Preparation and Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
The microtubule (MT) cytoskeleton functions in cytoplasmic organization, cellular movement, determination of cell polarity, intracellular transport, and chromosome segregation. Dynamic instability, continuous cycles of MT assembly (stabilization) and disassembly, mediates MT participation in these events. The function of MTs, particularly stabilization, is regulated by MT-associated proteins (MAPs). A subfamily of MAPs, called AP-MAPs (assembly promoting MAPs), includes tau, MAP2, and MAP4. These proteins are classified as type II MAPs and contain a C-terminal MT binding domain with 3 to 5 imperfect repeats of an 18 amino acid motif. While tau and MAP2 are specifically expressed in neuronal cells, MAP4 is the major MAP of nonneuronal mammalian cells. MAP activity and interaction with MTs are regulated by MARK (MAP/MT affinity-regulating kinase) and mapmodulin. MARK-mediated phosphorylation of MAPs on their homologous KXGS motifs results in detachment of MAPs from MTs and MT disruption. In addition, mapmodulin tightly interacts with the MT-binding domains of MAPs and hinders MAP binding to MTs. Thus, MAP4 is a highly regulated type II MAP that controls MT assembly and disassembly.
Development References (3)
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Chapin SJ, Lue CM, Yu MT, Bulinski JC. Differential expression of alternatively spliced forms of MAP4: a repertoire of structurally different microtubule-binding domains. Biochemistry. 1995; 34(7):2289-2301. (Biology). View Reference
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Drewes G, Ebneth A, Preuss U, Mandelkow EM, Mandelkow E. MARK, a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption. Cell. 1997; 89(2):297-308. (Biology). View Reference
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Ulitzur N, Humbert M, Pfeffer SR. Mapmodulin: a possible modulator of the interaction of microtubule-associated proteins with microtubules. Proc Natl Acad Sci U S A. 1997; 94(10):5084-5089. (Biology). View Reference
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Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims. Comparisons are not made against non-BD technologies, unless otherwise noted.
For Research Use Only. Not for use in diagnostic or therapeutic procedures.
