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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.

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Common stock solution preparation

Table 1. Volume of DMSO needed to reconstitute specific mass of DABCYL succinimidyl ester [4-((4-(Dimethylamino)phenyl)azo)benzoic acid, succinimidyl ester] *CAS 146998-31-4* to given concentration. Note that volume is only for preparing stock solution. Refer to sample experimental protocol for appropriate experimental/physiological buffers.

0.1 mg0.5 mg1 mg5 mg10 mg
1 mM272.948 µL1.365 mL2.729 mL13.647 mL27.295 mL
5 mM54.59 µL272.948 µL545.896 µL2.729 mL5.459 mL
10 mM27.295 µL136.474 µL272.948 µL1.365 mL2.729 mL

Molarity calculator

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Spectrum

Citations

View all 1 citations: Citation Explorer
Protein N-terminal processing: substrate specificity of Escherichia coli and human methionine aminopeptidases
Authors: Xiao, Qing and Zhang, Feiran and Nacev, Benjamin A and Liu, Jun O and Pei, Dehua
Journal: Biochemistry (2010): 5588--5599

References

View all 34 references: Citation Explorer
Recombinant expression and partial characterization of an active soluble histo-aspartic protease from Plasmodium falciparum
Authors: Xiao H, Sinkovits AF, Bryksa BC, Ogawa M, Yada RY.
Journal: Protein Expr Purif (2006): 88
Internally quenched peptides for the study of lysostaphin: An antimicrobial protease that kills Staphylococcus aureus
Authors: Warfield R, Bardelang P, Saunders H, Chan WC, Penfold C, James R, Thomas NR.
Journal: Org Biomol Chem (2006): 3626
A quenched fluorescent dipeptide for assaying dispase- and thermolysin-like proteases
Authors: Weimer S, Oertel K, Fuchsbauer HL.
Journal: Anal Biochem (2006): 110
Characterization and inhibition of SARS-coronavirus main protease
Authors: Liang PH., undefined
Journal: Curr Top Med Chem (2006): 361
Fluorogenic peptide substrates containing benzoxazol-5-yl-alanine derivatives for kinetic assay of cysteine proteases
Authors: Szabelski M, Rogiewicz M, Wiczk W.
Journal: Anal Biochem (2005): 20
Page updated on October 12, 2024

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Physical properties

Molecular weight

366.37

Solvent

DMSO

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

Storage

Freeze (< -15 °C); Minimize light exposure
UNSPSC12352200

CAS

146998-31-4
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.
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.
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