Beta III Tubulin (TUBB3) is one of six β-tubulin isoforms and is expressed highly during fetal and postnatal development (axon guidance and maturation). Its expression levels decrease in the adult central nervous system (CNS) but remain high in the peripheral nervous system (PNS). Microtubules enriched in β3-tubulin are more dynamic than those composed of other β-tubulin isoforms. Research studies have shown that mutations in the β3-tubulin gene TUBB3 cause ocular motility defects and other nervous system disorders. Furthermore, β3-tubulin is present in neoplastic but not in normal differentiated glial cells. Thus, β3-tubulin is a great neuronal marker.
Beta-tubulin is a protein that forms the backbone of cells. Tubulin can be divided into several kinds of Tubulin, including α, β, γ, δ, and ε, among which α -tubulin and β -tubulin can form heterodimers and are the two most important Tubulin for microtubule formation. The molecular weights of α-tubulin and β-tubulin are 55kDa and 50kDa, respectively, and the actual detected bands are around 55kDa. As an internal reference protein, the protein levels of β tubulin generally do not change. Therefore, it has been widely used as a reference for the consistency of sample loading in Western Bloting and also for immunostaining to observe the microtubule structure of cells.
Beta IV Tubulin (TUBB4) is a member of the beta tubulin family. Beta tubulins are one of two core protein families (alpha and beta tubulins) that heterodimerize and assemble to form microtubules. Mutations in TUBB4 cause hypomyelinating leukodystrophy and autosomal dominant torsion dystonia. Alternate splicing of the TUBB4 gene results in multiple transcript variants encoding different isoforms.
Beta tubulin forms a dimer with alpha tubulin and acts as a major structural component of microtubules.
FGF basic, also known as FGF-2 and HBGF-2, is a member of the FGF family of mitogenic proteins. FGF basic is widely expressed and affects diverse aspects of embryonic development by regulating cell proliferation, differentiation, and survival. Various N-terminal extensions affect localization of FGF basic in cellular compartments but do not affect biological activity. Binding of FGF to heparin or cell surface heparan sulfate proteoglycans is necessary for binding of FGF to high affinity FGF receptors. Mature human FGF basic shares greater than 96% aa sequence identity with bovine, mouse, and rat FGF basic.
Involved in the regulation of homocysteine metabolism. Converts betaine and homocysteine to dimethylglycine and methionine, respectively. This reaction is also required for the irreversible oxidation of choline.
The major proteolytic product p15 BID allows the release of cytochrome c . Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2.
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