Human Recombinant DPP4 protein, His Tag (V2LY-0526-LY3632)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant DPP4 protein, His Tag consist of Amino Acid: 34-766 and predicts a molecular mass of 86.3 kDa.
Molecule Mass
86.3 kDa
Verified
HPLC
Sequence
Amino Acid: 34-766
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
≥95% as determined by SDS-PAGE. ≥90% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Dipeptidyl Peptidase 4
Function
Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation (PubMed:10951221, PubMed:10900005, PubMed:11772392, PubMed:17287217).

Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC (PubMed:10951221, PubMed:10900005, PubMed:11772392, PubMed:14691230).

Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner (PubMed:17287217).

Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion (PubMed:11772392).

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 (PubMed:16651416, PubMed:10593948).

May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation (PubMed:18708048).

When overexpressed, enhanced cell proliferation, a process inhibited by GPC3 (PubMed:17549790).

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 such as brain natriuretic peptide 32 (PubMed:16254193, PubMed:10570924).

Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline (PubMed:10593948).

(Microbial infection) Acts as a receptor for human coronavirus MERS-CoV-2.
Biological Process
Behavioral fear response Source: Ensembl
Cell adhesion Source: UniProtKB-KW
Endothelial cell migration Source: UniProtKB
Locomotory exploration behavior Source: Ensembl
Negative regulation of extracellular matrix disassembly Source: UniProtKB
Negative regulation of neutrophil chemotaxis Source: CACAO
Positive regulation of cell population proliferation Source: UniProtKB
Proteolysis Source: CAFA
Psychomotor behavior Source: Ensembl
Regulation of cell-cell adhesion mediated by integrin Source: UniProtKB
Regulation of insulin secretion Source: Reactome
Response to hypoxia Source: UniProtKB
T cell activation Source: UniProtKB
T cell costimulation Source: UniProtKB
Cellular Location
Dipeptidyl peptidase 4 soluble form: Secreted. Detected in the serum and the seminal fluid.
Cell membrane; Apical cell membrane; Invadopodium membrane; Lamellipodium membrane; Cell junction; Membrane raft. Translocated to the apical membrane through the concerted action of N- and O-Glycans and its association with lipid microdomains containing cholesterol and sphingolipids (PubMed:11773049). Redistributed to membrane rafts in T-cell in an interleukin-12-dependent activation (PubMed:12676959). Its interaction with CAV1 is necessary for its translocation to membrane rafts (PubMed:17287217). Colocalized with PTPRC in membrane rafts (PubMed:12676959). Colocalized with FAP in invadopodia and lamellipodia of migratory activated endothelial cells in collagenous matrix. Colocalized with FAP on endothelial cells of capillary-like microvessels but not large vessels within invasive breast ductal carcinoma (PubMed:16651416). Colocalized with ADA at the cell junction in lymphocyte-epithelial cell adhesion (PubMed:11772392). Colocalized with IGF2R in internalized cytoplasmic vesicles adjacent to the cell surface (PubMed:10900005).
Topology
Cytoplasmic: 1-6
Helical: 7-28
Extracellular: 29-766
PTM
The soluble form (Dipeptidyl peptidase 4 soluble form also named SDPP) derives from the membrane form (Dipeptidyl peptidase 4 membrane form also named MDPP) by proteolytic processing.
N- and O-Glycosylated.
Phosphorylated. Mannose 6-phosphate residues in the carbohydrate moiety are necessary for interaction with IGF2R in activated T-cells. Mannose 6-phosphorylation is induced during T-cell activation.

Rakhmat, I. I., Kusmala, Y. Y., Handayani, D. R., Juliastuti, H., Nawangsih, E. N., Wibowo, A., ... & Pranata, R. (2021). Dipeptidyl peptidase-4 (DPP-4) inhibitor and mortality in coronavirus disease 2019 (COVID-19)–a systematic review, meta-analysis, and meta-regression. Diabetes & Metabolic Syndrome: Clinical Research & Reviews, 15(3), 777-782.

Hariyanto, T. I., & Kurniawan, A. (2021). Dipeptidyl peptidase 4 (DPP4) inhibitor and outcome from coronavirus disease 2019 (COVID-19) in diabetic patients: a systematic review, meta-analysis, and meta-regression. Journal of Diabetes & Metabolic Disorders, 20(1), 543-550.

Solerte, S. B., Di Sabatino, A., Galli, M., & Fiorina, P. (2020). Dipeptidyl peptidase-4 (DPP4) inhibition in COVID-19. Acta diabetologica, 57(7), 779-783.

Bassendine, M. F., Bridge, S. H., McCaughan, G. W., & Gorrell, M. D. (2020). COVID‐19 and comorbidities: a role for dipeptidyl peptidase 4 (DPP4) in disease severity?. Journal of diabetes, 12(9), 649-658.

Shao, S., Xu, Q., Yu, X., Pan, R., & Chen, Y. (2020). Dipeptidyl peptidase 4 inhibitors and their potential immune modulatory functions. Pharmacology & therapeutics, 209, 107503.

Gupta, S., & Sen, U. (2019). More than just an enzyme: Dipeptidyl peptidase-4 (DPP-4) and its association with diabetic kidney remodelling. Pharmacological research, 147, 104391.

Wang, X., Zheng, P., Huang, G., Yang, L., & Zhou, Z. (2018). Dipeptidyl peptidase-4 (DPP-4) inhibitors: promising new agents for autoimmune diabetes. Clinical and experimental medicine, 18(4), 473-480.

Deacon, C. F. (2018). A review of dipeptidyl peptidase‐4 inhibitors. Hot topics from randomized controlled trials. Diabetes, Obesity and Metabolism, 20, 34-46.

Berger, J. P., SinhaRoy, R., Pocai, A., Kelly, T. M., Scapin, G., Gao, Y. D., ... & Carr, R. D. (2018). A comparative study of the binding properties, dipeptidyl peptidase‐4 (DPP‐4) inhibitory activity and glucose‐lowering efficacy of the DPP‐4 inhibitors alogliptin, linagliptin, saxagliptin, sitagliptin and vildagliptin in mice. Endocrinology, diabetes & metabolism, 1(1), e00002.

Olivares, M., Schüppel, V., Hassan, A. M., Beaumont, M., Neyrinck, A. M., Bindels, L. B., ... & Delzenne, N. M. (2018). The potential role of the dipeptidyl peptidase-4-like activity from the gut microbiota on the host health. Frontiers in microbiology, 1900.

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For research use only. Not intended for any clinical use.

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