Microtubule-Associated Protein 4 (MAP4) (Isoform 4,pSer1074) antibody

Antigen: Microtubule-Associated Protein 4 (MAP4)

Synonyms: MGC8617, DKFZp779A1753, MAP4, Mtap-4, AA407148, Mtap4, XMAP4, mtap4

Binding Site: Isoform 4,pSer1074

Clonality: Polyclonal

Host: Please enquire

Reactivity: Human

Conjugate: Un-conjugated

Application: Please enquire

Catalog no.: ABIN966518

Additional Information

Alternative name: MAP4

Immunogen: Polyclonal antibody produced in rabbits immunizing with a synthetic peptide corresponding to C-terminal residues of human MAP4 (microtubule-associated protein 4 isoform 4)

Description: MAP4 (microtubule-associated protein 4 isoform 4) is a major non-neuronal microtubule-associated protein. This protein contains a domain similar to the microtubule-binding domains of neuronal microtubule-associated protein (MAP2) and microtubule-associated protein tau (MAPT/TAU). This protein promotes microtubule assembly, and has been shown to counteract destabilization of interphase microtubule catastrophe promotion. Cyclin B was found to interact with this protein, which targets cell division cycle 2 (CDC2) kinase to microtubules. The phosphorylation of this protein affects microtubule properties and cell cycle progression. Multiple transcript variants encoding different isoforms have been found for this gene.
Synonyms: DKFZp779A1753, MGC8617

Application Details

Restrictions: For Research Use only

Publications

Product: West, Tenbarge, Olmsted: "A model for microtubule-associated protein 4 structure. Domains defined by comparisons of human, mouse, and bovine sequences." in: The Journal of biological chemistry, Vol. 266, Issue 32, pp. 21886-96, 1991 (PubMed).

Chapin, Lue, Yu et al.: "Differential expression of alternatively spliced forms of MAP4: a repertoire of structurally different microtubule-binding domains." in: Biochemistry, Vol. 34, Issue 7, pp. 2289-301, 1995 (PubMed).

Ookata, Hisanaga, Bulinski et al.: "Cyclin B interaction with microtubule-associated protein 4 (MAP4) targets p34cdc2 kinase to microtubules and is a potential regulator of M-phase microtubule dynamics." in: The Journal of cell biology, Vol. 128, Issue 5, pp. 849-62, 1995 (PubMed).

Beausoleil, Villén, Gerber et al.: "A probability-based approach for high-throughput protein phosphorylation analysis and site localization." in: Nature biotechnology, Vol. 24, Issue 10, pp. 1285-92, 2006 (PubMed).

Olsen, Blagoev, Gnad et al.: "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." in: Cell, Vol. 127, Issue 3, pp. 635-48, 2006 (PubMed).

Wu, Ma, Brown et al.: "Systematic identification of SH3 domain-mediated human protein-protein interactions by peptide array target screening." in: Proteomics, Vol. 7, Issue 11, pp. 1775-85, 2007 (PubMed).