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Mouse Anti-DPP4 Recombinant Antibody (CBFYC-2593) (CBMAB-C2667-FY)


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Summary

Host Animal
Mouse
Specificity
Human
Clone
CBFYC-2593
Antibody Isotype
IgG1
Application
WB, IHC-P, FC, IF

Basic Information

Specificity
Human
Antibody Isotype
IgG1
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

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

Format
Liquid
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at-20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Dipeptidyl Peptidase 4
Introduction
The protein encoded by this gene is identical to adenosine deaminase complexing protein-2, and to the T-cell activation antigen CD26. It is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides.
Entrez Gene ID
1803
UniProt ID
P27487
Alternative Names
Dipeptidyl Peptidase 4; Adenosine Deaminase Complexing Protein 2; Dipeptidylpeptidase IV (CD26, Adenosine Deaminase Complexing Protein 2); T-Cell Activation Antigen CD26; Dipeptidyl Peptidase IV; EC 3.4.14.5; DPP IV; ADCP-2; ADCP2
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.
More Infomation

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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