Product: Tubulin beta Antibody
Catalog: AF7011
Description: Rabbit polyclonal antibody to Tubulin beta
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Mol.Wt.: 55kDa; 50kD(Calculated).
Uniprot: P07437
RRID: AB_2827688

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Product Info

Source:
Rabbit
Application:
WB 1:1000-1:5000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Clonality:
Polyclonal
Specificity:
Tubulin beta Antibody detects endogenous levels of total Tubulin beta.
RRID:
AB_2827688
Cite Format: Affinity Biosciences Cat# AF7011, RRID:AB_2827688.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

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

Immunogens

Immunogen:

A synthesized peptide derived from human Tubulin beta.

Uniprot:
Gene(ID):
Expression:
P07437 TBB5_HUMAN:

Ubiquitously expressed with highest levels in spleen, thymus and immature brain.

Description:
TUBB3 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. TUBB3 plays a critical role in proper axon guidance and mantainance.
Sequence:
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLDRISVYYNEATGGKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQVFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEEEEDFGEEAEEEA

PTMs - P07437 As Substrate

Site PTM Type Enzyme
R2 Methylation
C12 S-Nitrosylation
K19 Acetylation
K19 Methylation
K19 Ubiquitination
S25 Phosphorylation
T33 Phosphorylation
T35 Phosphorylation
Y36 Phosphorylation
S40 Phosphorylation
R46 Methylation
S48 Phosphorylation
Y50 Phosphorylation
Y51 Phosphorylation
T55 Phosphorylation
K58 Acetylation
K58 Methylation
K58 Sumoylation
K58 Ubiquitination
Y59 Phosphorylation
T72 Phosphorylation
S75 Phosphorylation
S78 Phosphorylation
S95 Phosphorylation
K103 Acetylation
K103 Sumoylation
K103 Ubiquitination
Y106 Phosphorylation
T107 Phosphorylation
S115 Phosphorylation
K122 Ubiquitination
S126 Phosphorylation
T136 Phosphorylation
S138 Phosphorylation
T143 Phosphorylation
S145 Phosphorylation
T149 Phosphorylation
S153 Phosphorylation
K154 Ubiquitination
Y159 Phosphorylation
R162 Methylation
T166 Phosphorylation
S168 Phosphorylation
S172 Phosphorylation
K174 Ubiquitination
Y183 Phosphorylation
T196 Phosphorylation
T199 Phosphorylation
Y200 Phosphorylation
Y208 Phosphorylation
K216 Ubiquitination
T218 Phosphorylation
T219 Phosphorylation
T221 Phosphorylation
Y222 Phosphorylation
S234 Phosphorylation
C239 S-Nitrosylation
K252 Sumoylation
K252 Ubiquitination
T274 Phosphorylation
S275 Phosphorylation Q5TCY1 (TTBK1)
R276 Methylation
S278 Phosphorylation
Y281 Phosphorylation
T285 Phosphorylation
T290 Phosphorylation
K297 Ubiquitination
C303 S-Nitrosylation
Y310 Phosphorylation
T312 Phosphorylation
R318 Methylation
S322 Phosphorylation
K324 Acetylation
K324 Sumoylation
K324 Ubiquitination
K336 Acetylation
K336 Ubiquitination
S338 Phosphorylation
S339 Phosphorylation
Y340 Phosphorylation
K350 Sumoylation
K350 Ubiquitination
T351 Phosphorylation
K362 Ubiquitination
T366 Phosphorylation
S371 Phosphorylation
K379 Acetylation
K379 Ubiquitination
S382 Phosphorylation
T386 Phosphorylation
K392 Ubiquitination
T399 Phosphorylation
Y422 Phosphorylation
Y425 Phosphorylation
T429 Phosphorylation

Research Backgrounds

Function:

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.

PTMs:

Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group. 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.

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.

Subcellular Location:

Cytoplasm>Cytoskeleton.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Ubiquitously expressed with highest levels in spleen, thymus and immature brain.

Subunit Structure:

Heterodimer of alpha and beta chains. 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. Interacts with DIAPH1. Interacts with MX1 (By similarity). May interact with RNABP10 (By similarity). Interacts with CFAP157 (By similarity).

Family&Domains:

The highly acidic C-terminal region may bind cations such as calcium.

Belongs to the tubulin family.

Research Fields

· Cellular Processes > Transport and catabolism > Phagosome.   (View pathway)

· Cellular Processes > Cellular community - eukaryotes > Gap junction.   (View pathway)

· Human Diseases > Infectious diseases: Bacterial > Pathogenic Escherichia coli infection.

References

1). The Nuclear Matrix Protein SAFA Surveils Viral RNA and Facilitates Immunity by Activating Antiviral Enhancers and Super-enhancers. Cell Host & Microbe (PubMed: 31513772) [IF=30.3]

Application: WB    Species: human    Sample: HEK293 cells

Figure 3.| Oligomerized SAFA Mediates IFNb Transcription(I) HEK293 cells were transfected with indicated plasmids and infected with virus for 6 h, followed by oligomerization assay.

