Lunatic Fringe Antibody (2D10-3C11) Summary
| Immunogen |
LFNG (AAH14851, 1 a.a. – 250 a.a.) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa. MTPGRCCLAADIQVETFIFTDGEDEALARHTGNVVITNCSAAHSRQALSCKMAVEYDRFIESGRKWFCHVDDDNYVNLRALLRLLASYPHTRDVYVGKPSLDRPIQAMERVSENKVRPVHFWFATGGAGFCISRGLALKMSPWASGGHFMNTAERIRLPDDCTIGYIVEALLGVPLIRSGLFHSHLENLQQVPTSELHEQVTLSYGMFENKRNAVHVKGPFSVEADPSRFRSIHCHLYPDTPWCPRTAIF
|
| Specificity |
LFNG – lunatic fringe homolog (Drosophila)
|
| Isotype |
IgG1 Kappa
|
| Clonality |
Monoclonal
|
| Host |
Mouse
|
| Gene |
LFNG
|
| Purity |
IgG purified
|
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|
Applications/Dilutions
| Dilutions |
|
| Application Notes |
Antibody reactivity against cell lysate for WB. It has been used for IF and ELISA.
|
Packaging, Storage & Formulations
| Storage |
Aliquot and store at -20C or -80C. Avoid freeze-thaw cycles.
|
| Buffer |
PBS (pH 7.4)
|
| Preservative |
No Preservative
|
| Purity |
IgG purified
|
Notes
Quality control test: Antibody Reactive Against Recombinant Protein.
This product is produced by and distributed for Abnova, a company based in Taiwan.
Alternate Names for Lunatic Fringe Antibody (2D10-3C11)
- beta-1,3-N-acetylglucosaminyltransferase lunatic fringe
- EC 2.4.1.222
- LFNG O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
- LFNG
- lunatic fringe (Drosophila) homolog
- lunatic fringe homolog (Drosophila)
- Lunatic Fringe
- O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase
- SCDO3
- SCDO3EC 2.4.1.222
Background
This gene encodes a member of the glycosyltransferase superfamily. The encoded protein is a single-pass type II Golgi membrane protein that functions as a fucose-specific glycosyltransferase, adding an N-acetylglucosamine to the fucose residue of a group of signaling receptors involved in regulating cell fate decisions during development. Mutations in this gene have been associated with autosomal recessive spondylocostal dysostosis 3. Alternatively spliced transcript variants that encode different isoforms have been described, however, not all variants have been fully characterized.