Human DPPIV / CD26 Protein, His Tag

Proteins and Peptides

貨號 Cat. No.
DP4-H5221
規格 Size
50ug
品牌 Brand
ACROBiosystems
Species
Human
Conjugate
Unconjugated
Expression System
HEK293
Tag
His Tag

Description




Source : 


Human DPPIV, His Tag (DP4-H5221) is expressed from human 293 cells (HEK293). It contains AA Asp 34 - Pro 766 (Accession # NP_001926.2).


 

Molecule : DPPIV


 

Synonyms : DPP4,ADABP,ADCP2,CD26,DPPIV,TP103


 

Format : Powder


 

Category : Enzymes


 

Accession : NP_001926.2


 

Storage : -20℃


 

Shipping condition : Powder,RT


 

Molecular Weight : 85.7 kDa


 

Characteristics :


This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 85.7 kDa. The protein migrates as 95 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.


 

Endotoxin Level : Less than 1.0 EU per μg by the LAL method.


 

Buffer : PBS, pH7.4


 

Description :


Dipeptidyl peptidase-IV (DPPIV) is also known as adenosine deaminase complexing protein 2, DPPIV or CD26 is antigenic enzyme expressed on the surface of most cell types and is associated with immune regulation, signal transduction and apoptosis. It is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides. The substrates of DPPIV are proline (or alanine)-containing peptides and include growth factors, chemokines, neuropeptides, and vasoactive peptides. DPPIV plays a major role in glucose metabolism. It is responsible for the degradation of incretins such as GLP-1. DPPIV plays an important role in tumor biology, and is useful as a marker for various cancers, with its levels either on the cell surface or in the serum increased in some neoplasms and decreased in others. DPPIV also binds the enzyme adenosine deaminase specifically and with high affinity. The significance of this interaction has yet to be established.


 

References :


(1) Kameoka J, et al.,1993, Science, 261 (5120): 466-9.
(2) Chen X, 2006, Adv. Exp. Med. Biol. 575: 27–32.
(3) Morimoto, C. et al., 1994, Proc. Natl. Acad. Sci. USA. 91: 9960-4.
(4) Havre PA, et al., 2008, Front. Biosci. 13: 1634–45.





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