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Human DPPIV/CD26 Protein 4898

$450.00$1,500.00

Summary

  • Expression: HEK293
  • Active: Yes (catalytic)
  • Amino Acid Range: Asn29-Pro766
SKU: 4898parent Categories: , Tags: , , ,
Weight1 lbs
Dimensions9 × 5 × 2 in
accession

P27487

express system

HEK293

product tag

C-His

purity

> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC

background

CD26/dipeptidyl peptidase (DPP)IV is a membrane-bound protein found in many cell types of the body, and a soluble form is present in body fluids. There is longstanding evidence that various primary tumors and also metastases express DPPIV/CD26 to a variable extent.

molecular weight

The protein has a predicted MW of 86.39 kDa. Due to glycosylation, the protein migrates to 90-115 kDa based on Tris-Bis PAGE result.

available size

100 µg, 500 µg

endotoxin

Less than 1EU per μg by the LAL method.

Human DPPIV/CD26 Protein 4898

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
Storage Instructions
Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer
Shipped at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
CD26/dipeptidyl peptidase (DPP)IV is a membrane-bound protein found in many cell types of the body, and a soluble form is present in body fluids. There is longstanding evidence that various primary tumors and also metastases express DPPIV/CD26 to a variable extent.
Protein names
Dipeptidyl peptidase 4 (EC 3.4.14.5) (ADABP) (Adenosine deaminase complexing protein 2) (ADCP-2) (Dipeptidyl peptidase IV) (DPP IV) (T-cell activation antigen CD26) (TP103) (CD antigen CD26) [Cleaved into: Dipeptidyl peptidase 4 membrane form (Dipeptidyl peptidase IV membrane form); Dipeptidyl peptidase 4 soluble form (Dipeptidyl peptidas
Gene names
DPP4,DPP4 ADCP2 CD26
Protein family
Peptidase S9B family, DPPIV subfamily
Mass
9606Da
Function
FUNCTION: Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation (PubMed:10900005, PubMed:10951221, PubMed:11772392, PubMed:17287217). Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC (PubMed:10900005, PubMed:10951221, 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:10593948, PubMed:16651416). 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:10570924, PubMed:16254193). Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline (PubMed:10593948). {ECO:0000269|PubMed:10570924, ECO:0000269|PubMed:10593948, ECO:0000269|PubMed:10900005, ECO:0000269|PubMed:10951221, ECO:0000269|PubMed:11772392, ECO:0000269|PubMed:14691230, ECO:0000269|PubMed:16254193, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17287217, ECO:0000269|PubMed:17549790, ECO:0000269|PubMed:18708048}.; FUNCTION: (Microbial infection) Acts as a receptor for human coronavirus MERS-CoV-2. {ECO:0000269|PubMed:23835475}.
Subellular location
SUBCELLULAR LOCATION: [Dipeptidyl peptidase 4 soluble form]: Secreted {ECO:0000269|PubMed:10951221, ECO:0000269|PubMed:16254193}. Note=Detected in the serum and the seminal fluid. {ECO:0000269|PubMed:10951221, ECO:0000269|PubMed:16254193}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10900005, ECO:0000269|PubMed:11772392, ECO:0000305|PubMed:8101391}; Single-pass type II membrane protein. Apical cell membrane {ECO:0000269|PubMed:11773049}; Single-pass type II membrane protein. Cell projection, invadopodium membrane {ECO:0000269|PubMed:16651416}; Single-pass type II membrane protein. Cell projection, lamellipodium membrane {ECO:0000269|PubMed:16651416}; Single-pass type II membrane protein. Cell junction {ECO:0000269|PubMed:11772392}. Membrane raft {ECO:0000269|PubMed:17287217}. Note=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). {ECO:0000269|PubMed:10900005, ECO:0000269|PubMed:11772392, ECO:0000269|PubMed:11773049, ECO:0000269|PubMed:12676959, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17287217}.
Tissues
TISSUE SPECIFICITY: Expressed 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. {ECO:0000269|PubMed:1677636, ECO:0000269|PubMed:18708048}.
Structure
SUBUNIT: Monomer. Homodimer (PubMed:12483204, PubMed:12646248, PubMed:12832764, PubMed:12906826, PubMed:15448155, PubMed:17287217). Heterodimer with Seprase (FAP) (PubMed:16651416). Requires homodimerization for optimal dipeptidyl peptidase activity and T-cell costimulation. Found in a membrane raft complex, at least composed of BCL10, CARD11, DPP4 and IKBKB (PubMed:17287217). Associates with collagen (PubMed:8526932). Interacts with PTPRC; the interaction is enhanced in an interleukin-12-dependent manner in activated lymphocytes (PubMed:12676959). Interacts (via extracellular domain) with ADA; does not inhibit its dipeptidyl peptidase activity (PubMed:10951221, PubMed:14691230, PubMed:15016824, PubMed:7907293, PubMed:8101391). Interacts with CAV1 (via the N-terminus); the interaction is direct (PubMed:17287217). Interacts (via cytoplasmic tail) with CARD11 (via PDZ domain); its homodimerization is necessary for interaction with CARD11 (PubMed:17287217). Interacts with IGF2R; the interaction is direct (PubMed:10900005). Interacts with GPC3 (PubMed:17549790). Interacts with human coronavirus-EMC spike protein and acts as a receptor for this virus (PubMed:23486063). {ECO:0000269|PubMed:10900005, ECO:0000269|PubMed:10951221, ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12676959, ECO:0000269|PubMed:12832764, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:14691230, ECO:0000269|PubMed:15016824, ECO:0000269|PubMed:15448155, ECO:0000269|PubMed:16651416, ECO:0000269|PubMed:17287217, ECO:0000269|PubMed:17549790, ECO:0000269|PubMed:23486063, ECO:0000269|PubMed:7907293, ECO:0000269|PubMed:8101391, ECO:0000269|PubMed:8526932}.; SUBUNIT: (Microbial infection) Interacts with MERS coronavirus/MERS-CoV spike protein. {ECO:0000269|PubMed:23835475}.
Post-translational modification
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.; PTM: N- and O-Glycosylated. {ECO:0000269|PubMed:10900005, ECO:0000269|PubMed:11773049, ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603}.; PTM: 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. {ECO:0000269|PubMed:10900005}.
Domain
DOMAIN: Th
Target Relevance information above includes information from UniProt accession : P27487
The UniProt Consortium

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