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vapor density
1.9 (vs air)
Quality Level
vapor pressure
1 mmHg ( 160.4 °C)
Assay
99.998% trace metals basis
form
powder
technique(s)
HPLC: suitable
impurities
≤25.0 ppm Trace Metal Analysis
mp
340 °C (subl.) (lit.)
SMILES string
N.Cl
InChI
1S/ClH.H3N/h1H;1H3
InChI key
NLXLAEXVIDQMFP-UHFFFAOYSA-N
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Application
Ammonium chloride (NH4Cl) is an ammonium salt which can be used for a variety of applications such as:
- a catalyst for the one-pot synthesis of 3,4-dihydropyrimidin-2-(1H)-ones
- a promoter in the multicomponent synthesis of pyrrolo[3,4-b]pyridine-5-one
- a reagent to improve the hydrolysis rate of magnesium hydride for the generation of hydrogen
- a reductant, which facilitates the recovery of metals that are utilized in lithium-ion batteries
Signal Word
Warning
Hazard Statements
Precautionary Statements
Hazard Classifications
Acute Tox. 4 Oral - Eye Irrit. 2
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Find documentation for the products that you have recently purchased in the Document Library.
Ammonium chloride-promoted four-component synthesis of pyrrolo [3, 4-b] pyridin-5-one
Journal of the American Chemical Society, 124(11), 2560-2567 (2002)
A sustainable process for metal recycling from spent lithium-ion batteries using ammonium chloride
Waste Management (New York, N.Y.), 79(18), 545-553 (2018)
Hydrogen generation by hydrolysis of MgH2 and enhanced kinetics performance of ammonium chloride introducing
International Journal of Hydrogen Energy, 40(18), 6145-6150 (2015)
Ammonium chloride-catalyzed one-pot synthesis of 3,4-dihydropyrimidin-2-(1H)-ones under solvent-free conditions.
Tetrahedron Letters, 44(4), 857-859 (2003)
Journal of cell science, 128(13), 2269-2277 (2015-05-23)
TM9 family proteins (also named Phg1 proteins) have been previously shown to control cell adhesion by determining the cell surface localization of adhesion proteins such as the Dictyostelium SibA protein. Here, we show that the glycine-rich transmembrane domain (TMD) of
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