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About This Item
Empirical Formula (Hill Notation):
C6H4IN3
CAS Number:
Molecular Weight:
245.02
UNSPSC Code:
12352200
NACRES:
NA.22
PubChem Substance ID:
MDL number:
Beilstein/REAXYS Number:
1939309
Assay:
≥95% (HPLC)
Form:
solution
Product Name
1-Azido-4-iodobenzene solution, 0.5 M in tert-butyl methyl ether, ≥95% (HPLC)
InChI
1S/C6H4IN3/c7-5-1-3-6(4-2-5)9-10-8/h1-4H
SMILES string
Ic1ccc(cc1)N=[N+]=[N-]
InChI key
FJOKWWVZXVTOIR-UHFFFAOYSA-N
assay
≥95% (HPLC)
form
solution
concentration
0.5 M in tert-butyl methyl ether
impurities
≤2.0% water
storage temp.
−20°C
Quality Level
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Flam. Liq. 2 - Skin Irrit. 2 - STOT RE 1
Storage Class
3 - Flammable liquids
wgk
WGK 3
flash_point_f
-27.4 °F
flash_point_c
-33 °C
Regulatory Information
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Labeling of hydrophobic polypeptides from the chick lens membrane.
L J Takemoto et al.
Experimental eye research, 35(5), 535-540 (1982-11-01)
M D Davison et al.
The Biochemical journal, 236(2), 389-395 (1986-06-01)
Opsin labelled with photoactivated 1-azido-4-[125I]iodobenzene was proteolysed in situ with Staphylococcus aureus V8 proteinase to yield two radioactive membrane-bound fragments. These were separated, cleaved with CNBr and the resultant peptides sequenced in order to locate the radiolabelled residues. In the
M E Haw
British journal of anaesthesia, 53(6), 577-584 (1981-06-01)
Xenopus laevis tadpoles were produced from wild-caught, laboratory-reared toads. Separate sets were fed on diets of (1) liver powder; (2) nettle powder; (3) aminosol and Intralipid. The tadpoles were reared for 3 weeks at 22 degrees C and then three
E Wells et al.
The Biochemical journal, 187(3), 719-725 (1980-06-01)
To investigate the intramembranous domains of the major band-3 polypeptide, human erythrocyte membranes were labelled with 1-azido-4-[125I]iodobenzene. The anion-exchange protein has been isolated by a new procedure that decreases possible contamination by other integral membrane proteins of similar molecular weight.
M D Davison et al.
The Biochemical journal, 234(2), 413-420 (1986-03-01)
The hydrophobic photosensitive probe 1-azido-4-[125I]iodobenzene (AIB) partitioned preferentially into photoreceptor disc membranes and, upon u.v. irradiation, became covalently bound to opsin and phospholipid. The labelling of both protein and phospholipid was linearly related to AIB concentration. The amount of probe
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