Human DPP4 / DPPIV / CD26 Protein
ADABP,ADCP2,CD26,DPPIV,TP103
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| Catalog Number | P10688-HNCH |
|---|---|
| Organism Species | Human |
| Host | Human Cells |
| Synonyms | ADABP,ADCP2,CD26,DPPIV,TP103 |
| Molecular Weight | The recombinant human DPPIV exists as the mature active form, and consists of 738 amino acids with a predicted molecular mass of 85.4 kDa. The apparent molecular mass of the glycosylated rhDPPIV is approximately 95 kDa in SDS-PAGE under reducing conditions. |
| predicted N | Asn 29 |
| SDS-PAGE |  |
| Purity | > 70 % as determined by SDS-PAGE |
| Protein Construction | The native mature form of human DPPIV (NP_001926.2) extracellular domain (Asn 29-Pro 766) was expressed and purified. |
| Bio-activity | 1. Measured by its ability to cleave the fluorogenic peptide substrate, Gly-Pro-7-amido-4-methylcoumarin (GP-AMC). The specific activity is > 2,500 pmoles/min/μg. 2. Using the Octet RED System, the affinity constant (Kd) of human DPP4 (P 10688-HNCH) bound to Spike (HCoV-EMC/2012) (P 40071-V31B) was 20 nM. 3. Using the Octet RED System, the affinity constant (Kd) of human DPP4 (P 10688-HNCH) bound to Spike (HCoV-EMC/2012) (P 40071-V05B) was 50 nM. 4. Using the Octet RED System, the affinity constant (Kd) of human DPP4 (P 10688-HNCH) bound to Spike (HCoV-EMC/2012) (ECD, aa 1-1297) (P 40069-V08B) was 33 nM. 5. Using the Octet RED System, the affinity constant (Kd) of human DPP4 (P 10688-HNCH) bound to Spike-His (aa 1-760) (P 40021-V08H) was 12 nM. |
| Research Area | Microbiology |Pathogenic microorganism |viruses |animal virus |Virus infection associated |Virus host receptor | |
| Formulation | Lyophilized from sterile 100mM NaCl, 50mM Tris, pH 7.5 1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA. |
| Background | Dipeptidyl peptidase-4 (DPP4) or adenosine deaminase complexing protein 2 (ADCP 2) or T-cell activation antigen CD26 is a serine exopeptidase belonging to the S9B protein family that cleaves X-proline dipeptides from the N-terminus of polypeptides, such as chemokines, neuropeptides, and peptide hormones. The enzyme is a type II transmembrane glycoprotein, expressed on the surface of many cell types. It is also present in serum and other body fluids in a truncated form (sCD26/DPPIV). The soluble CD26 (sCD26) as a tumour marker for the detection of colorectal cancer (CRC) and advanced adenomas. As both a regulatory enzyme and a signalling factor, DPP4 has been evaluated and described in many studies. DPP4 inhibition results in increased blood concentration of the incretin hormones glucagon-like peptide-1 (GLP-1) and gastric inhibitory polypeptide (GIP). This causes an increase in glucose-dependent stimulation, resulting in a lowering of blood glucose levels. Recent studies have shown that DPP4 inhibitors can induce a significant reduction in glycosylated haemoglobin (HbA(1c)) levels, either as monotherapy or as a combination with other antidiabetic agents. Research has also demonstrated that DPP4 inhibitors portray a very low risk of hypoglycaemia development, and are a new pharmacological class of drugs for treating Type 2 diabetes. |
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