52084-13-6

Basic information

• Product Name: H-VAL-PNA
• Synonyms: L-VAL-PARANITROANILIDE;L-VAL-PNA;L-VALINE 4-NITROANILIDE;L-VALINE-P-NITROANALIDE;H-VAL-PNA;VALINE-PNA;L-VALINE P-NITROANILIDE);(2S)-2-Amino-3-methyl-N-(4-nitrophenyl)butanamide
• CAS NO: 52084-13-6
• Molecular Formula: C₁₁H₁₅N₃O₃
• Molecular Weight: 237.26
• Product Categories: Amino Acids
• Mol File: 52084-13-6.mol

Chemical Properties

• Boiling Point: 446.5 °C at 760 mmHg
• Flash Point: 223.8 °C
• Appearance: /
• Density: 1.259g/cm³
• Vapor Pressure: 3.63E-08mmHg at 25°C
• Refractive Index: 1.6
• Storage Temp.: -15°C
• PKA: 12.84±0.70(Predicted)
• CAS DataBase Reference: H-VAL-PNA(CAS DataBase Reference)
• NIST Chemistry Reference: H-VAL-PNA(52084-13-6)
• EPA Substance Registry System: H-VAL-PNA(52084-13-6)

Safety Data

• Hazardous Substances Data: 52084-13-6(Hazardous Substances Data)

Usage

Uses

Used in Diagnostics:
H-VAL-PNA is used as a diagnostic tool for its ability to bind specifically to DNA and RNA, which can help in identifying genetic mutations and detecting diseases.
Used in Therapeutics:
H-VAL-PNA is used as a therapeutic agent for its potential to target specific DNA and RNA sequences, which can be useful in treating genetic disorders and diseases.
Used in Molecular Biology Research:
H-VAL-PNA is used as a research tool for its ability to bind to nucleic acids, which can aid in understanding the mechanisms of gene expression and regulation.
Used in Drug Delivery Systems:
H-VAL-PNA is used as a component in drug delivery systems for its potential to enhance the delivery and bioavailability of therapeutic agents by binding to specific DNA or RNA sequences.
Used in Nanotechnology:
H-VAL-PNA is used in nanotechnology applications for its ability to bind to nucleic acids, which can be utilized in the development of nanoscale devices and sensors for genetic analysis and detection.

InChI:InChI=1/C11H15N3O3/c1-7(2)10(12)11(15)13-8-3-5-9(6-4-8)14(16)17/h3-7,10H,12H2,1-2H3,(H,13,15)/t10-/m0/s1

Upstream product

• 100-01-6 4-nitro-aniline 
• 13734-41-3 t-Boc-L-valine 
• 90105-48-9 (S)-1-[(S)-2-((S)-2-Amino-propionylamino)-propionyl]-pyrrolidine-2-carboxylic acid [(S)-2-methyl-1-(4-nitro-phenylcarbamoyl)-propyl]-amide 
• 75670-93-8 Z-L-Val-pNA 
• 61043-47-8 N-succinyl-Ala-Ala-Val-p-nitroanilide 

Downstream Products

• 78588-21-3 BOC-L-Leu-L-Val-pNA 
• 89545-61-9 Boc-Asn-Val-pNA 
• 187884-16-8 Boc-Leu-Pro-pNA 
• 89545-68-6 Boc-Leu-Pro-D-Ala-Val-pNA 
• 89545-63-1 Boc-Leu-Pro-Asn-Val-pNA 
• 100-01-6 4-nitro-aniline 
• 61043-29-6 Z-Ala-Ala-Val-Nan 
• 76402-50-1 H-D-Leu-L-Val-pNA 
• 115700-55-5 Z-Gln-Val-Val-pNA 
• 115700-61-3 Suc-Gln-Val-Val-pNA 
• 115700-62-4 Suc-Gln-Val-pNA 
• 769082-62-4 H-Gln-Val-Val-pNA 
• 746568-00-3 H-Gln-Val-pNA 

Relevant articles and documents

L-valine dipeptide organocatalysts with two amide units for the direct asymmetric aldol reaction in brine

A series of valine dipeptide organocatalysts containing a primary amine group and two amide units have been developed and evaluated in the direct asymmetric intermolecular aldol reaction of 4-nitrobenzaldehyde and cyclohexanone. When 2,4-dinitrophenol (DN

Purification and Some Properties of a Protease from the Sarcocarp of Musk Melon Fruit

A protease has been purified from sarcocarp of musk melon.Cucumis melo ssp. melo var. reticulatus Naud.Earl's Favourite.The protease was mostly present in the placenta part of the fruit and next in the inside mesocarp.The molecular mass of the enzyme was estimated to be about 62 kDa on SDS-PAGE.The enzyme had a carbohydrate moiety.The optimum pH of the enzyme was 11 at 35 deg C using casein as a substrate.The enzyme was stable between pH 6 and 11.The enzyme was strongly inhibited by diisopropyl fluorophosphate, but was not inhibited by EDTA or cysteine protease inhibitors.From the digestion of Ala-Ala-Pro-X-pNA (X = Phe, Leu, Val, Ala, Gly, Lys, Glu, Pro, and diaminopropionic acid (Dap) substrates the specificity of the protease was found to be approximately broad, but the preferential cleavage sites were C-terminal sites of h)drophobic or acidic amino acid residues at P1 position.It was proved that the enzymatic properties of musk melon protease are similar to those of cucumisin .The enzvme was not inhibited by typical proteinous inhibitors such as STI or ovomucoid.Therefore, this enzyme seems to be a useful protease for the food industries. - Keywords: Cucumis melo; Cucurbitaceae; musk melon; plant protease; serine protease.