The chemotherapeutic agent paclitaxel arrests cell division by binding to the hetero-dimeric protein tubulin. Subtle differences in tubulin sequences, across eukaryotes and among β-tubulin isotypes, can have profound impact on paclitaxel-tubulin binding. To capture the experimentally observed paclitaxel-resistance of human βIII tubulin isotype and yeast β-tubulin, within a common theoretical framework, we have performed structural principal component analyses of β-tubulin sequences across eukaryotes. The paclitaxel-resistance of human βIII tubulin isotype and yeast β-tubulin uniquely mapped on to the lowest two principal components, defining the paclitaxel-binding site residues of β-tubulin. The molecular mechanisms behind paclitaxel-resistance, mediated through key residues, were identified from structural consequences of characteristic mutations that confer paclitaxel-resistance. Specifically, Ala277 in βIII isotype was shown to be crucial for paclitaxel-resistance. The present analysis
TY - JOUR. T1 - Requirement for the βI and βIV tubulin isotypes in mammalian cilia. AU - Jensen-Smith, Heather C.. AU - Ludueña, Richard F.. AU - Hallworth, Richard. PY - 2003/7/1. Y1 - 2003/7/1. N2 - [Nielsen et al., 2001: Curr Biol 11:529-533], based on studies in Drosophila, have proposed that β tubulin in axonemal microtubules must contain a specific acidic seven amino acid sequence in its carboxyl terminus. In mammals, the two βIV isotypes (βIVa and βIVb) contain that sequence. In order to test the application of this hypothesis to mammals, we have examined the expression of β tubulin isotypes in four different ciliated tissues (trachea, ependyma, uterine tube, and testis) using isotype-specific antibodies and indirect immunofluorescence. We find that βIV tubulin is present in all ciliated cell types examined, but so is β1 tubulin. Taken together with recent studies that show that β1 and βIV tubulin are both present in the cilia of vestibular hair cells, olfactory neurons, and ...
The role of formins in microtubules is not well understood. In this study, we have investigated the mechanism by which INF2, a formin mutated in degenerative renal and neurological hereditary disorders, controls microtubule acetylation. We found that silencing of INF2 in epithelial RPE-1 cells produced a dramatic drop in tubulin acetylation, increased the G-actin/F-actin ratio, and impaired myocardin-related transcription factor (MRTF)/serum response factor (SRF)-dependent transcription, which is known to be repressed by increased levels of G-actin. The effect on tubulin acetylation was caused by the almost complete absence of α-tubulin acetyltransferase 1 (α-TAT1) messenger RNA (mRNA). Activation of the MRTF-SRF transcriptional complex restored α-TAT1 mRNA levels and tubulin acetylation. Several functional MRTF-SRF-responsive elements were consistently identified in the α-TAT1 gene. The effect of INF2 silencing on microtubule acetylation was also observed in epithelial ECV304 cells, but not ...
We have tested the functional capacity of different beta tubulin isoforms in vivo by expressing beta 3-tubulin either in place of or in addition to beta 2-tubulin in the male germ line of Drosophila melanogaster. The testes-specific isoform, beta 2, is conserved relative to major metazoan beta tubulins, while the developmentally regulated isoform, beta 3, is considerably divergent in sequence. beta 3-tubulin is normally expressed in discrete subsets of cells at specific times during development, but is not expressed in the male germ line. beta 2-Tubulin is normally expressed only in the postmitotic germ cells of the testis, and is required for all microtubule-based functions in these cells. The normal functions of beta 2-tubulin include assembly of meiotic spindles, axonemes, and at least two classes of cytoplasmic microtubules, including those associated with the differentiating mitochondrial derivatives. A hybrid gene was constructed in which 5 sequences from the beta 2 gene were joined to ...
Microtubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulin. The genes encoding these microtubule constituents are part of the tubulin superfamily, which is composed of six distinct families. Genes from the alpha, beta and gamma tubulin families are found in all eukaryotes. The alpha and beta tubulins represent the major components of microtubules, while gamma tubulin plays a critical role in the nucleation of microtubule assembly. There are multiple alpha and beta tubulin genes and they are highly conserved among and between species. This gene encodes an alpha tubulin that is a highly conserved homolog of a rat testis-specific alpha tubulin. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jun 2013 ...
Stu2p/XMAP215/Dis1 family proteins are evolutionarily conserved regulatory factors that use αβ-tubulin-interacting tumor overexpressed gene (TOG) domains to catalyze fast microtubule growth. Catalysis requires that these polymerases discriminate between unpolymerized and polymerized forms of αβ-tubulin, but the mechanism by which they do so has remained unclear. Here, we report the structure of the TOG1 domain from Stu2p bound to yeast αβ-tubulin. TOG1 binds αβ-tubulin in a way that excludes equivalent binding of a second TOG domain. Furthermore, TOG1 preferentially binds a curved conformation of αβ-tubulin that cannot be incorporated into microtubules, contacting α- and β-tubulin surfaces that do not participate in microtubule assembly. Conformation-selective interactions with αβ-tubulin explain how TOG-containing polymerases discriminate between unpolymerized and polymerized forms of αβ-tubulin and how they selectively recognize the growing end of the microtubule.. ...
Tubulin synthesis in the naturally synchronous plasmodium of Physarum polycephalum is a markedly periodic event restricted to the late G2 period of the cell cycle. Mitosis in the plasmodium is intranuclear, and there are no cytoplasmic microtubules at any stage of the cell cycle. We have combined a biochemical investigation of the synthesis of the plasmodial tubulin isotypes and their participation in the mitotic spindle with a microscopic study (immunofluorescence) of the development of spindle microtubules throughout the cell cycle. We have shown that all four tubulin isotypes identified in the plasmodium (alpha 1, alpha 2, beta 1 and beta 2) are present in the mitotic spindle. The stoichiometry of isotype usage in the mitotic spindle generally reflects the overall abundance of isotypes in the plasmodium as a whole: beta 2 greater than alpha 1 greater than alpha 2 greater than beta 1. We have also shown that tubulins synthesized in the G2 period of one cell cycle can be incorporated into the spindles
The nucleotide sequence of a complete rat brain beta-tubulin T beta 15 has been determined from three overlapping cDNA clones. The overall length of the T beta 15 sequence is 1589 bp and shows between 84.5% and 88.6% homology within the coding region as compared with chick and human beta-tubulin sequences. On the other hand, the 3-non-coding region is highly divergent. Comparison of the derived amino acid sequences from different species demonstrates that the amino acid changes are not randomly distributed, but rather there are several conserved and two highly variable regions common to beta-tubulin polypeptides from various sources. The T beta 15 sequence encodes a dominant neuronal 1.8-kb beta-tubulin mRNA species. Two other minor beta-tubulin mRNA species of 2.6 and 2.9 kb are present in rat brain. By using two synthetic oligonucleotide probes complementary to the carboxyl-terminal divergent region and to the amino-terminal conserved region, we have shown that the three mRNAs are distinct species,
Although TUBB3 is a neuron‐specific isoform of β‐tubulin, only about 20% of total β‐tubulin in neuronal cells is TUBB3 (Joshi and Cleveland, 1989). TUBB3(E410K) and TUBB3(D417H) mutants induce neuronal diseases in an autosomal dominant manner, meaning that only 10% of mutant tubulin can significantly induce neuronal phenotypes. How is this small amount of mutated TUBB3 able to strongly affect neurons? Because our assay used CMV and CAG promoters and unknown copy numbers of transfected vectors, we could not quantify the amount of tubulin incorporated into microtubules in our system. Nevertheless, we think our results give insights to this question. Microtubules are composed of α‐ and β‐tubulin dimers. The size of each tubulin dimer is 8 nm (Nogales et al, 1999). Our analysis showed that TUBB3(E410K) and TUBB3(D417H) were incorporated into microtubules in cells and could inhibit axonal transport (Supplementary Figure S1; Figure 8A). The inhibition of motor domain accumulation, axonal ...
Microtubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulin. The genes encoding these microtubule constituents are part of the tubulin superfamily, which is composed of six distinct families. Genes from the alpha, beta and gamma tubulin families are found in all eukaryotes. The alpha and beta tubulins represent the major components of microtubules, while gamma tubulin plays a critical role in the nucleation of microtubule assembly. There are multiple alpha and beta tubulin genes and they are highly conserved among and between species. This gene is an alpha tubulin gene that encodes a protein 99% identical to the mouse testis-specific Tuba3 and Tuba7 gene products. This gene is located in the 13q11 region, which is associated with the genetic diseases Clouston hidrotic ectodermal dysplasia and Kabuki syndrome. [provided by RefSeq, Jul 2008 ...
During embryogenesis, the β3 tubulin gene of Drosophila is transcribed predominantly in the mesoderm. We have raised antibodies specific to the C-terminal domain of the β3 tubulin and analysed by immunostaining the distribution of this tubulin isotype during Drosophila embryogenesis. The protein is first detectable in the cephalic mesoderm at maximal germband extension. Shortly afterwards, β3 tubulin is expressed in single cells at identical positions of the thoracic and abdominal segments. We suggest that these cells represent muscle pioneer cells of Drosophila. During later embryonic development the somatic musculature, musculature, visceral musculature, dorsal vessel and macrophages contain β3 tubulin. In dorsalizing mutants dorsal, snail and twist, which do not form a ventral furrow during gastrulation, β3 expression is greatly reduced but not completely abolished. Our analysis shows that β3 tubulin immunostaining characterizes the differentiation of mesodermal derivatives during ...
The molecular mechanisms responsible for microtubule (MT) nucleation have not yet been identified in higher plants. Unlike other eukaryotic cells, no centrosome-like organelles are present to nucleate MT assembly. In animal cells, the centrosome functions as a microtubule-organizing center (MTOC), and in fungi, the spindle pole body (SPB) plays this role. MT nucleation is initiated by γ-tubulin ring complexes, or γ-TuRCs ( Zheng et al., 1995), which are recruited from the cytoplasm to the MTOC and activated ( Schiebel, 2000). The smallest complex unit capable of MT nucleation, the γ-tubulin small complex (γ-TuSC), was identified in yeast ( Knop and Schiebel, 1997) and in Drosophila ( Oegema et al., 1999; Gunawardane et al., 2000). The γ-TuSC, which is thought to be a γ-TuRC precursor, contains γ-tubulin, known as a universal nucleator ( Oakley, 1992) and two additional proteins, spindle pole body components Spc98p and Spc97p or their homologues. These proteins are essential for the ...
Although most eukaryotic cells can express multiple isotypes of alphabeta-tubulin, the significance of this diversity has not always been apparent. Recent data indicate that particular alphabeta-tubulin isotypes, both genome encoded and those derived by post-translational modification, can directly influence microtubule structure and function--thus validating ideas originally proposed in the multitubulin hypothesis over 25 years ago. It has also become increasingly evident over the past year that some (but intriguingly not all) eukaryotes encode several other tubulin proteins, and to date five further members of the tubulin superfamily, gamma, delta, epsilon, zeta and eta, have been identified. Although the role of gamma-tubulin in the nucleation of microtubule assembly is now well established, far less is known about the functions of delta-, epsilon-, zeta- and eta-tubulin. Recent work has expanded our knowledge of the functions and localisation of these newer members of the tubulin superfamily, and
Tubulin protein derived from Porcine brain provides a good target for drug discovery. Highly pure protein provided in lyophilized format from Cytoskeleton, Inc.
