Human CellExp DPPIV/CD26, human recombinant protein (untagged)
DPP4, DPP-4, ADABP, ADCP2, ADCP-2, CD26, CD-26, DPPIV, DPPIV, TP103, TP-103
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P27487 |
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Calculated MW | This protein with two amino acids (Gly-Pro) at the N- terminus has a calculated MW of 85.4 kDa expressed. Protein migrates as 95 kDa in reduced SDS-PAGE resulting from glycosylation. |
Gene ID | 1803 |
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Gene Symbol | DPP4 |
Other Names | DPP4, DPP-4, ADABP, ADCP2, ADCP-2, CD26, CD-26, DPPIV, DPPIV, TP103, TP-103 |
Gene Source | Human |
Source | HEK293 cells |
Assay&Purity | SDS-PAGE; ≥95% |
Assay2&Purity2 | N/A; |
Recombinant | Yes |
Results | Measured by its ability to cleave the fluorogenic peptide substrate, Gly-Pro-7-amido-4-methylcoumarin (GP-AMC). The specific activity is > 5500 pmoles /min / µg. |
Target/Specificity | DPPIV/CD26 |
Application Notes | Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 µg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C. |
Format | Lyophilized |
Storage | -20°C; Lyophilized from 0.22 µm filtered solution in PBS, pH7.4. Normally Mannitol or Trehalose is added as protectants before lyophilization. |
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Background
Dipeptidyl peptidase-IV (DPPIV), also known as adenosine deaminase complexing protein 2, DPPIV or CD26 is antigenic enzyme expressed on the surface of most cell types and is associated with immune regulation, signal transduction and apoptosis. It is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. The substrates of DPPIV are proline (or alanine)-containing peptides and include growth factors, chemokines, neuropeptides, and vasoactive peptides. DPPIV plays a major role in glucose metabolism. It is responsible for the degradation of incretins such as GLP-1. DPPIV plays an important role in tumor biology, and is useful as a marker for various cancers, with its levels either on the cell surface or in the serum increased in some neoplasms and decreased in others. DPPIV also binds the enzyme adenosine deaminase specifically and with high affinity. The significance of this interaction has yet to be established.
References
Misumi Y.,et al.Biochim. Biophys. Acta 1131:333-336(1992).
Darmoul D.,et al.J. Biol. Chem. 267:4824-4833(1992).
Tanaka T.,et al.J. Immunol. 149:481-486(1992).
Tanaka T.,et al.J. Immunol. 150:2090-2090(1993).
Abbott C.A.,et al.Immunogenetics 40:331-338(1994).
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