DPP4/CD26 (D6D8K) Rabbit mAb (IHC Formulated) #40134
- IHC
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| Source/Isotype | Rabbit IgG |
Application Key:
- IHC-Immunohistochemistry
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Immunohistochemistry (Paraffin) | 1:200 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu491 of human DPP4 protein.
Background
DPP4 (CD26) is a type II transmembrane glycoprotein expressed ubiquitously in most tissues and different cell types (1,2). The protein has a short cytoplasmic domain, a transmembrane domain, a flexible stalk fragment, and an extracellular fragment (2). Both the catalytic peptide hydrolase domain and the beta-propeller ligand binding domain are located in the extracellular fragment (2). DPP4 is a multifunctional protein that exists in both a membrane-bound form as well as an extracellular soluble form. As a peptidase, it removes N-terminal dipeptides sequentially from proteins with a proline or alanine as the penultimate P1 amino acid (3,4). DPP4 has been shown to cleave a wide range of substrates, including GLP-1, BNP, substance P, etc. It is also involved in the regulation of related biological functions (5). In addition to its peptidase activity, DPP4 interacts with multiple important cell surface ligands, such as adenosine deaminase, fibronectin, and IGF2 receptor, to influence processes like T cell activation, cell migration, and proliferation (5). Several DPP4 inhibitors have been developed and their effects have been tested in the field of diabetes, cardiovascular disease, and tumor immunity (2,5,6).
This product detects a SARS-CoV-2-related target for research into the mechanisms of the Novel Coronavirus, which has caused the COVID-19 pandemic.
- Mentzel, S. et al. (1996) J Histochem Cytochem 44, 445-61.
- Röhrborn, D. et al. (2015) Front Immunol 6, 386.
- Hopsu-Havu, V.K. and Glenner, G.G. (1966) Histochemie 7, 197-201.
- Lone, A.M. et al. (2010) AAPS J 12, 483-91.
- Zhong, J. et al. (2015) J Diabetes Res 2015, 606031.
- Ohnuma, K. et al. (2015) Nat Immunol 16, 791-2.
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