Products
DPP4 antibody
- Product Name
- DPP4 antibody
- Catalogue No.
- FNab02520
- Size
- 100μg
- Form
- liquid
- Purification
- Immunogen affinity purified
- Purity
- ≥95% as determined by SDS-PAGE
- Clonality
- polyclonal
- Isotype
- IgG
- Storage
- PBS with 0.02% sodium azide and 50% glycerol pH 7.3, -20℃ for 12 months(Avoid repeated freeze / thaw cycles.)
Immunogen
- Immunogen
- dipeptidyl-peptidase 4
- Alternative Names
- ADABP antibody, ADCP 2 antibody, ADCP2 antibody, CD26 antibody, dipeptidyl peptidase 4 antibody, Dipeptidyl peptidase IV antibody, DPP IV antibody, DPP4 antibody, DPPIV antibody, T cell activation antigen CD26 antibody, TP103 antibody
- UniProt ID
- P27487
- Observed MW
- 110 kDa
Application
- Tested Applications
- ELISA, WB, IHC, IF
- Recommended dilution
- WB: 1:500-1:1000; IHC: 1:20-1:200; IF: 1:10-1:100
Validated Images
U-937 cells were subjected to SDS PAGE followed by western blot with FNab02520(DPP4 antibody) at dilution of 1:500
Immunohistochemistry of paraffin-embedded human prostate cancer using FNab02520(DPP4 antibody) at dilution of 1:100
- Background
- 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 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.
