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    AcSDKP ELISA kit
  • AcSDKP ELISA kit
Cat No: A05881
Assay Kits - Elisa
Bertin Bioreagent

Enzyme ImmunoAssay (EIA) is a technique to detect and quantify antigens (proteins, hormones…) or antibodies in samples. It relies on the ability of an antibody to bind a specific antigen. Either the antibody or the antigen is labelled with an enzyme wh...

: 96 wells

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Territorial Availability: Available worldwide directly through Bertin or your local distributor
Technical Warning: Check the Additional Items Required section of this kit booklet to verify if UltraPure Water (Milli-Q or equivalent) is needed for this assay
  • Ac-SDKP
  • Acetyl-SDKP
  • N-acetyl-seryl-aspartyl-lysyl-proline
  • Acetyl-Ser-Asp-Lys-Pro
  • seraspenide
  • goralatide
  • 589451
Correlated keywords:
  • Hematopoiesis
  • S-phase
  • Angiogenesis
  • thymosin β4
  • Tβ4
  • fibrosis
  • serine
  • aspartamine
Show more...
Product Overview:
Enzyme ImmunoAssay (EIA) is a technique to detect and quantify antigens (proteins, hormones…) or antibodies in samples. It relies on the ability of an antibody to bind a specific antigen. Either the antibody or the antigen is labelled with an enzyme whose substrate is a chromogen or a fluorogen converted in a measurable product (color or fluorescence).
Enzyme-linked Immunosorbent Assay (ELISA) is a type of EIA using a solid phase (ex: microtiter plate) coated with an antigen immobilizing the molecule to detect. Over the time, scientists have extended the term ELISA to EIAs using an antibody coating the solid phase. That explains why our EIA kits using coated antibodies are also called ELISA kits.
AcSDKP is a new reliability marker of chronic ACE inhibition. The tetrapeptide N-acetyl-seryl-aspartyl-lysyl-proline (AcSDKP) is an endogenous regulatory factor of hematopoiesis which reverses stem cells and normal early progenitors into S-phase. Angiotensin I-Converting Enzyme (ACE) has two homologous active NH2- and COOH-terminal domains and displays activity toward a broad range of substrates. The AcSDKP has been shown to be hydrolyzed by ACE and to be a preferential substrate for its NH2-terminal active site. In healthy subjects, the acute administration of the ACE inhibitor captopril increases the AcSDKP plasma levels. Several studies aimed to measure plasma or urine AcSDKP levels during treatment with various ACE inhibitors and to confirm its relevance as a marker of ACE inhibition.
Size 96 wells
Shipping Dry ice
Specificity Show more...
Application Media Plasma, urine and blood cells|Blood collection with captoprill.|Plasma/serum: purification using methanol precipitation.|Blood Cells: methanol precipitation.|Urine: no extraction required.
Sample volume 50 µL
Tracer AcetylCholinesterase AChE
Detection Limit 0,1 nM
Custom Code 3822000000
UNSPSC code 41116104


Struthers A.D., McFayden R. et al. Non adherence with ACE inhibitor therapy: a comparison of different ways of measuring it with observations on its frequency in heart failure. JACC, 1999, 34, 2072-2077.

Azizi M., Rousseau A., Ezan E. et al. Acute angiotensin-converting enzyme inhibition increases the plasma level of the natural stem cell regulator N-acetyl-seryl-aspartyl-lysyl-proline. J Clin Invest. 1996 Feb 1, 97(3), 839-44.

Lenfant M., Wdzieczak-Bakala J., Guittet E. et al. Inhibitor of hematopoietic pluripotent stem cell proliferation: purification and determination of its structure. Proc. Natl. Acad. Sci. USA. 86: 779–782 (1989)

Bonnet D., Lemoine F. M., Ponvert-Delucq S. et al. Direct and reversible inhibitory effect of the tetrapeptide acetyl-N-Ser-Asp-Lys-Pro (Serapenide) on the growth of human CD34+ subpopulations in response to growth factors. Blood. 82:3307–3314 (1993)

Rousseau A., Michaud A., Chauvet M.-T. et al. The hemoregulatory peptide N-Acetyl-Ser-Asp-Lys-Pro is a natural and specific substrate of the N-terminal active site of human angiotensin-converting enzyme. J. Biol. Chem. 270:3656–3661 (1995)

Azizi M., Ezan E., Reny J.L. et al. Renal and metabolic clearance of N-acetyl-seryl-aspartyl-lysyl-proline (AcSDKP) during angiotensin-converting enzyme inhibition in human. Hypertension. 1999 Mar, 33(3), 879-86

Azizi M., Ezan E., Nicolet L. et al. High plasma level of N-acetyl-seryl-aspartyl-lysyl-proline: a new marker of chronic angiotensin-converting enzyme inhibition. Hypertension. 1997 Nov, 30(5),1015-9

Pradelles Ph., Frobert Y., Créminon C., et al. Distribution of a negative regulator of haematopoietic stem cell proliferation (AcSDKP) and thymosin ß4 in mouse tissues. FEBS 10125, 1991, 289(2), 171-175

Pradelles P., Frobert Y., Créminon C., et al. Negative regulator of pluripotent hematopoiectic stem cell proliferation in human white blood cells and plasma as analysed by enzyme immunoassay. Bioch. Bioph. Res. Com., 1990, August 16, 170-3, 986-993

Junot C., Nicolet L., Ezan E. et al. Effect of Angiotensin-Converting Enzyme Inhibition on Plasma, Urine, and Tissue Concentrations of Hemoregulatory Peptide Acetyl-Ser-Asp-Lys-Pro in Rats. JPET 291:982-987,1999


Zhou D., Wang J., HE L.N. et al.Prolyl oligopeptidase attenuates hepatic stellate cell activation through induction of Smad7 and PPAR‑γ. Experimental and Therapeutic Medicine , 13, 780-786 (2017)

Chan G. C. W., Yiu W.H., Wu H.J. N-Acetyl-seryl-aspartyl-lysyl-proline Alleviates Renal Fibrosis Induced by Unilateral Ureteric Obstruction in BALB/C Mice. Hindawi Publishing Corporation, Mediators of Inflammation, Volume 2015, Article ID 283123

Ntsekhe M. , Matthews K., Wolske J. A Pilot Study of Ac-SDKP (N-acetyl-seryl-aspartyl-lysyl-proline) and Galectin-3 Levels in Normal Pericardial Fluid and Tuberculous Pericardial Effusion: Implications for Pathogenesis and Prevention of Pericardial Constriction. Heart. 2012 September ; 98(17): 1326–1328

Srivastava S.P., Shi S., Kanasaki M. et al. Effect of Antifibrotic MicroRNAs Crosstalk on the Action of N-acetyl-seryl-aspartyl-lysyl-proline in Diabetes-related Kidney Fibrosis. Sci Rep. 2016; 6: 29884

Myohanen TT., Tenorio-Laranga J., Jokinen B. et al. Prolyl oligopeptidase induces angiogenesis both in vitro and in vivo in a novel regulatory manner. British Journal of Pharmacology (2011) 163 1666–1678

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