Screening for Arabidopsis mutants that displayed twisted growth of elongating organs and abnormal growth responses to propyzamide resulted in a large collection of dominant-negative tubulin mutants. The data presented here provide some of the strongest evidence to date showing conserved residues of both α- and β-tubulins directly contribute to the stability and helical pattern of cortical microtubule arrays.. Incorporation of mutant tubulins into the microtubule polymer suggests that the structure and/or dynamics of cortical microtubules are altered in these mutants. Many of the affected amino acid residues are located at the longitudinal interface of the α- and β-tubulins within and between the αβ-heterodimer and at the lateral interface between two adjacent protofilaments, indicating that the mutations generally affect the protein-protein interactions but not the stability or the folding of tubulin monomers. Several mutated residues, such as P325 and T439 in α-tubulin and S95 and G96 in ...
Posttranslational modifications of tubulin are thought to fine‐tune MT functions in specific cells and tissues. Modifications that take place on the C‐terminal tails of tubulin are involved in the regulation of interactions between MTs and associated proteins (reviewed in: Janke & Bulinski, 2011). The three principal modifications found in these tail domains are detyrosination, (poly)glutamylation and (poly)glycylation. While first insights into the molecular mechanisms that are controlled by detyrosination (Peris et al, 2006, 2009; Bieling et al, 2008) and polyglutamylation (Kubo et al, 2010; Lacroix et al, 2010) have been obtained, little is known about the roles and mechanisms of glycylation.. In contrast to other tubulin modifications, glycylation has so far only been detected in motile cilia and flagella in different organisms (Bré et al, 1996). In line with this rather restricted occurrence of glycylation, only three modifying enzymes are expressed in mammals (Rogowski et al, 2009), ...
While the heterozygous Q43P β1-tubulin carriers have a reduced function, the β1-tubulin-deficient mice present with only minor abnormalities in platelet hemostatic functions. Besides the fact that human platelets are more easy to handle and study in detail than mouse platelets, this can probably be explained by the fact that the loss of β1-tubulin expression in mouse platelets was overcome by overexpression of the other platelet β-tubulin variants,7 while the Q43P carrier platelets not only show reduced β1-tubulin but also total β-tubulin protein levels. In addition, incorporation of GFP-tagged Q43P β1-tubulin into wild-type tubulin structures seems to be inefficient and delocalized.. Due to the platelet dysfunction phenotype, the Q43P β1-tubulin variant could not only be conceived as a genetic risk factor for the development of thrombocytopenia but also as a protective genetic factor against cardiovascular disease. Indeed, a case-control study showed that the prevalence of Q43P ...
Microtubules are filaments of the cytoskeleton. They typically form through the polymerization of α- and β-tubulin dimers elongating existing microtubules. The de novo formation of microtubules requires an initiation event called microtubule nucleation. Microtubule nucleation requires the action of a third type of tubulin, γ-tubulin, which is distinct from the α and β subunits which compose the microtubules themselves. The γ-tubulin combines with several other associated proteins to form a circular structure known as the γ-tubulin ring complex (γ-TuRC). This complex acts as a scaffold for α/β tubulin dimers to begin polymerization. It also acts as a cap of the (−) end while microtubule growth continues towards the (+) direction. The γ-TuRC is typically found as the core functional unit in a microtubule organizing center (MTOC), such as the centrosome in animal cells or the spindle pole bodies in fungi and algae. However, the cells of higher plants for example lack distinct MTOCs and ...
Microtubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulin. The genes encoding these microtubule constituents are part of the tubulin superfamily, which is composed of six distinct families. Genes from the alpha, beta and gamma tubulin families are found in all eukaryotes. The alpha and beta tubulins represent the major components of microtubules, while gamma tubulin plays a critical role in the nucleation of microtubule assembly. There are multiple alpha and beta tubulin genes and they are highly conserved among and between species. This gene is an alpha tubulin gene that encodes a protein 99% to the mouse testis-specific Tuba3 and Tuba7 gene products. This gene is located in the 13q11 region, which is associated with the genetic diseases Clouston hidrotic ectodermal dysplasia and Kabuki syndrome. Alternative splicing has been observed for this gene and two variants have been identified.[4] ...
