Human DPPIV/CD26 (His Tag)

SKU: 93758ES20

Size: 20 μg
Price:
Sale price$271.00

Shipping calculated at checkout

Stock:
In stock

Description

 

DPPIV/CD26 (EC 3.4.14.5) is an approximately 110 kDa serine exopeptidase that releases Xaa-Pro or Xaa-Ala dipeptides from the N-terminus of oligo- and polypeptides. It regulates immune and endocrine function through the cleavage of multiple chemokines, growth factors, and peptide hormones. Mature human DPPIV consists of a 6 amino acid (aa) cytoplasmic tail, a 22 aa transmembrane segment, and a 738 aa extracellular domain (ECD) that contains the catalytic active site (Ser, Asp, and His charge relay system). Within the ECD, human DPPIV/CD26 shares 84% amino acid sequence identity with mouse and rat DPPIV. DPPIV is expressed as a noncovalent homodimer on the surface of epithelial cells, endothelial cells, and activated lymphocytes, and it can be released by MMP mediated shedding. It cleaves a range of peptide hormones including Glucagon, Glucagon-like Peptides 1 and 2, GIP, GHRH, Procalcitonin, Neuropeptide Y, and Substance P. It is released from adipocytes and induces insulin resistance in adipocytes and skeletal muscle. DPPIV also cleaves many chemokines, resulting in reduced chemotactic activity of CXCL6, 9, 10, 11, 12, and CCL5 but unchanged angiostatic activity of CXCL9 and CXCL10. Cleavage can increase (CCL5), decrease (CXCL12), or have no effect (CCL4) on chemokine blockade of HIV-1 cellular infectivity . In addition, DPPIV cleavage of CCL4 broadens chemokine receptor usage to also include CCR2b. DPPIV serves as a cell entry coreceptor for HIV and coronavirus.

 

Specifications

Synonyms

ADCP2; CD26; DPPIV; DPP4; ADABP; TP103; EC 3.4.14.5

Uniprot No.

 P27487

Source

Recombinant Human DPPIV/CD26 Protein is expressed from HEK293 Cells with His tag at the C-terminal. It contains Asn29-Pro766. 

Molecular Weight

The protein has a predicted MW of 90.5 kDa. Due to glycosylation, the protein migrates to 91-115 kDa based on Tris-Bis PAGE result.

Physical Appearance

Sterile Filtered White lyophilized (freeze-dried) powder.

Purity

> 95% as determined by SDS-PAGE and HPLC

Activity

ELISA DataImmobilized Human DPPIV at 1μg/ml (100μl/well) on the plate. Dose response curve for Anti-DPPIV Antibody, hFc Tag with the EC50 of 8.1ng/ml determined by ELISA.

Endotoxin

< 1.0 EU per 1μg of the protein by the LAL method.

Formulation

Lyophilized from 0.22 μm filtered solution in PBS (pH 7.4). Normally 5% trehalose is added as protectant before lyophilization.

Reconstitution

Centrifuge tubes before opening. Reconstituting to a concentration more than 100 μg/mL is recommended (usually we use 1 mg/mL solution for lyophilization). Dissolve the lyophilized protein in distilled water.

 

Storage

Transported with ice packs. Store at -20℃ to -80℃, valid for one year.

After reconstitution, store unopened at -20 to -80°C for 3 to 6 months. After reconstitution, store at 2 to 8°C for 2 to 7 days.

It is recommended to store in aliquots and freeze for the first use to avoid repeated freezing and thawing.

 

Note

1. Avoid repeated freezing and thawing.

2. For your safety and health, please wear a lab coat and disposable gloves when operating.

3. This product is for scientific research purposes only.

 

Product Data

Tris-Bis PAGE

Payment & Security

American Express Apple Pay Diners Club Discover Google Pay Mastercard Visa

Your payment information is processed securely. We do not store credit card details nor have access to your credit card information.

Inquiry

You may also like

FAQ

The product is for research purposes only and is not intended for therapeutic or diagnostic use in humans or animals. Products and content are protected by patents, trademarks, and copyrights owned by Yeasen Biotechnology. Trademark symbols indicate the country of origin, not necessarily registration in all regions.

Certain applications may require additional third-party intellectual property rights.

Yeasen is dedicated to ethical science, believing our research should address critical questions while ensuring safety and ethical standards.