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DABCYL succinimidyl ester
4-((4-(Dimethylamino)phenyl)azo)benzoic acid, succinimidyl ester; CAS 146998-31-4
DABCYL, SE is the amino-reactive form of DABCYL, and widely used to prepare a variety of FRET-based probes that contain DABCYL. DABCYL is one of the most popular acceptors for developing FRET-based nucleic acid probes and protease substrates.
Methionine aminopeptidase (MetAP) catalyzes the hydrolytic cleavage of the N-terminal methionine from newly synthesized polypeptides. The extent of removal of methionyl from a protein is dictated by its N-terminal peptide sequence. Earlier studies revealed that MetAPs require amino acids containing small side chains (e.g., Gly, Ala, Ser, Cys, Pro, Thr, and Val) as the P1&prime; residue, but their specificity at positions P2&prime; and beyond remains incompletely defined. In this work, the substrate specificities of <em>Escherichia coli</em> MetAP1, human MetAP1, and human MetAP2 were systematically profiled by screening against a combinatorial peptide library and kinetic analysis of individually synthesized peptide substrates. Our results show that although all three enzymes require small residues at the P1&prime; position, they have differential tolerance for Val and Thr at this position. The catalytic activity of human MetAP2 toward Met-Val peptides is consistently 2 orders of magnitude higher than that of MetAP1, suggesting that MetAP2 is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences <em>in vivo</em>. At positions P2&prime;&minus;P5&prime;, all three MetAPs have broad specificity but are poorly active toward peptides containing a proline at the P2&prime; position. In addition, the human MetAPs disfavor acidic residues at the P2&prime;&minus;P5&prime; positions. The specificity data have allowed us to formulate a simple set of rules that can reliably predict the N-terminal processing of <em>E. coli</em> and human proteins. Source: <strong>Protein N-Terminal Processing: Substrate Specificity of Escherichia coli and Human Methionine Aminopeptidases</strong> by Xiao et al., <em>ACS Publications</em>, June 2010.
Methionine aminopeptidase (MetAP) catalyzes the hydrolytic cleavage of the N-terminal methionine from newly synthesized polypeptides. The extent of removal of methionyl from a protein is dictated by its N-terminal peptide sequence. Earlier studies revealed that MetAPs require amino acids containing small side chains (e.g., Gly, Ala, Ser, Cys, Pro, Thr, and Val) as the P1&prime; residue, but their specificity at positions P2&prime; and beyond remains incompletely defined. In this work, the substrate specificities of <em>Escherichia coli</em> MetAP1, human MetAP1, and human MetAP2 were systematically profiled by screening against a combinatorial peptide library and kinetic analysis of individually synthesized peptide substrates. Our results show that although all three enzymes require small residues at the P1&prime; position, they have differential tolerance for Val and Thr at this position. The catalytic activity of human MetAP2 toward Met-Val peptides is consistently 2 orders of magnitude higher than that of MetAP1, suggesting that MetAP2 is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences <em>in vivo</em>. At positions P2&prime;&minus;P5&prime;, all three MetAPs have broad specificity but are poorly active toward peptides containing a proline at the P2&prime; position. In addition, the human MetAPs disfavor acidic residues at the P2&prime;&minus;P5&prime; positions. The specificity data have allowed us to formulate a simple set of rules that can reliably predict the N-terminal processing of <em>E. coli</em> and human proteins. Source: <strong>Protein N-Terminal Processing: Substrate Specificity of Escherichia coli and Human Methionine Aminopeptidases</strong> by Xiao et al., <em>ACS Publications</em>, June 2010.
CatalogSize
Price
Quantity
20041 g
Price
20055 g
Price
 
Physical properties

Molecular weight366.37
SolventDMSO
Spectral properties

Absorbance (nm)454
Correction factor (280 nm)0.516
Storage, safety and handling

H-phraseH303, H313, H333
Hazard symbolXN
Intended useResearch Use Only (RUO)
R-phraseR20, R21, R22
StorageFreeze (< -15 °C); Minimize light exposure
UNSPSC12352200
CAS146998-31-4
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Page updated on October 13, 2025