D3196
Dipeptidyl Peptidase VIII human
recombinant, expressed in Sf9 cells
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About This Item
Código UNSPSC:
12352204
NACRES:
NA.54
En este momento no podemos mostrarle ni los precios ni la disponibilidad
Productos recomendados
Nivel de calidad
recombinante
expressed in Sf9 cells
Formulario
solution
actividad específica
≥20 units/μg protein
mol peso
100 kDa
concentración
≥0.08 mg/mL
Condiciones de envío
dry ice
temp. de almacenamiento
−70°C
Categorías relacionadas
Aplicación
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.
Acciones bioquímicas o fisiológicas
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.[1]
Propiedades físicas
Full length sequence with an N-terminal GST tag
Definición de unidad
One unit will hydrolyze 1.0 picomole of Ala-Pro-AMC per minute at pH 7.4 at 25 deg °C
Forma física
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.
Código de clase de almacenamiento
10 - Combustible liquids
Clase de riesgo para el agua (WGK)
WGK 1
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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
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
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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