Recombinant Human DPPIV/CD26 Fc Chimera Avi-tag Protein, CF Summary
| Additional Information |
Biotinylated |
| Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant MERS-CoV Spike RBD His-tag Protein
(Catalog #
10621-CV)
is immobilized at 1.00 μg/mL, 100 μL/well, Biotinylated Recombinant Human DPPIV/CD26 Fc Chimera Avi-tag (Catalog # AVI11141) binds with an ED 50 of 10.0-80.0 ng/mL. Measured by its ability to cleave the fluorogenic peptide substrate, Gly-Pro-7-amido-4-methylcoumarin (GP-AMC). The specific activity is >2700 pmol/min/μg, as measured under the described conditions. |
| Source |
Human embryonic kidney cell, HEK293-derived human DPPIV/CD26 protein Human CD26
(Asn29-Pro766)
Accession # CAA43118.1 | DIEGRMD | Human IgG1
(Pro100-Lys330) | Avi-tag | | N-terminus | | | C-terminus | |
|
| Accession # |
|
| N-terminal Sequence |
Asn29 |
| Structure / Form |
Disulfide-linked homodimer |
| Protein/Peptide Type |
Recombinant Enzymes |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
| Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
| Dilutions |
- Bioactivity
- Enzyme Activity
|
| Theoretical MW |
114 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
| SDS-PAGE |
114-134 kDa, under reducing conditions. |
Packaging, Storage & Formulations
| Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 6 months from date of receipt, -20 to -70 °C as supplied.
- 3 months, -20 to -70 °C under sterile conditions after opening.
|
| Buffer |
Supplied as a 0.2 μm filtered solution in Tris and NaCl. |
| Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human DPPIV/CD26 Fc Chimera Avi-tag Protein, CF
Background
Dipeptidyl peptidase 4 (DPPIV, also known as CD26) is an approximately 110 kDa serine exopeptidase that releases Xaa-Pro or Xaa-Ala dipeptides from the N-terminus of oligo- and polypeptides. Mature human DPPIV consists of a 6 amino acid (aa) cytoplasmic tail, a 22 aa transmembrane segment, and a 738 aa extracellular domain (ECD) that contains the catalytic active site (1). DPPIV is expressed as a noncovalent homodimer on the surface of epithelial cells, endothelial cells, and activated lymphocytes, and it can be released by MMP mediated shedding (2). It regulates immune and endocrine function through the cleavage of multiple chemokines, growth factors, and peptide hormones (3,4). It cleaves a range of peptide hormones including Glucagon, Glucagon-like Peptides 1 and 2, GIP, GHRH, Procalcitonin, Neuropeptide Y, and Substance P (5). It is released from adipocytes and induces insulin resistance in adipocytes and skeletal muscle (6). DPPIV also cleaves many chemokines, resulting in altered chemotactic activity (7-10) or impacting chemokine blockade of HIV-1 cellular infectivity depending on the chemokine target (7,9,11). It cleaves human GM-CSF and IL-3 and reduces their ability to promote myeloid cell development (12). In addition to enzymatic cleavage functions, DPPIV interacts with adenosine deaminase on T cells and with caveolin-1 on antigen presenting cells (13), provides costimulatory proliferation and activation signals to both CD4+ and CD8+ T cells (13,14), and serves as a cell entry coreceptor for HIV and coronavirus MERS-CoV-2 (15,16). DPPIV inhibitors are approved for therapeutic treatment in type 2 diabetes (17) and are being explored for treatment of several additional conditions including autoimmune diseases (18).
- Tanaka, T. et al. (1992) J. Immunol. 149:481.
- Rohrborn, D. et al. (2014) FEBS Lett. 588:3870.
- Klemann, C. et al. (2016) Clin. Exp. Immunol. 185:1.
- Mortier, A. et al. (2016) J. Leukoc. Biol. 99:955.
- Waumans, Y. et al. (2015) Front. Immunol. 6:387.
- Lamers, D. et al. (2011) Diabetes 60:1917.
- Proost, P. et al. (1998) J. Biol. Chem. 273:7222.
- Proost, P. et al. (2001) Blood 98:3554.
- Ohtsuki, T. et al. (1998) FEBS Lett. 431:236.
- Barreira da Silva, R. et al. (2015) Nat. Immunol. 16:850.
- Guan, E. et al. (2002) J. Biol. Chem. 277:32348.
- Broxmeyer, H.E. et al. (2012) Nat. Med. 18:1786.
- Ohnuma, K. et al. (2007) J. Biol. Chem. 282:10117.
- Hatano, R. et al. (2013) Immunology 138:165.
- Callebaut, C. et al. (1993) Science 262:2045.
- Raj, V.S. et al. (2013) Nature 495:251.
- Makrilakis, K. (2019) Int. J. Environ. Res. Public Health 16:2720.
- Huang, J. et al. (2022) Front. Immunol. 13:830863.
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