Microtubule nucleation requires the γ-tubulin ring complex, and during the M-phase (mitosis) this complex accumulates at the centrosome to support mitotic spindle formation. The posttranslational modification of γ-tubulin through ubiquitination is vital for regulating microtubule nucleation and centrosome duplication. Blocking the BRCA1/BARD1-dependent ubiquitination of γ-tubulin causes centrosome amplification. In the current study, we identified BRCA1-associated protein-1 (BAP1) as a deubiquitination enzyme for γ-tubulin. BAP1 was downregulated in metastatic adenocarcinoma breast cell lines compared with noncancerous human breast epithelial cells. Furthermore, low expression of BAP1 was associated with reduced overall survival of patients with breast cancer. Reduced expression of BAP1 in breast cancer cell lines was associated with mitotic abnormalities. Importantly, rescue experiments including expression of full length but not the catalytic mutant of BAP1 reduced ubiquitination of γ-tubulin and
The function of microtubules depends on their arrangement into highly ordered arrays. Spatio-temporal control over the formation of new microtubules and regulation of their properties are central to the organization of these arrays. The nucleation of new microtubules requires γ-tubulin, an essential protein that assembles into multi-subunit complexes and is found in all eukaryotic organisms. However, the way in which γ-tubulin complexes are regulated and how this affects nucleation and, potentially, microtubule behavior, is poorly understood. γ-tubulin has been found in complexes of various sizes but several lines of evidence suggest that only large, ring-shaped complexes function as efficient microtubule nucleators. Human γ-tubulin ring complexes (γTuRCs) are composed of γ-tubulin and the γ-tubulin complex components (GCPs) 2, 3, 4, 5 and 6, which are members of a conserved protein family. Recent work has identified additional unrelated γTuRC subunits, as well as a large number of more ...
MTs are cylindrical polymers 25 nanometers (nm = 10-9 meter) in diameter, comprised of 13 longitudinal protofilaments which are each chains of the protein tubulin (Figure 8). Each tubulin is a peanut-shaped dimer (8 nm by 4 nm by 5 nm) which consists of two slightly different monomers known as alpha and beta tubulin, (each 4 nm by 4 nm by 5 nm, weighing 55,000 daltons). Tubulin subunits within MTs are arranged in a hexagonal lattice which is slightly twisted, resulting in differing neighbor relationships among each subunit and its six nearest neighbors (Figure 9). Thus pathways along contiguous tubulins form helical pathways which repeat every 3, 5 and 8 rows (the Fibonacci series). Alpha tubulin monomers are more negatively charged than beta monomers, so each tubulin (and each MT as a whole) is a ferroelectric dipole with positive (beta monomer) and negative (alpha monomer) ends.[xxiii ...
Along the length of the conoid fibers, tubulin molecules are spaced 4 nm apart, just as in microtubules. It seems probable that conoid protofilaments exhibit parallel, as opposed to antiparallel, orientation (implying that the fiber as a whole is a polar structure) as has been observed in all naturally occurring tubulin polymers, but the signal-to-noise ratio in images of conoid fibers obtained to date is too low to confirm this supposition. However, the lack of circular symmetry in cross-section means that the lateral association of protofilaments in conoid fibers must be quite different from microtubules. The noncircular cross-sectional profile implies that the bonds between adjacent protofilaments are very different at one end of the comma compared to the other: adjacent protofilaments at the curved end must be rotated by ∼30° with respect to each other (similar to the 360/13 = 27.7 degrees in a canonical 13 protofilament microtubule), whereas adjacent protofilaments at the tail of the ...
