alpha Tubulin Antibody - #AF4651

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Product: alpha Tubulin Antibody
Catalog: AF4651
Description: Rabbit polyclonal antibody to alpha Tubulin
Application: WB
Cited expt.: WB
Reactivity: Human, Mouse, Rat
Prediction: Pig, Zebrafish, Bovine, Horse, Sheep, Dog
Mol.Wt.: 52kDa; 50kD(Calculated).
Uniprot: P68363
RRID: AB_2844660

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 50ul $250 In stock
 100ul $350 In stock
 200ul $450 In stock

Lead Time: Same day delivery

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Related Downloads
MSDS
Data Sheet
COA
Protocols
WB Handbook
IHC Protocol
IF/ICC Protocol

Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000
*The optimal dilutions should be determined by the end user. For optimal experimental results, antibody reuse is not recommended.
*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
Prediction:
Pig(100%), Zebrafish(92%), Bovine(100%), Horse(100%), Sheep(100%), Dog(100%)
Clonality:
Polyclonal
Specificity:
alpha Tubulin Antibody detects endogenous levels of alpha Tubulin.
RRID:
AB_2844660
Cite Format: Affinity Biosciences Cat# AF4651, RRID:AB_2844660.
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

Alpha tubulin ubiquitous; Alpha-tubulin ubiquitous; K alpha 1; TBA1B_HUMAN; TUBA1B; Tubulin alpha 1B; Tubulin alpha 1B chain; Tubulin alpha ubiquitous; Tubulin alpha ubiquitous chain; Tubulin alpha-1B chain; Tubulin alpha-ubiquitous chain; Tubulin K alpha 1; Tubulin K-alpha-1;

Immunogens

Immunogen:

A synthesized peptide derived from human alpha Tubulin, corresponding to a region within N-terminal amino acids.

Uniprot:

P68363(TBA1B_HUMAN) >>Visit HPA database.

Gene(ID):
TUBA1B(10376)
Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Pig
100
Horse
100
Bovine
100
Sheep
100
Dog
100
Zebrafish
92
Xenopus
0
Chicken
0
Rabbit
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

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).

Acetylation of alpha chains at Lys-40 is located inside the microtubule lumen. This modification has been correlated with increased microtubule stability, intracellular transport and ciliary assembly.

Methylation of alpha chains at Lys-40 is found in mitotic microtubules and is required for normal mitosis and cytokinesis contributing to genomic stability.

Nitration of Tyr-451 is irreversible and interferes with normal dynein intracellular distribution.

Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively.

Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (By similarity). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules. In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity).

Detyrosination is involved in metaphase plate congression by guiding chromosomes during mitosis: detyrosination promotes interaction with CENPE, promoting pole-proximal transport of chromosomes toward the equator. Detyrosination increases microtubules-dependent mechanotransduction in dystrophic cardiac and skeletal muscle. In cardiomyocytes, detyrosinated microtubules are required to resist to contractile compression during contraction: detyrosination promotes association with desmin (DES) at force-generating sarcomeres, leading to buckled microtubules and mechanical resistance to contraction (By similarity).

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
Family&Domains:

Belongs to the tubulin family.

Research Fields

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

· Cellular Processes > Cell growth and death > Apoptosis.   (View pathway)

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

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

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

References

1). Brain region-specific action of ketamine as a rapid antidepressant. Science (New York, N.Y.), 2024 (PubMed: 39116252) [IF=44.7]
2). LncRNA-MEG3 Regulates Muscle Mass and Metabolic Homeostasis by Facilitating SUZ12 Liquid-Liquid Phase Separation. Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2025 (PubMed: 40285575) [IF=15.1]

Application: WB    Species: Mouse    Sample:

