138529-46-1

Basic information

• Product Name: N-BIOTINYL-3,6-DIOXAOCTANE-1,8-DIAMINE
• Synonyms: N-BIOTINYL-3,6-DIOXAOCTANE-1,8-DIAMINE;Biotin-PEG3-amine;Biotin-PEG2-aMine;1H-Thieno[3,4-d]iMidazole-4-pentanaMide, N-[2-[2-(2-aMinoethoxy)ethoxy]ethyl]hexahydro-2-oxo-, (3aS,4S,6aR)-;(+)-Biotinyl-3,6-dioxaoctanediaMine(AMine-PEG2-Biotin);(+)-Biotin-(PEO)3-aMine;(+)-Biotinyl-3,6-dioxaoctanediamine;(+)-Biotin-PEG2-aMine
• CAS NO: 138529-46-1
• Molecular Formula: C₁₆H₃₀N₄O₄S
• Molecular Weight: 374.5
• Mol File: 138529-46-1.mol
• Article Data: 27

Chemical Properties

• Melting Point: 109-110℃
• Boiling Point: 689.4±55.0 °C(Predicted)
• Appearance: /
• Density: 1.172±0.06 g/cm3(Predicted)
• Storage Temp.: Keep in dark place,Inert atmosphere,Store in freezer, under -20°C
• Solubility: Soluble in Water, DMSO, DMF
• PKA: 13.90±0.40(Predicted)
• CAS DataBase Reference: N-BIOTINYL-3,6-DIOXAOCTANE-1,8-DIAMINE(CAS DataBase Reference)
• NIST Chemistry Reference: N-BIOTINYL-3,6-DIOXAOCTANE-1,8-DIAMINE(138529-46-1)
• EPA Substance Registry System: N-BIOTINYL-3,6-DIOXAOCTANE-1,8-DIAMINE(138529-46-1)

Safety Data

• Hazardous Substances Data: 138529-46-1(Hazardous Substances Data)

Usage

Description

N-BIOTINYL-3,6-DIOXAOCTANE-1,8-DIAMINE, also known as Biotin-PEG2-amine, is a biotinylation agent that can react with NHS ester or carboxylic acid in the presence of EDC or HATU. It is a versatile molecule with a biotin group, PEG2 spacer, and amine functionality, which allows for various applications in different industries.

Uses

Used in Biochemical Research:
N-BIOTINYL-3,6-DIOXAOCTANE-1,8-DIAMINE is used as a biotinylation reagent for the modification of biomolecules such as proteins, peptides, and nucleic acids. The biotin group provides a handle for detection, purification, or immobilization of the modified biomolecules on streptavidin-coated surfaces.
Used in Drug Delivery Systems:
In the pharmaceutical industry, N-BIOTINYL-3,6-DIOXAOCTANE-1,8-DIAMINE is used as a targeting ligand for the development of targeted drug delivery systems. The biotin group can be utilized to specifically bind to receptors or other biomolecules overexpressed in diseased cells, enhancing the selectivity and efficacy of the drug delivery system.
Used in Diagnostics:
N-BIOTINYL-3,6-DIOXAOCTANE-1,8-DIAMINE is used as a detection agent in diagnostic assays, such as immunoassays and molecular diagnostics. The biotin group can be used to label antibodies, enzymes, or other detection molecules, allowing for the specific detection of target analytes through the formation of a biotin-streptavidin complex.
Used in Chemical Synthesis:
In the field of chemical synthesis, N-BIOTINYL-3,6-DIOXAOCTANE-1,8-DIAMINE is used as a building block for the synthesis of more complex biotinylated molecules, such as biotinylated polymers, dendrimers, and other macromolecules with potential applications in various industries.
Used in Material Science:
In material science, N-BIOTINYL-3,6-DIOXAOCTANE-1,8-DIAMINE can be used as a functional component in the development of biotinylated materials with specific properties, such as self-assembly, recognition, or sensing capabilities. The biotin group can be exploited to create materials with tailored interactions with biological systems or other functional components.

