Overview |
bs-70462r-100ul |
EB3 (central region) Antibody |
WB |
The antibody detects a 32 kDa* protein corresponding to the apparent molecular mass of EB3 on SDS-PAGE immunoblots of mouse brain and human recombinant full length EB3 protein. This peptide sequence is highly conserved in mouse and rat EB3, and has low homology to other EB family members. |
Human, Mouse, Rat |
Specifications |
Unconjugated |
Rabbit |
EB3 synthetic peptide (coupled to KLH) corresponding to amino acid residues from the central region of human EB3. |
Polyclonal |
IgG |
Antigen Affinity purification |
PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol |
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C. |
Target |
Q9UPY8 |
Microtubule RP/EB, MAPRE3, APC, EB3, End-binding. RP3 |
The microtubule (MT) plus-end is a crucial site for the regulation of MT dynamics and interactions by several groups of plus-end tracking proteins (+TIPs). These +TIPs form comet-like accumulations at the plus ends of MTs to regulate MT dynamics and interactions with organelles and macromolecular complexes. The +TIPs include diverse groups of proteins, such as motor and nonmotor proteins, MT polymerases and depolymerases as well as various regulatory and adaptor proteins. The CLIP-associated protein (CLASP) family includes CLASP1 and CLASP2 proteins, which are expressed as long (α) and short (β) isoforms. Thse +TIPs conatin an N-terminal TOG domain, multiple TOG-like domains, and a basic and serine-rich motif (SxIP). The TOG domain facilitates interaction with tubulin dimers, while the SxIP motif promotes interaciton with EB1 and MTs. A C-terminal domain is involved in interaction with CLIPs, as well as several other proteins. CLASPs are MT stabilizing fators that localize to mitotic spindles, kinetochores, and the midbody. CLASPs are important for cell division, and may regulate cell migration and neuronal growth cone motility. |
Application Dilution |
WB |
1:300-5000 |