146987-10-2

Basic information

• Product Name: FMOC-LYS(BIOTIN)-OH
• Synonyms: FMOC-LYS(BIOTIN)-OH 95+%;Fmoc-Lys(Biotin)-OH(N-a-Fmoc-N-e-(d-Biotin)-L-lysine;nα-fmoc-nε-biotinyl-l-lysine;ε-Biotinoyl-α-(9-fluorenylmethoxycarbonyl)-L-lysine;Fmoc-Lys(biotinyl)-OH, Nα-Biotinyl-Nε-Fmoc-L-lysine;N-(9-Fluorenylmethyloxycarbonyl)-N'-biotinyl-L-lysine;N^a-Biotinyl-N^e-FMoc-L-lysine, 95%;Nα-FMoc-Nε-biotinyl-L-lysine
• CAS NO: 146987-10-2
• Molecular Formula: C₃₁H₃₈N₄O₆S
• Molecular Weight: 594.72
• Product Categories: Amino Acids
• Mol File: 146987-10-2.mol
• Article Data: 5

Chemical Properties

• Melting Point: 178-180 °C(Solv: methanol (67-56-1); N,N-dimethylformamide (68-12-2))
• Boiling Point: 936.166 °C at 760 mmHg
• Flash Point: 519.974 °C
• Appearance: /Solid
• Density: 1.272 g/cm³
• Storage Temp.: -15°C
• Solubility: DMSO (Slightly, Heated)
• PKA: 3.88±0.21(Predicted)
• Water Solubility: Slightly soluble in water and dimethyl sulfoxide.
• CAS DataBase Reference: FMOC-LYS(BIOTIN)-OH(CAS DataBase Reference)
• NIST Chemistry Reference: FMOC-LYS(BIOTIN)-OH(146987-10-2)
• EPA Substance Registry System: FMOC-LYS(BIOTIN)-OH(146987-10-2)

Safety Data

• Safety Statements: 22-24/25
• WGK Germany: 3
• F: 10
• Hazardous Substances Data: 146987-10-2(Hazardous Substances Data)

Usage

Chemical Properties

Beige powder

Uses

Nα-Fmoc-Nε-biotinyl-L-lysine is useful in the synthesis of site-specific biotinylated probes.

Upstream product

• 58-85-5 biotin 
• 105047-45-8 Fmoc-Lys-OH 
• 71989-26-9 Fmoc-Lys(tert-butoxycarbonyl) 
• 35013-72-0 biotin N-Hydroxysuccinimide ester 

Downstream Products

• 576-19-2 biocytin 

Relevant articles and documents

Identification of Pyruvate Carboxylase as the Cellular Target of Natural Bibenzyls with Potent Anticancer Activity against Hepatocellular Carcinoma via Metabolic Reprogramming

Cancer cell proliferation in some organs often depends on conversion of pyruvate to oxaloacetate via pyruvate carboxylase (PC) for replenishing the tricarboxylic acid cycle to support biomass production. In this study, PC was identified as the cellular target of erianin using the photoaffinity labeling-click chemistry-based probe strategy. Erianin potently inhibited the enzymatic activity of PC, which mediated the anticancer effect of erianin in human hepatocellular carcinoma (HCC). Erianin modulated cancer-related gene expression and induced changes in metabolic intermediates. Moreover, erianin promotes mitochondrial oxidative stress and inhibits glycolysis, leading to insufficient energy required for cell proliferation. Analysis of 14 natural analogs of erianin showed that some compounds exhibited potent inhibitory effects on PC. These results suggest that PC is a cellular target of erianin and reveal the unrecognized function of PC in HCC tumorigenesis; erianin along with its analogs warrants further development as a novel therapeutic strategy for the treatment of HCC.

Target Identification of Kinase Inhibitor Alisertib (MLN8237) by Using DNA-Programmed Affinity Labeling

Accurate identification of the molecular targets of bioactive small molecules is a highly important yet challenging task in biomedical research. Previously, a method named DPAL (DNA-programmed affinity labeling) for labeling and identifying the cellular targets of small molecules and nucleic acids was developed. Herein, DPAL is applied for the target identification of Alisertib (MLN8237), which is a highly specific aurora kinase A (AKA) inhibitor and a drug candidate being tested in clinical trials for cancer treatment. Apart from the well-established target of AKA, several potential new targets of MLN8237 were identified. Among them, p38 mitogen-activated protein kinase (p38) and laminin receptor (LAMR) were validated to be implicated in the anticancer activities of MLN8237. Interestingly, these new targets were not identified with non-DNA-based affinity probes. This work may facilitate an understanding of the molecular basis of the efficacy and side effects of MLN8237 as a clinical drug candidate. On the other hand, this work has also demonstrated that the method of DPAL could be a useful tool for target identification of bioactive small molecules.

Activity-based high-throughput profiling of metalloprotease inhibitors using small molecule microarrays

We herein describe a high-throughput small molecule microarray (SMM) method that enables quick and cost-effective identification of potent inhibitors of metalloproteases in an activity-dependent manner, thereby offering a rapid means for inhibitor discove