Dpp4 (NM_010074) Mouse Tagged ORF Clone Lentiviral Particle
CAT#: MR222697L3V
- LentiORF®
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Lenti ORF particles, Dpp4 (Myc-DDK-tagged) - Mouse dipeptidylpeptidase 4 (Dpp4), transcript variant 1, 200ul, >10^7 TU/mL
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CNY 12,445.00
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规格
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Specifications
Product Data | |
Product Name | Dpp4 (NM_010074) Mouse Tagged ORF Clone Lentiviral Particle |
Synonyms | Cd26; Dpp-4; THAM |
Vector | pLenti-C-Myc-DDK-P2A-Puro |
ACCN | NM_010074 |
ORF Size | 2280 bp |
Sequence Data |
The ORF insert of this clone is exactly the same as(MR222697).
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OTI Disclaimer | The molecular sequence of this clone aligns with the gene accession number as a point of reference only. However, individual transcript sequences of the same gene can differ through naturally occurring variations (e.g. polymorphisms), each with its own valid existence. This clone is substantially in agreement with the reference, but a complete review of all prevailing variants is recommended prior to use. More info |
OTI Annotation | This clone was engineered to express the complete ORF with an expression tag. Expression varies depending on the nature of the gene. |
Reference Data | |
RefSeq | NM_010074.3, NP_034204.1 |
RefSeq Size | 5268 bp |
RefSeq ORF | 2283 bp |
Locus ID | 13482 |
Gene Summary | 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. Removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline.[UniProtKB/Swiss-Prot Function] |
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