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Safety Information

D3196

Sigma-Aldrich

Dipeptidyl Peptidase VIII human

recombinant, expressed in Sf9 cells

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About This Item

UNSPSC Code:
12352204
NACRES:
NA.54

Quality Level

200

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

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

Cartagena Act

Cartagena Act Listed

JAN Code

D3196-VAR:
D3196-BULK:
D3196-10UG:
D3196-10UG-PW:

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Certificates of Analysis (COA)

Lot/Batch Number
SLCJ0269
SLBP3118V
SLBN6181V
SLBK9227V
SLBJ6250V

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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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