Human Recombinant DPP10 protein, His Tag (V2LY-0526-LY3628)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Human
Tag
His Tag
Protein Construction
This product is Human Recombinant DPP10 protein, His Tag consist of Amino Acid: 56-796 and predicts a molecular mass of 87.4 kDa.
Molecule Mass
87.4 kDa
Sequence
Amino Acid: 56-796
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
>97% as determined by SDS-PAGE
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile PBS
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Dipeptidyl Peptidase Like 10
Function
Promotes cell surface expression of the potassium channel KCND2 (PubMed:15454437).

Modulates the activity and gating characteristics of the potassium channel KCND2 (PubMed:15454437).

Has no dipeptidyl aminopeptidase activity (PubMed:12662155).
Biological Process
Positive regulation of protein localization to plasma membrane Source: CACAO
Protein localization to plasma membrane Source: UniProtKB
Regulation of potassium ion transmembrane transport Source: UniProtKB
Cellular Location
Cell membrane
Involvement in disease
Asthma (ASTHMA):
The most common chronic disease affecting children and young adults. It is a complex genetic disorder with a heterogeneous phenotype, largely attributed to the interactions among many genes and between these genes and the environment. It is characterized by recurrent attacks of paroxysmal dyspnea, with wheezing due to spasmodic contraction of the bronchi.
Topology
Cytoplasmic: 1-34
Helical: 35-55
Extracellular: 56-796
PTM
N-glycosylation is important for cell surface expression, specially at Asn-257, which is crucial.

Sim, S., Choi, Y., Lee, D. H., Lee, H. R., Seob Shin, Y., & Park, H. S. (2022). Contribution of dipeptidyl peptidase 10 to airway dysfunction in patients with NSAID‐exacerbated respiratory disease. Clinical & Experimental Allergy, 52(1), 115-126.

Qian, X. K., Zhang, J., Li, X. D., Song, P. F., & Zou, L. W. (2022). Research Progress on Dipeptidyl Peptidase Family: Structure, Function and Xenobiotic Metabolism. Current Medicinal Chemistry.

Choy, T. K., Wang, C. Y., Phan, N. N., Khoa Ta, H. D., Anuraga, G., Liu, Y. H., ... & Kao, T. J. (2021). Identification of Dipeptidyl Peptidase (DPP) family genes in clinical breast cancer patients via an integrated bioinformatics approach. Diagnostics, 11(7), 1204.

Metzner, K. (2020). The impact of the β-subunit DPP10 on cardiac action potential and native voltage-gated K+ and Na+ currents.

Belau, F., Metzner, K., Christ, T., Ravens, U., Schaefer, M., Künzel, S., ... & Kämmerer, S. (2019). DPP10 is a new regulator of Nav1. 5 channels in human heart. International Journal of Cardiology, 284, 68-73.

Ni, H., Rajamani, S., & Giles, W. R. (2019). Novel regulation of the mammalian cardiac Na+ channel by dipeptidyl peptidase 10 interactions: An editorial comment. International journal of cardiology, 284, 74-76.

Zhang, Y., Poobalasingam, T., Yates, L. L., Walker, S. A., Taylor, M. S., Chessum, L., ... & Dean, C. H. (2018). Manipulation of dipeptidylpeptidase 10 in mouse and human in vivo and in vitro models indicates a protective role in asthma. Disease models & mechanisms, 11(1), dmm031369.

Sato, A., & Ogita, H. (2017). Pathophysiological implications of dipeptidyl peptidases. Current Protein and Peptide Science, 18(8), 843-849.

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For research use only. Not intended for any clinical use.

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