Mlig034227.g3 {REF} {Length: 2733} {Pfam: Tubulin/FtsZ family, GTPase domain [PF00091.25, score=231.9]; Tubulin C-terminal domain [PF03953.17, score=146.9]; Misato Segment II tubulin-like domain [PF10644.9, score=25.7]} {Human: ENSG00000188229, TUBB4B, tubulin beta 4B class IVb, [RH, Score=920, Expect=0.0]; ENSG00000137285, TUBB2B, tubulin beta 2B class IIb, [RH, Score=908, Expect=0.0]; ENSG00000104833, TUBB4A, tubulin beta 4A class IVa, [RH, Score=905, Expect=0.0]; ENSG00000232575, TUBB, tubulin beta class I, [RH, Score=903, Expect=0.0]; ENSG00000196230, TUBB, tubulin beta class I, [RH, Score=903, Expect=0.0]; ENSG00000183311, TUBB, tubulin beta class I, [RH, Score=903, Expect=0.0]; ENSG00000227739, TUBB, tubulin beta class I, [RH, Score=903, Expect=0.0]; ENSG00000235067, TUBB, tubulin beta class I, [RH, Score=903, Expect=0.0]; ENSG00000229684, TUBB, tubulin beta class I, [RH, Score=903, Expect=0.0]; ENSG00000137267, TUBB2A, tubulin beta 2A class IIa, [RH, Score=903, Expect=0.0]; ...
beta Tubulin antibody (tubulin, beta) for ICC/IF, IHC-P, WB. Anti-beta Tubulin pAb (GTX101279) is tested in Human, Mouse, Rat, Hamster samples. 100% Ab-Assurance.
beta Tubulin antibody (tubulin, beta) for ICC/IF, IHC-P, WB. Anti-beta Tubulin pAb (GTX112659) is tested in Human, Mouse samples. 100% Ab-Assurance.
TY - JOUR. T1 - Preparation of Tubulin from Brain. AU - Williams, Robley C.. AU - Lee, James C.. PY - 1982/1/1. Y1 - 1982/1/1. N2 - This chapter presents procedure for preparation of tubulin from brain. Two methods for preparing tubulin is presented (a) purification by cycles of assembly and disassembly followed by chromatography on phospbocellulose (b) purification by the modified Weisenberg procedure, each of which yields several hundred milligrams of purified protein. The principal properties of the tubulin prepared by the two methods appear to be identical and a choice of one route or the other can be made on the basis of available apparatus or of the investigators familiarity with the manipulations involved. The tubulin that results from either preparation is substantially free of microtubule-associated proteins. The protein concentration of the solution is determined spectrophotometrically in 6 M guanidine hydrochloride at 275 nm with an absorptivity value of 1.03 ml/(mg cm). It is then ...
gamma tubulin Antibody 66320-1-Ig has been identified with ELISA, IF, IHC, WB. 66320-1-Ig detected 48-55 kDa band in NCCIT, HepG2, HSCT6, NIH/3T3 cell with 1:1000-1:8000 dilution...
Rat anti Tubulin alpha antibody, clone YL1/2 recognizes the alpha subunit of tubulin, specifically binding tyrosylated Tubulin (Tyr-Tubulin) (Wehland
购买gamma Tubulin兔多克隆抗体(ab50721),gamma Tubulin抗体经WB验证,3篇文献引用,1个独立用户反馈。产品出库一年都在质保范围内。中国现货速达。
Background: The disordered Tubulin Polymerization Promoting Protein/p25 (TPPP/p25) modulates the dynamics and stability of the microtubule system. In this paper the role of dimerization in its microtubulerelated functions is established, and an approach is proposed to evaluate thermodynamic constants for multiple equilibrium systems from ITC measurements. Methods: For structural studies size exclusion chromatography, SDS-PAGE, chemical cross-linking, circular dichroism, fluorescence spectroscopy and isothermal titration calorimetry were used; the functional effect was analyzed by tubulin polymerization assay. Numerical simulation of the multiple equilibrium was performed with Mathematica software. Results: The dimerization of TPPP/p25 is promoted by elevation of the protein concentration and by GTP addition. The dimeric form displaying enhanced tubulin polymerization promoting activity is stabilized by disulfide bond or chemical cross-linking. The GTP binding to the dimeric form ...
alpha Tubulin / TUBA1A / TUBA3, 0.1 mg. Tubulin is one of the main components of the cytoskeleton. It is a heterodimeric structure consisting of interlocking alpha and beta chains.