2). SOX9 Modulates the Transformation of Gastric Stem Cells Through Biased Symmetric Cell Division. Gastroenterology (PubMed: 36740200) [IF=29.4]

3). The microglial innate immune receptors TREM-1 and TREM-2 in the anterior cingulate cortex (ACC) drive visceral hypersensitivity and depressive-like behaviors following DSS-induced colitis. Brain, Behavior, and Immunity (PubMed: 37286175) [IF=15.1]

4). Circular RNA circBbs9 promotes PM2. 5-induced lung inflammation in mice via NLRP3 inflammasome activation. ENVIRONMENT INTERNATIONAL (PubMed: 32707273) [IF=11.8]

Application: WB    Species: mouse    Sample: lung

Fig. 3. Involvement of the NLRP3 inflammasome pathway in PM2.5-induced inflammatory response. (A) The mRNA expression of NLRP3 was examined in lung tissue from normal and COPD model mice. (B) The mRNA expression of NLRP3 was examined in RAW264.7 cells exposed to PM2.5. (C) The immunohistochemistry images of NLRP3 protein were analyzed in FA and PM2.5 exposed groups of normal and COPD model mice. (D) The score of lung tissue NLRP3 protein immunohistochemistry between FA and PM2.5 exposed mice. (E) The protein expression of NLRP3 inflammasome-related genes NLRP3, caspase-1, cleaved-caspase-1, IL-1β, and IL-18, were detected by western blot in normal and COPD model mouse lung tissue. Relative expression levels of NLRP3, caspase-1, cleaved-caspase-1, IL-1β, and IL-18 are shown in F-J. (K) The protein expression level of NLRP3 inflammasome-related genes, including NLRP3, caspase-1, cleaved-caspase-1, IL-1β, and IL-18, were analyzed in RAW264.7 cells exposed to PM2.5 for 24 h and 48 h. (L) Relative expression levels of NLRP3, caspase-1, cleaved-caspase-1, IL-1β, and IL-18 in RAW264.7 cells between the control and PM2.5 exposed group. The (M) mRNA and (N, O) protein expression levels of NLRP3 inflammasome-related genes were detected after treatment with NLRP3 siRNA and PM2.5 exposure, respectively. *p < 0.05, **p < 0.01, ***p < 0.001.

5). Circulating proteomic panels for risk stratification of intracranial aneurysm and its rupture. EMBO Molecular Medicine (PubMed: 34978375) [IF=11.1]

Application: WB    Species: Human    Sample: IA tissue

Figure 2 IA tissue proteome remodeling due to IA formation and rupture Five pairs of IA and STA tissues surgically excised from intracranial aneurysm patients. Differentially expressed proteins between IA group and STA group, as determined by plotting Student’s t‐test (P‐value < 0.05, two‐sided) P‐values versus the log2 fold change (IA/STA) are represented on volcano plots. Proteins with significant change in expression levels are indicated by pink (upregulated) and blue (downregulated) dots. The dashed line (x = ±1) represents the cutoff of the log2 fold change in protein levels, and dashed line (y = 2) represents the cutoff of the −log10 t‐test P‐value. Significantly altered top ranked pathways in IA tissues compared with STA tissues. Interaction network of tissue downregulated proteins in IA group compared to STA group. Western blot validation of selected protein (PDLIM1) differentially expressed between STA and IA. Downregulation of PDLIM1 in IA tissue as compared to STA tissue was confirmed. Immunoblots showing expression differences of PDLIM1 in STA and IA specimens are shown in the left panel using β‐tubulin as the loading control. The semi‐quantitative densitometric measurement of blot bands is summarized in the lower panel. Error bars indicate standard deviations (three biological replicates for each group, two‐tailed Student’s t‐test, * P‐value < 0.05).

6). Opsonized nanoparticles target and regulate macrophage polarization for osteoarthritis therapy: A trapping strategy. Journal of Controlled Release (PubMed: 35489544) [IF=10.8]

7). Glutamine‐based Metabolism Normalization and Oxidative Stress Alleviation by Self‐assembled bilirubin/V9302 Nanoparticles for Psoriasis Treatment. Advanced Healthcare Materials (PubMed: 36690435) [IF=10.0]

8). Nanomechanical vibration profiling of oocytes. Nano Research [IF=9.9]

9). A marine-derived small molecule induces immunogenic cell death against triple-negative breast cancer through ER stress-CHOP pathway. International Journal of Biological Sciences (PubMed: 35541893) [IF=9.2]

Application: WB    Species: human    Sample: MDA-MB-231 cells

Figure 2. | MHO7 induced ER stress and cell cycle arrest in TNBC cells.(D) The expression of BiP/p-PERK/p-eIF2α/ATF4/CHOP were measured by western blot under MHO7 treatment in MDA-MB-231 cells.

10). NLRP3-dependent microglial training impaired the clearance of amyloid-beta and aggravated the cognitive decline in Alzheimer’s disease. Cell Death & Disease (PubMed: 33051464) [IF=9.0]

Application: WB    Species: mice    Sample: cortex and hippocampus

Fig. 2 Histological and western blotting analysis of NACHT-, LRR-, and pyrin (PYD)-domain-containing protein 3 (NLRP3) activation. A Immunofluorescence staining of NLRP3 and ionized calcium-binding adapter molecule 1 (Iba1) (×63 oil immersion objective). B Comparisons of NLRP3 intensities in the cortex and hippocampus. C Chemiluminescence images of NLRP3, caspase-1 and β-tubulin, IL-1β and β-actin. D Comparisons of the NLRP3/β-tubulin, cleaved caspase-1/β-tubulin, and IL-1β/β-actin ratios. Each dataset is expressed as mean ± SD. *P ≤ 0.05; **P ≤ 0.01; ***P ≤ 0.001; ****P ≤ 0.0001. n = 6 mice

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