Upstream product

• 101187-31-9 (3aS,4S,6aR)-4-[5-(1H-imidazol-1-yl)-5-oxopentyl]tetrahydro-1H-thieno-[3,4-d]imidazol-2(3H)-one 
• 929-59-9 3,6-dioxa-1,8-diaminooctane 
• 153086-78-3 tert-butyl {2-[2-(2-aminoethoxy)ethoxy]ethyl}carbamate 
• 58-85-5 biotin 
• 35013-72-0 biotin N-Hydroxysuccinimide ester 
• 120550-35-8 biotin pentafluorophenyl ester 
• 109-73-9 N-butylamine 
• 175885-18-4 tert-butyl-N-(2-(2-(2-(5-(2-oxo-1,3,3a,4,6,6a-hexahydrothieno(3,4-d)imidazol-6-yl)pentanoylamino)ethoxy)ethoxy)ethyl)carbamate 

Downstream Products

• 1011268-29-3 C₂₂H₃₉N₇O₅S 
• 1011268-28-2 C₂₂H₃₆N₄O₅S 
• 1166232-56-9 N₅-[2-(N₃-{2-[2-(2-biotinylaminoethoxy)ethoxy]ethyl}-N₂-fluorenylmethyloxycarbonylguanidino)ethylcarbonyl]-N₁-(tritylaminooxyacetyl)-1,5-diaminonaphthalene 
• 1166232-73-0 1-(N₃-{2-[2-(2-biotinylaminoethoxy)ethoxy]ethyl}-N₂-fluorenylmethyloxycarbonylguanidino)-N₅-(tritylaminooxyacetyl)-5-aminonaphthalene 
• 1559003-54-1 C₃₈H₅₈N₈O₁₄S₂ 
• 1426247-01-9 C₆₃H₉₇N₉O₁₁S 
• 1426246-95-8 C₅₆H₉₃N₉O₁₀S 
• 1212057-35-6 N-biotinyl-N′-(3-(4-phenylthiocarbonylthio-4-cyanovaleryl)-3,6-dioxaoctane-1,8-diamine) 

Relevant articles and documents

A Chemical Probe for Protein Crotonylation

Protein lysine crotonylation has emerged as an important post-translational modification (PTM) in the regulation of gene transcription through epigenetic mechanisms. Here we introduce a chemical probe, based on a water-soluble phosphine warhead, which reacts with the crotonyl modification. We show that this reagent is complementary to antibody-based tools allowing detection of endogenous cellular proteins such as histones carrying the crotonylation PTM. The tool is also used to show that the histone acylation activity of the transcriptional coactivator, p300, can be activated by pre-existing lysine crotonylation through a positive feedback mechanism. This reagent provides a versatile and sensitive probe for the analysis of this PTM.

Characterization of streptavidin binding to biotinylated, binary self-assembled thiol monolayers - Influence of component ratio and solvent

Many biosensor applications are based on streptavidin (SA) binding to partially biotinylated self-assembled thiol monolayers (SAMs). In our study, binary SAMs on gold were prepared from solutions containing 16-mercapto-1- hexadecanol (thiol I) and N-(8-biotinyl-3,6-dioxa-octanamidyl)-16- mercaptohexadecanamide (thiol II) in varying component ratios. Either chloroform or ethanol was used as solvent. After 24 h thiol incubation, SA was immobilized on the resulting SAMs using the strong SA-biotin interaction. The SA binding process was monitored by QCM-D (quartz crystal microbalance monitoring dissipation factor). It is shown that the Sauerbrey equation is valid to calculate the mass quantities of the immobilized SA layers. Under the chosen incubation conditions, marginal fractions of the biotinylated component II in chloroform ((nI/nII)solution ≈ 1000) lead to SAMs which ensure a maximal SA binding quantity of mSauerbrey SA ≈ 400 ngcm-2, being equivalent to a SA single-layer arrangement on the SAM surface. In case of incubations from ethanolic solutions, a complete SA layer formation needs significantly higher amounts of the biotinylated component II during SAM preparation ((nI/nII) solution ≈ 50). X-ray photoelectron spectroscopy data show that the fraction of biotinylated thiol II in the SAM determines the amount of surface-bound SA. The SAM thiol ratio ((nI/nII) SAM) not only depends on the corresponding component ratio in the incubation solution, but is also strongly influenced by the solvent. Using chloroform as solvent during SAM preparation significantly increased the fraction of biotinylated thiol II in the SAMs compared to ethanol.