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Taxol-stabilized GDP-microtubules were prepared by polymerizing 10 μl of 100 μM glycerol-free porcine tubulin (Cytoskeleton, Denver, CO) in 80 mM K-PIPES (pH 6.8), 1 mM MgCl2, 1 mM EGTA, 10% DMSO, and 1 mM GTP for 1 hour in a 37°C water bath. Taxol was added to 20 μM final concentration, and the reaction was incubated on the bench top for 1 to 2 hours. Microtubules were loaded onto a 60% glycerol cushion [BRB80, 60% (v/v) glycerol, and 20 μM Taxol] at 37°C by using a pipette tip with the tip cut off. Nonpolymerized tubulin was removed by centrifugation in a TLA100 rotor at 35,000 rpm for 15 min at 37°C. The pellet was gently resuspended to 2.5 μM tubulin in BRB80 supplemented with 20 μM Taxol and 1 mM GTP at 37°C by using a pipette tip with the tip cut off.. For GDP-microtubules, all polymerization and severing reactions were performed at 37°C. Twenty microliters of 100 μM glycerol-free porcine tubulin (Cytoskeleton) was polymerized in 10% DMSO, 1 mM GTP, and 10 mM MgCl2 for 1 hour ...
Microtubules (MTs) are essential structural components of cells. They are made up of polymers of protein subunits of α,β-tubulin and are highly dynamic, undergoing rapid phases of assembly and disassembly. The dynamic behavior of MTs is essential for their cellular activities.
alpha Tubulin小鼠单克隆抗体[4G1](ab28439)可与小鼠, 大鼠, 人样本反应并经WB, ELISA, Flow Cyt, ICC/IF实验严格验证,被3篇文献引用。所有产品均提供质保服务,中国75%以上现货。
Mouse monoclonal alpha Tubulin antibody [TU-01]. Validated in WB, IP, ELISA, IHC, ICC, Flow Cyt, ICC/IF and tested in Mouse, Cow, Dog, Human, Pig. Cited in 22 publication(s). Independently reviewed…
Mouse monoclonal alpha Tubulin antibody [4G1] validated for WB, ELISA, Flow Cyt, ICC/IF and tested in Human, Mouse and Rat. Referenced in 3 publications…
Dimeric alpha-beta tubulin. Computer model showing the structure of the tight dimeric complex formed by alpha (green) and beta (blue) tubulin. The beta tubulin has a site binding docetaxel (red). Polymers of alpha- and beta-tubulin make up microtubules, part of the cells cytoskeleton. - Stock Image C035/5590
Fox lung cells with mEGFP fused to tubulin - The ends of microtubules are always in dynamic formation: addition or removal of tubulin proteins alters the length of the biopolymer. The rate of depolymerization is different for each end according to its polarity, and the side that grows the fastest is considered the positive end while the other, more stable terminus, is negative. The dynamic, fast-growing portion of the microtubule is composed of beta-tubulin projected out towards the membrane of the cell. The alpha-tubulins stabilize their structure toward the nucleus at the centriole located in the centrosome of the cell. The digital videos presented in this section explore Gray fox lung fibroblast cells (FoLu line) expressing a fusion construct of mEGFP and human alpha-tubulin to highlight microtubules (green fluorescence) in order to visualize dynamic processes.. Observing Chromosomes and the Spindle in Mitosis. ...
