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Novel Reagent Using Spectrophotometry

Sensitive detection of iron (II) sulfate with a novel reagent using spectrophotometry

In this study, a novel reagent was developed for sensitive detection of iron (II) sulfate, spectrophotometrically. A novel thio-anthraquinone derivative, 1-(Dodecylthio)anthracene-9,10-dione (3), was synthesized from the chemical reaction of 1-Chloroanthraquinone (1) and 1-Dodecanethiol (2) by an original reaction method and was used in the preparation of the novel reagent called Catal’s reagent.
  • A synthesized thio-anthraquinone analogue (3) was purified by column chromatography, and its chemical structure was characterized by spectroscopic methods such as Fourier-transform infrared spectroscopy (FT-IR), nuclear magnetic resonance (NMR) spectroscopy, mass spectrometry (MS), and ultraviolet (UV)-visible spectrophotometry.
  • The chemical and molecular structure of the developed thio-antraquinone derivative (3) was illuminated using computational methods with the GaussView5 and Gaussian09 programs. Various solvents including ethanol, methanol, and acetonitrile were examined in the preparation of the reagent. A concentration range from 0.2 mg mL-1 up to 10 mg mL-1 of iron (II) sulfate heptahydrate solution in distilled water was prepared. The absorption spectra of Catal’s reagent (0.816 mM) showed three peaks between 185 nm-700 nm of wavelength.
  • However, after the reaction with H2O2 and the 30 mM trisodium citrate dihydrate mixture in the presence of an iron sulfate (II) solution, a single peak was observed, producing a stable and reddish/brownish homogenous solution (λ max = 304 nm).
  • The following concentrations of iron (II) sulfate heptahydrate was examined using developed protocol and the reagent, and the concentrations were measured spectrophotometrically at 304 nm, 0.2-1 mg mL-1. Absorbances of reaction mixtures of iron (II) sulfate remained stable up to 48 h.
  • The results indicated that the novel Catal’s reagent can be used for sensitive spectrophotometric detection of iron (II) sulfate in aqueous solutions.
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61R-1220 100 ug
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Description: Rat monoclonal CD20 antibody (PE)

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NATtrol Zika Virus Stock (Qualitative) (1 mL)
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human CD20/MS4A1 linear peptide (165-184, 20-aa, extracellular domain) broad reactivity with CD20-specific antibodies
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B-Lymphocyte Antigen CD20 (CD20) Antibody (PE)
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B-Lymphocyte Antigen CD20 (CD20) Antibody (PE-Cy5)
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Humanized (chimeric) Anti-Human CD20/MS4A1 IgG (rituximab biosimilar), pure
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Anti-Hu CD20 PE-DyLight594
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B-Lymphocyte Antigen CD20 (CD20) Antibody (PE-DyLight 594)
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Recombinant (HEK cells) human CD20/MS4A1 (141-184 aa) hFc- fusion Protein
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Recombinant (HEK cells) purified human CD20/MS4A1 (213-297 aa) His-tag Protein
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Rabbit Anti-Human CD20/MS4A1 peptide (EC-domain, rituximab binding domain) IgG, aff pure
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CD20/MS4A1 linear peptide (QDKLTQWPKWLEg, 13-aa) contains WPXWLE motif and reacts with rituximab
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Goat Anti-Camel IgG-RPE conjugate
30835-RPE 0.5 ml
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BI 6015
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BI-847325
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BI-9564
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BI-9564
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BI-D1870
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BI-D1870
B2227-5.1 10 mM (in 1mL DMSO)
EUR 235
Description: BI-D1870 is a cell-permeable inhibitor of the p90 RSK isoforms with IC50 values of 31nM, 24nM, 18nM and 15nM for RSK1, RSK2, RSK3 and RSK4 respectively [1].BI-D1870 is a derivative of dihydropteridinone and found to be a remarkably specific inhibitor of RSK isoforms.

BI-D1870
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BI 78D3
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Description: BI-78D3 is a substrate competitive inhibitor of JNK inhibitor [2].JNK is a member of the MAPK family. JNK is a stress-activated protein kinase that modulates pathways implicated in a variety of disease states.

