IMG-EN-AS-29877-01.jpg
Peptides

MBP, MAPK Substrate, Biotinylated, Phosphorylated [Biotin-APR-pT-PGGRR] - 1 mg

$303.00
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  • Cat.Number : AS-29877
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This is an N-terminally biotinylated peptide, with a phosphorylated Thr97. The sequence APRTPGGRR contains a native sequence derived from bovine myelin basic protein amino acids 95-98 (PRTP). The rest of the sequence is not derived from a native sequence, but is a synthetic construct. APRTPGGRR is specific for MAP kinases: p44MAPK [extracellular signal-regulated kinase 1 (ERK1)] and p42MAPK (ERK2). It contains the consensus sequence Pro-X-(Ser/Thr)-Pro that is recognized by MAP kinase. APRTPGGRR is the most efficient substrate for phosphorylation reaction by ERK and is phosphorylated by kinases on threonine 97 and can also be phosphorylated by MAPK p38.

Specifications

Chemistry
Sequence one letter code
  • Biotin-APR-pT-PGGRR
Sequence three letter code
  • Biotin-Ala-Pro-Arg-pThr-Pro-Gly-Gly-Arg-Arg-OH
Molecular Formula
  • C49H85N20O16PS
Molecular Mass/ Weight
  • 1273.4
Modification
Conjugation type
  • Biotins
Modification Name
Conjugation
  • Conjugated
Quantity & Purity
Purity
  • Peak Area by HPLC ≥95%
Storage & stability
Form
  • Lyophilized
Storage Conditions
  • - 20 °C
Activity
Application
Biomarker Target
Research Area
Sub-category Research Area
Usage
  • Research use
Source
Source / Species
  • Synthetic construct

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References

A New Peptide Conjugate as a Highly Specific Substrate for MAP Kinase

J Biochem (Tokyo) . 1997 Jul 01 ; 122(1) 168 | DOI : 10.1093/oxfordjournals.jbchem.a021723

  • I. Kameshita
  • et al

Activation and Phosphorylation on Thr-160 of Nuclear-Targeted CDK2 Is ERK Dependent

Ann N. Y. Acad Sci . 2002 Nov 01 ; 973(1) 265 | DOI : https://doi.org/10.1111/j.1749-6632.2002.tb04646.x

  • NH. Lents
  • et al

MAP kinase 1/2 (Erk 1/2) and serine/threonine specific protein kinase Akt/PKB expression and activity in the human corpus cavernosum

Int J Impot Res . 2002 Aug 05 ; 14(4) 217 | DOI : https://doi.org/10.1038/sj.ijir.3900856

  • F. Sommer
  • et al