Immunological Data Discovery Index
Immunological Data Discovery Index
| identifier: | 1790471 |
| description: |
epitope description:alpha-D-Manp-(1->3)-[alpha-D-Manp-(1->6)]-[beta-D-Xylp-(1->2)]-beta-D-Manp-(1->4)-beta-D-GlcpNAc-(1->4)-D-GlcpNAc
antigen name:Hemocyanin, beta-C chain unit D
host organism:Rattus norvegicus
antibody name:YZ1/2.23
|
| aggregation: |
instance of dataset
|
| availability: |
available
|
| primaryPublications: |
15033940 |
| authorizations: |
registration not required
|
| accessURL: |
http://www.iedb.org/reference/1016056 |
| landingPage: |
http://www.iedb.org/assay/1790471 |
| type: |
Literature
|
| publicationVenue: |
Glycobiology
|
| dates: |
2004
|
| study type: | b cell assays |
| subject species: | Helix pomatia |
| fullName: |
Monika Bencú
rová
Wolfgang Hemmer
Margarete Focke-Tejkl
Iain B H Wilson
Friedrich Altmann
|
| method: |
antigen inhibition
|
| name: |
Specificity of IgG and IgE antibodies against plant and insect glycoprotein glycans determined with artificial glycoforms of human transferrin.
|
| description: |
The epitope is part of the N-glycan of several glycoproteins. A representative example is given.
The mAb reacted with the epitope when expressed artificially on human transferrin in an in vitro expression system. This reactivity was observed in Western blot, direct ELISA, and competitive ELISA. The mAb also reacted with the similar glycan MMF (without xylose and with fucose) and the two epitopes compete each other, while the structure MM, lacking both, is poorly recognized, implying that both fucose and xylose are important for recognition. The fucose residue seems to confer higher affinity.
|
| name: |
iedb
|
| homePage: |
http://www.iedb.org |
