D3196
Dipeptidyl Peptidase VIII human
recombinant, expressed in Sf9 cells
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About This Item
UNSPSC Code:
12352204
NACRES:
NA.54
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Quality Level
recombinant
expressed in Sf9 cells
form
solution
specific activity
≥20 units/μg protein
mol wt
100 kDa
concentration
≥0.08 mg/mL
shipped in
dry ice
storage temp.
−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.
Biochem/physiol Actions
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.
Physical properties
Full length sequence with an N-terminal GST tag
Unit Definition
One unit will hydrolyze 1.0 picomole of Ala-Pro-AMC per minute at pH 7.4 at 25 deg °C
Physical form
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.
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
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Beat Nyfeler et al.
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
Beat Nyfeler et al.
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
C A Abbott et al.
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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