D3196
Dipeptidyl Peptidase VIII human
recombinant, expressed in Sf9 cells
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About This Item
Produits recommandés
Niveau de qualité
Produit recombinant
expressed in Sf9 cells
Forme
solution
Activité spécifique
≥20 units/μg protein
Poids mol.
100 kDa
Concentration
≥0.08 mg/mL
Conditions d'expédition
dry ice
Température de stockage
−70°C
Application
Human dipeptidyl peptidase VIII has been used in a study to identify ERGIC-53 as an intracellular transport receptor of α1-antitrypsin. Human dipeptidyl peptidase VIII has also been used in a study to investigate the cargo selectivity of the ERGIC-53/MCFD2 transport receptor complex.
Actions biochimiques/physiologiques
Dipeptidyl peptidase VIII (DPP8) is a 100 kDa monomeric protein expressed in the cytoplasm. It is a postproline dipeptidyl aminopeptidase that is homologous to DPPIV and fibroblast activation protein (FAP). It hydrolyzes Ala-Pro, Arg-Pro and Gly-Pro. DPP8 has a neutral pH optimum. It may be involved in T-cell activation and immune function as it is similar to DPPIV . It is upregulated during immune activation.
Propriétés physiques
Full length sequence with an N-terminal GST tag
Définition de l'unité
One unit will hydrolyze 1.0 picomole of Ala-Pro-AMC per minute at pH 7.4 at 25 deg °C
Forme physique
Supplied as a solution in 40 mM Tris-HCL, pH 8.0, 110 mM NaCl, 2.2 mM KCl, 3 mM DTT and 20% glycerol.
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
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The Journal of cell biology, 180(4), 705-712 (2008-02-20)
Secretory proteins are exported from the endoplasmic reticulum (ER) by bulk flow and/or receptor-mediated transport. Our understanding of this process is limited because of the low number of identified transport receptors and cognate cargo proteins. In mammalian cells, the lectin
Traffic (Copenhagen, Denmark), 7(11), 1473-1481 (2006-10-03)
Exit of soluble secretory proteins from the endoplasmic reticulum (ER) can occur by receptor-mediated export as exemplified by blood coagulation factors V and VIII. Their efficient secretion requires the membrane lectin ER Golgi intermediate compartment protein-53 (ERGIC-53) and its soluble
European journal of biochemistry, 267(20), 6140-6150 (2000-09-30)
Dipeptidyl peptidase (DPP) IV has roles in T-cell costimulation, chemokine biology, type-II diabetes and tumor biology. Fibroblast activation protein (FAP) has been implicated in tumor growth and cirrhosis. Here we describe DPP8, a novel human postproline dipeptidyl aminopeptidase that is
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