TUBB3, CDCBM, Beta III Tubulin, Class III beta-tubulin, TUBB4, Tubulin, beta 3, Tubulin beta-III, Tubulin beta-3 chain, Tubulin beta-4 chain, Tubulin, beta 3 class III, CFEOM3A
WB: 1:10000~1:500000, IHC: 1:200, IF/ICC: 1:200, ELISA(peptide) 1:20000-1:40000
Human, Mouse, Rat, Sheep, Rabbit, Dog, Monkey, Hamster, Chicken
beta-Tubulin Mouse Monoclonal antibody detects endogenous levels of total beta-Tubulin protein.
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl.
Full-length beta-tubulin protein of human.
Observed Mol.Wt.: 55KD.
Predicted Mol.Wt.: 50kDa.
Cytoplasm > cytoskeleton.
Ubiquitously expressed with highest levels in spleen, thymus and immature brain.
Microtubules are constituent parts of the mitotic apparatus, cilia, flagella, and elements of the cytoskeleton. They consist principally of 2 soluble proteins, alpha- and beta-tubulin, each of about 55,000 kDa. Antibodies against beta Tubulin are useful as loading controls for Western Blotting. However it should be noted that levels of beta-Tubulin may not be stable in certain cells. For example, expression of beta-Tubulin in adipose tissue is very low and therefore beta-Tubulin should not be used as loading control for these tissues.
10 20 30 40 50
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY
60 70 80 90 100
YNEATGGKYV PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN
110 120 130 140 150
WAKGHYTEGA ELVDSVLDVV RKEAESCDCL QGFQLTHSLG GGTGSGMGTL
160 170 180 190 200
LISKIREEYP DRIMNTFSVV PSPKVSDTVV EPYNATLSVH QLVENTDETY
210 220 230 240 250
CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL RFPGQLNADL
260 270 280 290 300
RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQVFDAKNMM
310 320 330 340 350
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK
360 370 380 390 400
TAVCDIPPRG LKMAVTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG
410 420 430 440
EGMDEMEFTE AESNMNDLVS EYQQYQDATA EEEEDFGEEA EEEA
Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate tails: severing activity by SPAST increases as the number of glutamates per tubulin rises from one to eight, but decreases beyond this glutamylation threshold (PubMed:26875866).Some glutamate residues at the C-terminus are monoglycylated but not polyglycylated due to the absence of functional TTLL10 in human. Monoglycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally. The precise function of monoglycylation is still unclear (Probable).Phosphorylated on Ser-172 by CDK1 during the cell cycle, from metaphase to telophase, but not in interphase. This phosphorylation inhibits tubulin incorporation into microtubules.
Heterodimer of alpha and beta chains (PubMed:26637975). A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Interacts with PIFO (PubMed:20643351). Interacts with DIAPH1 (PubMed:23325789). Interacts with MX1 (By similarity). May interact with RNABP10 (By similarity). Interacts with CFAP157 (By similarity).
The highly acidic C-terminal region may bind cations such as calcium.Belongs to the tubulin family.
Application: WB Species:human; Sample:Not available
Figure 4. Microtubule involved in PKC z activation. (A) In resting condition, co-immunoprecipitation of PKC z in Scr and siSIN1 cells lysis buﬀer, and the expression of b-tubulin was measured by western blotting. Nonimmune IgG was used as a control. (B) SIN1 and b-tubulin co-IP with PKC z antibody at diﬀerent intervals stimulated by 100 nmol/L insulin. (C) After being treated with 10 nM PTX and 10 μM NDZ for four hours, membrane translocation of PKC z induced by insulin was tested. (D) After being treated by 10 nM PTX and 10 μM NDZ, phosphorylation of PKC z and downstream coflin induced by insulin was measured. (E) The relationship of microtubules with PKC z was tested by confocal microscopy before and after 100 nmol/L insulin stimulation.
Tips: For phospho antibody, we provide phospho peptide（0.5mg) and non-phospho peptide(0.5mg).
Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. This mechanism is useful when non-specific binding is an issue, for example, in Western blotting (immunoblot) and immunohistochemistry (IHC). By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific; Specific binding will be absent from the western blot or immunostaining performed with the neutralized antibody.
Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 10 mg/ml.The purity is >90%,tested by HPLC and MS.Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
This product is for research use only. Not for use in diagnostic or therapeutic procedures.