protein

Recombinant human CD26/DPP4 protein

DPP0901

20 ug

105 USD

Recombinant human CD26/DPP4 protein

39-766aa

DPP0901

NP_001926.2

DPP4, dipeptidyl peptidase-4 is a complex enzyme expressed on the surface of most cell types and is a serine exopeptidase that cleaves x-proline dipeptides from the N-terminus of polypeptides. DPP4 protein is associated with intracellular signal transduction, apoptosis and plays an important role in tumor biology. There are at least 63 substrates which can bind specifically to DPP4 enzyme including growth factors, chemokines, neuro peptides. Furthermore, DPP4 plays a major role in glucose metabolism by cleaving incretins such as glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1). Recombinant human DPP4 protein was expressed with c-terminal His-tag in high-5 cells using baculovirus expression system and purified by using conventional chromatography techniques.

Dipeptidyl peptidase 4, dipeptidyl peptidase 4 isoform 1, ADABP, ADCP2, CD26, DPPIV, TP103, Adenosine deaminase complexing protein 2, Dipeptidyl peptidase IV, DPP4, T-cell activation antigen CD26

0.5mg/ml (determined by absorbance at 280nm)

Liquid in. 20mM Tris-HCl buffer (pH 8.0) containing 100mM NaCl, 1mM EDTA, 10% glycerol

Can be stored at +2C to +8C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Pratley RE and Salsali A. (2007) Curr Med Res Opin. 23(4):919-31.;; Rosenstock J. and Zinman B. (2007) Curr Opin Endocrino Diabetes Obes.60(11):1454-70.;; Barnett A. (2006). J.Clin. Pract. 60(11):1454-70.;;

> 95% by SDS-PAGE

Specific activity is > 200unit/mg, One unit produces 1.0 umole of p-Nitroaniline from Gly-Pro- p-Nitroaniline per minute at pH 8.0 at 37C.

SDS-PAGE, Enzyme Activity

Human

Enzymes & Proteases

85.4 kDa (737aa) confirmed by MALDI-TOF

< 1 EU per 1ug of protein (determined by LAL method)

Specific activity is > 200 units/mg, One unit produces 1.0 umole of p-Nitroaniline from Gly-Pro- p-Nitroaniline per minute at pH 8.0 at 37C.

SRKTYTL TDYLKNTYRL KLYSLRWISD HEYLYKQENN ILVFNAEYGN SSVFLENSTF DEFGHSINDY SISPDGQFIL LEYNYVKQWR HSYTASYDIY DLNKRQLITE ERIPNNTQWV TWSPVGHKLA YVWNNDIYVK IEPNLPSYRI TWTGKEDIIY NGITDWVYEE EVFSAYSALW WSPNGTFLAY AQFNDTEVPL IEYSFYSDES LQYPKTVRVP YPKAGAVNPT VKFFVVNTDS LSSVTNATSI QITAPASMLI GDHYLCDVTW ATQERISLQW LRRIQNYSVM DICDYDESSG RWNCLVARQH IEMSTTGWVG RFRPSEPHFT LDGNSFYKII SNEEGYRHIC YFQIDKKDCT FITKGTWEVI GIEALTSDYL YYISNEYKGM PGGRNLYKIQ LSDYTKVTCL SCELNPERCQ YYSVSFSKEA KYYQLRCSGP GLPLYTLHSS VNDKGLRVLE DNSALDKMLQ NVQMPSKKLD FIILNETKFW YQMILPPHFD KSKKYPLLLD VYAGPCSQKA DTVFRLNWAT YLASTENIIV ASFDGRGSGY QGDKIMHAIN RRLGTFEVED QIEAARQFSK MGFVDNKRIA IWGWSYGGYV TSMVLGSGSG VFKCGIAVAP VSRWEYYDSV YTERYMGLPT PEDNLDHYRN STVMSRAENF KQVEYLLIHG TADDNVHFQQ SAQISKALVD VGVDFQAMWY TDEDHGIASS TAHQHIYTHM SHFIKQCFSL P

His-Tag

Baculovirus

Ala

Recombinant Protein

P27487

TP103, T-cell activation antigen CD26, DPPIV, DPP4, Dipeptidylpeptidase IV (CD26 adenosine deaminase complexing protein 2), Dipeptidyl-peptidase 4, Dipeptidyl peptidase-4, Dipeptidyl peptidase 4, CD26, Adenosine deaminase complexing protein 2, ADCP2, ADABP, DPP0901-10ug, DPP0901-20ug, DPP0901-50ug, DPP0901-100ug, DPP0901-250ug, DPP0901-500ug, DPP0901-1mg, DPP0901-010, DPP0901-020, DPP0901-050, DPP0901-100, DPP0901-250, DPP0901-500, DPP0901-01M

Hussein GM, et al. Mate tea (Ilex paraguariensis) promotes satiety and body weight lowering in mice: involvement of glucagon-like peptide-1. (Biol Pharm Bull. 2011){https://pubmed.ncbi.nlm.nih.gov/22130241/};;Sato Y, et al. The role of dipeptidyl peptidase 4 (DPP4) in the preservation of renal function: DPP4 involvement in hemoglobin expression. (J Endocrinol. 2014){https://pubmed.ncbi.nlm.nih.gov/25122001/};;Roppongi S, et al. Crystal structures of a bacterial dipeptidyl peptidase IV reveal a novel substrate recognition mechanism distinct from that of mammalian orthologues. (Sci Rep. 2018){https://pubmed.ncbi.nlm.nih.gov/29426867/};;Guan C, et al. Strategic Preparations of DPP-IV Inhibitory Peptides from Val-Pro-Xaa and Ile-Pro-Xaa Peptide Mixtures. (Int J Pept Res Ther. 2020){https://pubmed.ncbi.nlm.nih.gov/25122001/};;Guan C, et al. Exploration of DPP-IV Inhibitory Peptide Design Rules Assisted by the Deep Learning Pipeline That Identifies the Restriction Enzyme Cutting Site. (ACS Omega. 2023){https://pubmed.ncbi.nlm.nih.gov/37901493/}