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Key Documents

D4943

Sigma-Aldrich

Dipeptidyl Peptidase IV human

recombinant, expressed in baculovirus infected Sf9 cells, pkg of ≥1.0 units/vial, ≥10 units/mg protein

Sinônimo(s):

CD26, DPPIV, Dipeptidyl aminopeptidase IV, Glycoprotein GP110

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About This Item

Número da licença da enzima:
Número MDL:
Código UNSPSC:
12352204
NACRES:
NA.54

recombinante

expressed in baculovirus infected Sf9 cells

Nível de qualidade

forma

solution

atividade específica

≥10 units/mg protein

peso molecular

105 kDa

embalagem

pkg of ≥1.0 units/vial

nº de adesão UniProt

Condições de expedição

wet ice

temperatura de armazenamento

−20°C

Informações sobre genes

human ... DPP4(1803)

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Descrição geral

C-terminal histidine-tagged. Soluble form (residues 29-766) MW 105 kDa

Aplicação

Human dipeptidyl peptidase IV has been used to study interactive hemodynamic effects of its inhibition and angiotensin-converting enzyme inhibition in humans. Human dipeptidyl peptidase IV has also been used in a study that informed the understanding of Hymenoptera venom allergies.
The enzyme from Sigma has been used to study the LC-MS (liquid chromatography-mass spectrometry) based assay method for DPP-IV inhibitor screening and substrate discovery.

Ações bioquímicas/fisiológicas

DPPIV has a post-proline dipeptidyl aminopeptidase activity that hydrolyzes N-terminal dipeptides from the unsubstituted N-terminus of peptides with the sequence of X-Pro-Z and X-Ala-Z. The optimum pH is found to be 7.4-8.7. DPPIV is involved in the regulation of several important physiological processes such as immune functions, inflammation, CNS, endocrine functions, bone marrow mobilization, cancer growth, cell adhesion, glucose hemostasis and sepsis/severe infection.
Native DPPIV is a ubiquitous type II transmembrane glycoprotein and a serine protease of the S9 prolyl-oligopeptidase family. In vivo, it is synthesized with a signal peptide, which functions as the membrane anchoring domain. There is an 88% sequence homology between the human and porcine kidney enzymes. Both exist as homodimers with a subunit molecular weight of ~30 kDa. The high mannose 100 kDa DPPIV precursor is processed in the Golgi to yield a 124 kDa heavily N-and O-linked mature glycoprotein. It is then sorted to the apical membrane through the concerted action of both N- and O-linked glycans and its association with lipid microdomains. The porcine enzyme contains 18.3% carbohydrates, which the glycan composition is 0.9% fucose, 3.4% mannose, 5.1% galactose, 8.2% glucosamine, and 0.7% sialic acid. DPPIV is highly expressed on endothelial cells, epithelial cells, and lymphocytes. It is also present in plasma in its soluble form.

Definição da unidade

One unit will produce 1.0 μmole of p-nitroaniline from Gly-L-Pro p-nitroanilide per min in 100 mM Tris-HCl at pH 7.6 at 37 °C.

forma física

Supplied as a solution in 10 mM Tris-HCl, pH 7.6, 200 mM NaCl, 1 mM EDTA and 10% glycerol.

Outras notas

Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 1

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable


Certificados de análise (COA)

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LC-MS based assay method for DPP-IV inhibitor screening and substrate discovery.
Liu, J., Cheng, X., & Fu, L.
Analytical Methods : Advancing Methods and Applications, 4(6), 1797-1805 (2012)
Ryugen Takahashi et al.
Frontiers in oncology, 11, 714527-714527 (2021-09-08)
Radical resection is the only curative treatment for pancreatic cancer, which is a life-threatening disease. However, it is often not easy to accurately identify the extent of the tumor before and during surgery. Here we describe the development of a
Mark D Gorrell
Clinical science (London, England : 1979), 108(4), 277-292 (2004-12-09)
DP (dipeptidyl peptidase) IV is the archetypal member of its six-member gene family. Four members of this family, DPIV, FAP (fibroblast activation protein), DP8 and DP9, have a rare substrate specificity, hydrolysis of a prolyl bond two residues from the
Petr Busek et al.
The international journal of biochemistry & cell biology, 36(3), 408-421 (2003-12-23)
Post-translational modification of proteins is an important regulatory event. Numerous biologically active peptides that play an essential role in cancerogenesis contain an evolutionary conserved proline residue as a proteolytic-processing regulatory element. Proline-specific proteases could therefore be viewed as important "check-points".
Ivan O Maslov et al.
Pharmaceuticals (Basel, Switzerland), 15(3) (2022-03-27)
Compounds that contain (R)-3-amino-4-(2,4,5-trifluorophenyl)butanoic acid substituted with bicyclic amino moiety (2-aza-bicyclo[2.2.1]heptane) were designed using molecular modelling methods, synthesised, and found to be potent DPP-4 (dipeptidyl peptidase-4) inhibitors. Compound 12a (IC50 = 16.8 ± 2.2 nM), named neogliptin, is a more

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