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Full length protein
Amino Acid Sequence
MSRGPEEVNRLTESTYRNVMEQFNPGLRNLINLGKNYEKAVNAMILAGKA YYDGVAKIGEIATGSPVSTELGHVLIEISSTHKKLNESLDENFKKFHKEI IHELEKKIELDVKYMNATLKRYQTEHKNKLESLEKSQAELKKIRRKSQGS RNALKYEHKEIEYVETVTSRQSEIQKFIADGCKEALLEEKRRFCFLVDKH CGFANHIHYYHLQSAELLNSKLPRWQETCVDAIKVPEKIMNMIEEIKTPA STPVSGTPQASPMIERSNVVRKDYDTLSKCSPKMPPAPSGRAYTSPLIDM FNNPATAAPNSQRVNNSTGTSEDPSLQRSVSVATGLNMMKKQKVKTIFPH TAGSNKTLLSFAQGDVITLLIPEEKDGWLYGEHDVSKARGWFPSSYTKLL EENETEAVTVPTPSPTPVRSISTVNLSENSSVVIPPPDYLECLSMGAAAD RRADSARTTSTFKAPASKPETAAPNDANGTAKPPFLSGENPFATVKLRPT VTNDRSAPIIR
1 to 511
proprietary tag N-Terminus
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in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Stability and Storage
Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.
Constituents: 0.31% Glutathione, 0.79% Tris HCl
- BAI1 associated protein 2 like 1
- BAI1 associated protein 2 like protein 1
- BAI1-associated protein 2-like protein 1
May function as adapter protein. Involved in the formation of clusters of actin bundles. Plays a role in the reorganization of the actin cytoskeleton in response to bacterial infection.
Contains 1 IMD (IRSp53/MIM homology) domain.
Contains 1 SH3 domain.
The IMD domain is predicted to have a helical structure. It may induce actin bundling and filopodia formation.
Phosphorylated on tyrosine in response to insulin.
Cytoplasm, cytoskeleton. Recruited to actin pedestals that are formed upon infection by bacteria at bacterial attachment sites.
Information by UniProt
has not yet been referenced specifically in any publications.
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