BI 78D3
B9011-100 100 mg
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Description: BI-78D3 is a substrate competitive inhibitor of JNK inhibitor [2].JNK is a member of the MAPK family. JNK is a stress-activated protein kinase that modulates pathways implicated in a variety of disease states.

BI 78D3
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Description: BI-78D3 is a substrate competitive inhibitor of JNK inhibitor [2].JNK is a member of the MAPK family. JNK is a stress-activated protein kinase that modulates pathways implicated in a variety of disease states.

BI 78D3
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BI 78D3
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EUR 183
Description: BI-78D3 is a substrate competitive inhibitor of JNK inhibitor [2].JNK is a member of the MAPK family. JNK is a stress-activated protein kinase that modulates pathways implicated in a variety of disease states.

BI 78D3
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BI 2536
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EUR 224
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BI 2536
A3965-5 5 mg
EUR 148
Description: BI 2536 is a potent, ATP-competitive, well tolerated and highly specific human polo-like kinase 1 (PLK1) inhibitor with IC value of 0.83 nM, which shows 1000-fold selectivity against other kinases [1].

BI 2536
A3965-5.1 10 mM (in 1mL DMSO)
EUR 195
Description: BI 2536 is a potent, ATP-competitive, well tolerated and highly specific human polo-like kinase 1 (PLK1) inhibitor with IC value of 0.83 nM, which shows 1000-fold selectivity against other kinases [1].

BI 2536
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EUR 595
Description: BI 2536 is a potent, ATP-competitive, well tolerated and highly specific human polo-like kinase 1 (PLK1) inhibitor with IC value of 0.83 nM, which shows 1000-fold selectivity against other kinases [1].

BI 2536
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Engineering caspase 7 as an affinity reagent to capture proteolytic products

Many proteases recognize their substrates with high specificities, with this in mind, it should theoretically be possible to utilize the substrate binding cleft of a protease as a scaffold to engineer an affinity reagent. In this study, we sought to develop reagents that would differentiate between substrates and products of proteolysis, based on a caspase 7 scaffold. Firstly, we engineered a form of caspase 7 that can undergo conversion to a substrate binding conformation without catalysis. Seeking to generate a product-only trap, we further engineered this construct by incorporating mutations that compensate for the generation of a negative charge in the neo C terminus of a newly generated product.
  • This was accomplished with only three substitutions within the substrate binding cleft. Moreover, the affinity of the product trap for peptides was comparable to the affinity of caspase 7 to parental substrates.
  • Finally, generation of a hybrid fluorescent protein with the product trap provided a reagent that specifically recognized apoptotic cells and highlights the versatility of such an approach in developing affinity and imaging agents for a variety of cysteine and serine proteases.

Leveraging nature’s biomolecular designs in next-generation protein sequencing reagent development

Next-generation approaches for protein sequencing are now emerging that could have the potential to revolutionize the field in proteomics. One such sequencing method involves fluorescence-based imaging of immobilized peptides in which the N-terminal amino acid of a polypeptide is readout sequentially by a series of fluorescently labeled biomolecules.

When selectively bound to a specific N-terminal amino acid, the NAAB (N-terminal amino acid binder) affinity reagent identifies the amino acid through its associated fluorescence tag. A key technical challenge in implementing this fluoro-sequencing approach is the need to develop NAAB affinity reagents with the high affinity and selectivity for specific N-terminal amino acids required for this biotechnology application.

One approach to develop such a NAAB affinity reagent is to leverage naturally occurring biomolecules that bind amino acids and/or peptides. Here, we describe several candidate biomolecules that could be considered for this purpose and discuss the potential for developability of each.

Key points • Next-generation sequencing methods are emerging that could revolutionize proteomics. • Sequential readout of N-terminal amino acids by fluorescent-tagged affinity reagents. • Native peptide/amino acid binders can be engineered into affinity reagents. • Protein size and structure contribute to feasibility of reagent developability.

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