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The effect of a change in neurofilament (NF) and tubulin gene expression on the elongation of axonal sprouts by adult rat sensory neurons was examined. Distal sciatic nerve crush axotomy was used to initiate changes in cytoskeletal gene expression in lumbar dorsal root ganglion (DRG) neurons. In situ hybridization of DRG neurons with 35S- labeled cDNA probes revealed a significant reduction in the level of mRNAs for the low-molecular weight-NF protein and a significant increase in the level of beta tubulin mRNAs by 2 weeks after axotomy. A novel modification of the axonal transport paradigm was used to examine the biochemical composition of the regenerating axons formed by primed and unprimed DRG neurons. Primed neurons (which had sustained a crush axotomy of the distal sciatic nerve 2 weeks earlier) and unprimed (normal) neurons were labeled by microinjection of 35S-methionine and then stimulated to regenerate axons by a crush located very close to the DRG. In this paradigm, axonal sprouts that ...
Mouse Monoclonal Anti-beta-III Tubulin Antibody (5H2). Neuronal Marker. Validated: WB. Tested Reactivity: Human. 100% Guaranteed.
The free tubulin concentration at a point x in the neurite at time t is given by c(x, t). The length of the neurite at time t is given by l(t). Space x lies in the domain 0 to l. Tubulin moves by active transport (a) and diffusion (D), and degrades with rate g. Synthesis of tubulin in the cell body at rate ∈0c0 results in a flux of tubulin across the boundary at x = 0. Assembly of tubulin onto microtubules results in a flux of tubulin across the boundary at x = l (assembly flux ∈ l and return flux ζ l ) and a change in length (assembly rate r g and disassembly s g ).. This model is a generalisation of previous ODE and algebraic treatments of this scenario [19, 22]. Its solution, both analytically and numerically, is complicated by the fact that it is of the moving boundary type ie the spatial domain changes over time due to changes in the length, l. A stable and accurate numerical solution has been proposed in which the spatial domain is discretized into a fixed number of N grid points and ...
Mouse Monoclonal Anti-gamma-2 Tubulin Antibody (4F6) [PerCP]. Validated: WB, ELISA, ICC/IF. Tested Reactivity: Human. 100% Guaranteed.
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In neurons, the microtubule cytoskeleton supports the formation of elaborate neuronal morphologies, facilitates axon pathfinding and synapse formation, and allows for intracellular trafficking. The alpha tubulin gene, TUBA1A, encodes the most highly expressed alpha tubulin protein in the brain. TUBA1A is expressed in developing post-mitotic neurons, and mutations to this gene in humans result in severe developmental brain malformations, called tubulinopathies. We showed that an Asparagine to Aspartic acid substitution at residue 102 (Tuba1aN102D) results in severe brain malformations and perinatal death in mice that are homozygous for this mutation. Recently we have shown that mice heterozygous for this mutation (Tuba1aN102D/+) display more subtle disruption of brain development, specifically impairing axon pathfinding through large brain commissures. Additionally, Tuba1aN102D/+ mice develop an adult-onset behavioral motor deficit, that is not accompanied by neuronal cell death. Thus, we are ...
BioAssay record AID 214536 submitted by ChEMBL: Tested for the effect on polymerization of the tubulin present by microtubule assembly assay.
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Dynamic instability, in which abrupt transitions occur between growing and shrinking states, is an intrinsic property of microtubules that is regulated by both mechanics and specialized proteins. We discuss a model of dynamic instability based on the popular idea that growth is maintained by a cap at the tip of the fiber. The loss of this cap is thought to trigger the transition from growth to shrinkage, called a catastrophe. The model includes longitudinal interactions between the terminal tubulins of each protofilament, and ``gating rescues between neighboring protofilaments. These interactions allow individual protofilaments to transiently shorten in a phase of overall microtubule growth. The model reproduces the reported dependency of the catastrophe rate on tubulin concentration, the time between tubulin dilution and catastrophe, and the induction of microtubule catastrophes by walking depolymerases. The model also reproduces the comet tail distribution that is characteristic of proteins ...