Recombinant Pig Dipeptidyl peptidase 4 (DPP4), partial

Product Details

Purity
>85% (SDS-PAGE)
Target Names
DPP4
Uniprot NO.
Species
Sus scrofa (Pig)
Source
Yeast
Protein Length
Partial
Tag Info
N-terminal His-tagged/Tag-Free
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Storage
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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 Customer Reviews

Target Background

Function(From Uniprot)
Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T-cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. 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. May be involved in the promotion of lymphatic endothelial cells adhesion, migration and tube formation. When overexpressed, enhanced cell proliferation, a process inhibited by GPC3. 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. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.
Gene References into Functions
  1. This study shows that porcine DPP-IV is generally inhibited with greater potency by protein-derived peptides than is the human enzyme PMID:25828735
  2. DPP-IV from porcine kidney cortex was characterized. PMID:21093607
  3. Neutral endopeptidase 24.11 and DPP-IV is superior to DPP-IV inhibition alone in preserving intact GLP-1, which implies possibility that the combination has therapeutic potential. PMID:16025254
  4. Results describe the distribution of dipeptidyl peptidase IV-like activity enzymes in porcine tissue sections by RT-PCR. PMID:16700514

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Subcellular Location
[Dipeptidyl peptidase 4 soluble form]: Secreted.; Cell membrane; Single-pass type II membrane protein. Apical cell membrane; Single-pass type II membrane protein. Cell projection, invadopodium membrane; Single-pass type II membrane protein. Cell projection, lamellipodium membrane; Single-pass type II membrane protein. Cell junction. Membrane raft.
Protein Families
Peptidase S9B family, DPPIV subfamily
Database Links
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