Mouse Dipeptidyl Peptidase 4 / CD26 (DPP4) Protein

Este producto es parte de DPP4 - dipeptidyl peptidase 4
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2249€ (1 mg)

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935106861
info@markelab.com
name
Mouse Dipeptidyl Peptidase 4 / CD26 (DPP4) Protein
category
Proteins and Peptides
provider
Abbexa
reference
abx066346
tested applications
WB, SDS-PAGE

Description

Recombinant Dipeptidyl Peptidase IV (DPP4) is a recombinant Mouse protein produced in a Prokaryotic expression system (E. coli).

Documents del producto

Instrucciones
Data sheet
Descargar

Product specifications

Category
Proteins and Peptides
Immunogen Target
Dipeptidyl Peptidase 4 / CD26 (DPP4)
Host
E. coli
Origin
Mouse
Conjugation
Unconjugated
Observed MW
Molecular Weight: Calculated MW: 16.3 kDa
Concentration: Prior to lyophilization: 200 µg/ml
Sequence Fragment: Ser631-His760
Tag: N-terminal His tag
Expression
Recombinant
Purity
> 95%
Size 1
1 mg
Size 2
5 mg
Form
Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex.
Tested Applications
WB, SDS-PAGE
Buffer
Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300.
Availability
Shipped within 1-2 months.
Storage
Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles.
Dry Ice
No
UniProt ID
P28843
Gene ID
13482
Alias
CD26,ADABP,ADCP2,DPPIV,TP103,Dipeptidyl peptidase 4,Adenosine deaminase complexing protein 2,ADCP-2,Dipeptidyl peptidase IV,T-cell activation antigen CD26
Background
Protein DPP4
Status
RUO
Note
This product is for research use only.   Not for human consumption, cosmetic, therapeutic or diagnostic use.

Descripción

Dipeptidyl peptidase 4 (DPP4), also known as CD26, is a transmembrane glycoprotein and serine protease that plays a significant role in regulating glucose metabolism, immune function, and cell signaling. It is expressed on the surface of various cell types, including epithelial cells, endothelial cells, and immune cells such as T cells and B cells. DPP4 is widely known for its role in glucose homeostasis through its enzymatic activity, where it deactivates incretin hormones like glucagon-like peptide-1 (GLP-1) and glucose-dependent insulinotropic polypeptide (GIP). These hormones promote insulin release in response to meals, and their inactivation by DPP4 reduces insulin secretion, thereby impacting blood sugar levels. Beyond its metabolic functions, DPP4 also participates in various immune regulatory pathways. As CD26, it is involved in T-cell activation and co-stimulation. DPP4 is linked to inflammatory processes and certain cancers, particularly due to its enzymatic activity and role in regulating immune responses. Additionally, the soluble form of DPP4 (sDPP4), which circulates in the plasma, plays a role in systemic metabolic and immune regulation.

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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.

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