminal 6xHis-SUMO-tagged; SMVLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPEDNLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQISKALVDAGVDFQAMWYTDEDHGIASSTAHQHIYSHMSHFLQQCFSLR |
| Uniprot ID : | P14740 |
| Alternative Name : | Bile canaliculus domain-specific membrane glycoprotein Dipeptidyl peptidase IV Short name: DPP IV GP110 glycoprotein T-cell activation antigen CD26 CD_antigen: CD26 Cleaved into the following 3 chains: Dipeptidyl peptidase 4 membrane form Alternative name(s): Dipeptidyl peptidase IV membrane form Dipeptidyl peptidase 4 soluble form Alternative name(s): Dipeptidyl peptidase IV soluble form Dipeptidyl peptidase 4 60KDA soluble form Alternative name(s): Dipeptidyl peptidase IV 60KDA soluble form |
Source : E.coli ; Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor,CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the Extracellular domain matrix (ECM), the migration and invasion of endothelial cells into the ECM. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. Acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation, including many chemokines, mitogenic growth factors, neuropeptides and peptide hormones. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
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