Product nameAnti-DPP4 antibody
See all DPP4 primary antibodies
DescriptionRabbit polyclonal to DPP4
SpecificityDoes not recognize other DPP family members.
Tested applicationsSuitable for: WBmore details
Species reactivityReacts with: Human
Synthetic peptide corresponding to Human DPP4. Based on the spacer region of Human DPP4, mid-molecule, before the cysteine-rich region.
Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Storage bufferPreservative: 0.05% Sodium azide
Constituent: 50% Glycerol
Concentration information loading...
PurityImmunogen affinity purified
Purification notesThe antibody has been peptide-affinity purified.
Our Abpromise guarantee covers the use of ab28340 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/1000 - 1/5000. Detects a band of approximately 110-120 kDa (predicted molecular weight: 88 kDa). 1/1000 when using colorimetric substrates such as BCIP/NBT - 1/5000 for chemiluminescent substrates. Bands run high because of post-translational modifications and reduction. EDTA/EGTA treatment of tissues or lysates is required to see latent zymogen. Dilution optimised using Chromogenic detection.|
FunctionCell 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.
Tissue specificityExpressed specifically in lymphatic vessels but not in blood vessels in the skin, small intestine, esophagus, ovary, breast and prostate glands. Not detected in lymphatic vessels in the lung, kidney, uterus, liver and stomach (at protein level). Expressed in the poorly differentiated crypt cells of the small intestine as well as in the mature villous cells. Expressed at very low levels in the colon.
Sequence similaritiesBelongs to the peptidase S9B family. DPPIV subfamily.
DomainThe extracellular cysteine-rich region is necessary for association with collagen, dimer formation and optimal dipeptidyl peptidase activity.
modificationsThe 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.
Cellular localizationCell membrane. Apical cell membrane. Cell projection > invadopodium membrane. Cell projection > 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. Redistributed to membrane rafts in T-cell in a interleukin-12-dependent activation. Its interaction with CAV1 is necessary for its translocation to membrane rafts. Colocalized with PTPRC in membrane rafts. 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. Colocalized with ADA at the cell junction in lymphocyte-epithelial cell adhesion. Colocalized with IGF2R in internalized cytoplasmic vesicles adjacent to the cell surface and Secreted. Detected in the serum and the seminal fluid.
- Information by UniProt
- CD26 antigen antibody
- ADA-binding protein antibody
- ADABP antibody
All lanes : Anti-DPP4 antibody (ab28340) at 1/1000 dilution
Lane 1 : DPP-4 at 0.08 µg
Lane 2 : DPP-4 at 0.04 µg
Lane 3 : DPP-4 at 0.02 µg
Lane 4 : DPP-4 at 0.01 µg
Predicted band size: 88 kDa
Observed band size: 115 kDa why is the actual band size different from the predicted?
Postranslational modifications and reduction lead to an apparent mass of 110-120 kDa on SDS-PAGE gels.
ab28340 has been referenced in 21 publications.
- Marques C et al. The dipeptidyl peptidase 4 inhibitor sitagliptin improves oxidative stress and ameliorates glomerular lesions in a rat model of type 1 diabetes. Life Sci 234:116738 (2019). PubMed: 31398418
- Fan L et al. Sitagliptin protects against hypoxia/reoxygenation (H/R)-induced cardiac microvascular endothelial cell injury. Am J Transl Res 11:2099-2107 (2019). PubMed: 31105821
- Ng PK et al. Systematic Functional Annotation of Somatic Mutations in Cancer. Cancer Cell 33:450-462.e10 (2018). PubMed: 29533785
- Li L et al. LncRNA-OIS1 regulates DPP4 activation to modulate senescence induced by RAS. Nucleic Acids Res 46:4213-4227 (2018). PubMed: 29481642
- Guida C et al. Sitagliptin and Roux-en-Y gastric bypass modulate insulin secretion via regulation of intra-islet PYY. Diabetes Obes Metab 20:571-581 (2018). PubMed: 28892258