Product Pathways - Cytoskeletal Signaling
KIF3A (D7G3) Rabbit mAb #8507
|8507S||100 µl (10 western blots)||---||In Stock||---|
|8507||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||80||Rabbit IgG|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IP=Immunoprecipitation
Specificity / Sensitivity
KIF3A (D7G3) Rabbit mAb recognizes endogenous levels of total KIF3A protein.
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human KIF3A protein.
Kinesin superfamily proteins (KIFs) are molecular motors that drive directional, microtubule-dependent intracellular transport of membrane-bound organelles and other macromolecules (e.g. proteins, nucleic acids). The intracellular transport functions of KIFs are fundamentally important for a variety of cellular functions, including mitotic and meiotic division, motility/migration, hormone and neurotransmitter release, and differentiation (1-4). Disruptions to KIF-mediated intracellular transport have been linked with a variety of pathologies, ranging from tumorigenesis to defects in higher order brain function, such as learning and memory (4-6).
Kinesin superfamily protein 3A (KIF3A) is a central component of the kinesin-2 protein complex (7). KIF3A and its paralog KIF3B bind to form a heterodimeric motor protein with ATP-dependent, plus-end-directed microtubule sliding activity (8). The tail domain of this heterodimer binds to kinesin-associated protein 3 (KAP3), which facilitates binding of the KIF3A/3B motor protein to its cargo (7,8). Recent studies in a variety of model organisms have demonstrated a critical role for kinesin-family proteins, including KIF3A, in the formation and function of cilia (9). Notably, KIF3A was shown to mediate cilia-dependent protein-protein interactions that function to transduce canonical Hedgehog signaling (10).
- Hirokawa, N. et al. (2009) Nat Rev Mol Cell Biol 10, 682-96.
- Yu, Y. and Feng, Y.M. (2010) Cancer 116, 5150-60.
- Park, J.J. et al. (2008) Mol Endocrinol 22, 989-1005.
- Hirokawa, N. et al. (2010) Neuron 68, 610-38.
- Yoshimura, Y. et al. (2010) Mol Cell Biol 30, 2206-19.
- Hirokawa, N. and Noda, Y. (2008) Physiol Rev 88, 1089-118.
- Haraguchi, K. et al. (2006) J Biol Chem 281, 4094-9.
- Yamazaki, H. et al. (1995) J Cell Biol 130, 1387-99.
- Zhao, C. et al. (2012) Proc Natl Acad Sci U S A 109, 2388-93.
- Humke, E.W. et al. (2010) Genes Dev 24, 670-82.
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