A trifunctional cyclooctyne for modifying azide-labeled biomolecules with photocrosslinking and affinity tags

A bicyclo[6.1.0]nonyne (BCN)-based cyclooctyne reagent bearing a photocrosslinking diazirine (DAz) group and a biotin affinity handle, BCN-DAz-Biotin, is reported. BCN-DAz-Biotin is capable of simultaneously delivering photocrosslinking and affinity tags to azide-labeled biomolecules, enabling photoactivated capture and enrichment/detection of interacting species in native contexts.

N-terminal labeling of proteins by the Pictet-Spengler reaction

The Pictet-Spengler reaction was applied to the N-terminal labeling of horse heart myoglobin. This was performed in the following two steps: (1) conversion of the N-terminal glycine residue to an α-keto aldehyde by a transamination reaction and (2) condensation of the resulting activated myoglobin with tryptamine analogues by the Pictet-Spengler reaction. Ultraviolet (UV)/visible (vis) absorption and circular dichroism (CD) spectral data revealed that the tertiary structure of myoglobin was not altered by the Pictet-Spengler reaction.

Scutellarin inhibits Hela cell growth and glycolysis by inhibiting the activity of pyruvate kinase M2

Scutellarin, one of natural flavonoids, is widely and clinically used for treating many diseases in China. Recently, scutellarin has demonstrated a broad spectrum of anti-proliferative activities against multiple cancer cell lines. However, the molecular mechanism of action remains to be investigated. We herein report the design and synthesis of biotinylated scutellareins as probes, which can be applied to discover scutellarein interacting proteins. Finally, we show that scutellarin directly targets pyruvate kinase M2 (PKM2) and inhibits its cytosolic activity to decrease glycolytic metabolism; on the other hand, scutellarin may also participate in regulating cell cycle and apoptotic proteins by activating MEK/ERK/PIN1 signaling pathway to promote the nuclear translocation of PKM2.

Efficient solid-phase synthesis of trifunctional probes and their application to the detection of carbohydrate-binding proteins

(Chemical Equation Presented) An efficient solid-phase synthesis of trifunctional probes containing a photoreactive group, a reporter tag, and a carbohydrate ligand was developed. Labeling studies with these probes demonstrate that specific lectins can be

Steric-Free Bioorthogonal Labeling of Acetylation Substrates Based on a Fluorine-Thiol Displacement Reaction

We have developed a novel bioorthogonal reaction that can selectively displace fluorine substitutions alpha to amide bonds. This fluorine-thiol displacement reaction (FTDR) allows for fluorinated cofactors or precursors to be utilized as chemical reporters, hijacking acetyltransferase-mediated acetylation both in vitro and in live cells, which cannot be achieved with azide- or alkyne-based chemical reporters. The fluoroacetamide labels can be further converted to biotin or fluorophore tags using FTDR, enabling the general detection and imaging of acetyl substrates. This strategy may lead to a steric-free labeling platform for substrate proteins, expanding our chemical toolbox for functional annotation of post-translational modifications in a systematic manner.

Rapid and Selective Labeling of Endogenous Transmembrane Proteins in Living Cells with a Difluorophenyl Ester Affinity-Based Probe

The long-term stability of affinity-based protein labeling probes is crucial to obtain reproducible protein labeling results. However, highly stable probes generally suffer from low protein labeling efficiency and pose significant challenges when labeling low abundance native proteins in living cells. In this paper, we report that protein labeling probes based on an ortho-difluorophenyl ester reactive module exhibit long-term stability in DMSO stock solution and aqueous buffer, yet they can undergo rapid and selective labeling of native proteins. This novel electrophile can be customized with a wide range of different protein ligands and is particularly well-suited for the labeling and imaging of transmembrane proteins. With this probe design, the identity and relative levels of basal and hypoxia-induced transmembrane carbonic anhydrases were revealed by live cell imaging and in-gel fluorescence analysis. We believe that the extension of this difluorophenyl ester reactive module would allow for the specific labeling of various endogenous membrane proteins, facilitating in-depth studies of their distribution and functions in biological processes.