4-Azido-L-homoalanine HCl (L-AHA) [942518-29-8]

Cat# CLK-AA005-10

Size : 10mg

Marca : Jena Bioscience

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Telefono : +1 850 650 7790

(S)-2-Amino-4-azidobutanoic acid hydrochloride

Structural formula of 4-Azido-L-homoalanine HCl (L-AHA) ((S)-2-Amino-4-azidobutanoic acid hydrochloride)
Structural formula of 4-Azido-L-homoalanine HCl (L-AHA)

For general laboratory use.

Shipping: shipped on gel packs

Storage Conditions: store at 4 °C
store dry

Shelf Life: 12 months after date of delivery

Molecular Formula: C4H8N4O2

Molecular Weight: 144.13 g/mol (free acid)

Exact Mass: 144.06 g/mol (free acid)

CAS#: 942518-29-8

Purity: mass identification conforms (ESI-MS)

Form: powder

Color: white

Applications:
Proteins synthesis monitoring[1,2,3]

Description:
4-Azido-L-homoalanine (L-AHA) provides a non-radioactive alternative to analyze the global protein synthesis in cell culture. It is cell-permeable and randomly incorporated instead of methionine during translation[1,2,3]. The resulting azide-labeled full-length proteins can subsequently be detected via Cu(I)-catalyzed or Cu(I)-free click chemistry that offers the choice to introduce a Biotin group (via Azides of Biotin or DBCO-containing Biotin, respectively) for subsequent purification tasks or a fluorescent group (via Azides of fluorescent dyes or DBCO-containing fluorescent dyes, respectively) for subsequent microscopic imaging.

Presolski et al.[4] and Hong et al.[5] provide a general protocol for Cu(I)-catalyzed click chemistry reactions that may be used as a starting point for the set up and optimization of individual assays.

BIOZ Product Citations:

Selected References:
[1] Dieck et al. (2012) Metabolic Labeling with Noncanonical Amino Acids and Visualisation by Chemoselective Fluorescent Tagging. Current Protocols in Cell Biology 7:7.11.1.
[2] Kiick et al. (2002) Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation. Proc. Natl. Acad. Sci. USA 99 (1):19.
[3] Dieterich et al. (2010) In situ visualization and dynamics of newly synthesized proteins in rat hippocampal neurons. Nature Neuroscience 13 (7): 897.
[4] Presolski et al. (2011) Copper-Catalyzed Azide-Alkyne Click Chemistry for Bioconjugation. Current Protocols in Chemical Biology 3:153.
[5] Hong et al. (2011) Analysis and Optimization of Copper-Catalyzed Azide-Alkyne Cycloaddition for Bioconjugation. Angew. Chem. Int. Ed. 48:9879.


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