Figure 5 Characterization of the interaction between lncRNA-MEG3 and SUZ12. A) RNA-binding motif enrichment analysis showing the most frequently detected RNA-binding proteins associated with lncRNA-MEG3 by catRAPID (http://s.tartaglialab.com/page/catrapid_group). B) Fluorescent in situ hybridization (FISH) showing lncRNA-MEG3 localization (green) in primary mouse myoblasts and C2C12 myoblasts. Nuclei are stained with DAPI (blue) (n = 3). Scale bar = 20 µm. C–E) RNA pull-down assay of SUZ12, β-actin (negative control), and GAPDH (negative control) using antisense and sense probes for lncRNA-MEG3 in C2C12 myoblast lysates (n = 3). Input represents total lysates. F) Quantification of the lncRNA-MEG3 interaction with SUZ12 normalized to input level (n = 3). G) Predicted secondary structure of lncRNA-MEG3 highlighting structural domains (D1, D2, and D3). H) RNA pull-down assay was performed to analyze the binding of lncRNA-MEG3 WT, deletion expression vectors (D1, D2, and D3), and SUZ12 protein (n = 3). I,J) Domain mapping of SUZ12 using truncated fragments (B1, B2, and B3) in pull-down assays, identifying the lncRNA-MEG3 interaction domain in SUZ12 (n = 3). K) Schematic of the deletion constructs in the B3 domain, with the deleted regions located at the following amino acid positions: c1 (500-550 aa deletion), c2 (551–600 aa deletion), c3 (601–650 aa deletion), c4 (651–700 aa deletion), and c5 (701–739 aa deletion). L) RNA pull-down assay showing the interaction between biotinylated lncRNA-MEG3 and the B3 domain deletion variants (n = 3). M) Schematic representation of SUZ12 domains, indicating the lncRNA-MEG3 binding region and the EZH2/EED interaction region. N) Co-IP was performed to analyze the interaction between SUZ12 and EZH2/EED after C2C12 myoblasts were treated with RNase T1, DNase I, and lncRNA-MEG3 shRNA (n = 3). O) Co-IP was performed to analyze the interaction between SUZ12 and EZH2/EED after overexpression of lncRNA-MEG3 in C2C12 myoblasts (n = 3). P,Q) Co-IP was performed to analyze the interaction between SUZ12 and EZH2/EED in C2C12 myoblasts with knockdown of lncRNA-MEG3 (n = 3). R) IF staining of SUZ12 (red) in control and lncRNA-MEG3-overexpressing C2C12 cells showing enhanced nuclear localization. DAPI stains nuclei (blue) (n = 3). Scale bar = 20 µm. S) Western blot showing the expression of Suz12 in the nucleus, cytoplasm, and whole cell lysates of C2C12 myoblasts after lncRNA-MEG3 overexpression (n = 3). Lamin B1 was used as a marker for the nuclear protein, α-Tubulin as a marker for the cytoplasmic protein, and Gapdh as a marker for the total protein. Data are mean ± SD; p-values were calculated using Student's t-test. **p < 0.01.
3). C5a/C5aR pathway blocking promoted CuS-mediated cancer therapy effect by inhibiting cuproptosis resistance. Journal for immunotherapy of cancer, 2025 (PubMed: 40484643) [IF=10.9]

Application: WB    Species: Mouse    Sample: 4T1 cells

Figure 2. C5a/C5aR pathway was related to breast cancer cell cuproptosis. (A) GO analysis of differently expressed genes in epithelial cells from the breast cancer group versus the normal group. (B) Violin plots show the cuproptosis score in 18 epithelial cell clusters. (C) Association between complement activation score (cited from BP entry in GO enrichment) and cuproptosis score analyzed by Spearman’s analysis. (D) ssGSEA analysis of cuproptosis in epithelial cells derived from tumor and normal tissue. (E) Cuproptosis score, complement activation score, and cells with both high scores visualized by UMAP plot of epithelial cells. (F) Potential trajectory of all epithelial cells identified two distinct cell fates colored by cluster. (G) Heatmap showing selected-related genes of cuproptosis and C5-C5aR pathway along the pseudotime, which was clustered into three profiles. Color keys differentially coding from blue to red indicated the relative expression levels from low to high. (H) Dot plots of dynamic expression of key genes in cuproptosis and C5-C5aR pathway along two cell fates. (I) PPI network shows potentially existing connections between complement-related genes, copper transporters genes and cuproptosis-related genes. (J) GSEA analysis of various forms of programmed cell death (PCD) in 4T1 cells treated with C5a. (K–L) Volcano plot and heatmaps of differentially expressed genes between control groups and C5a treated groups in 4T-1 cells. (M–N) Western blotting and RT-qPCR analysis of ATP7B expression in 4T1 cells between control and C5a treated groups. (O) GSEA analysis of various forms of PCD in MDA-MB-231 cells treated with C5a. (P–Q) Volcano plot and heatmaps of differentially expressed genes between control groups and C5a treated groups in MDA-MB-231 cells. (R–S) Western blotting and RT-qPCR analysis of ATP7B expression in MDA-MB-231 cells between control and C5a-treated groups. Statistical differences are assessed by unpaired t-test. Data were mean±SEM. *p
4). Probiotic Pediococcus pentosaceus restored gossypol-induced intestinal barrier injury by increasing propionate content in Nile tilapia. Journal of animal science and biotechnology, 2024 (PubMed: 38582865) [IF=7.0]

Application: WB    Species: Fish    Sample:

Fig. 3 Addition of P. pentosaceus YC inhibited Nlrc3 and promoted the gene expression of ISC markers. A KEGG enrichment analysis; B Heatmap of genes of NOD-like signaling pathway; C and D Volcano plot of DEGs in the compared groups (n = 3). E and F The relative gene expression of ISC markers (lgr5 and olfm4) in PI and DI; G The protein expression of Nlrc3 in PI and DI; H and I The quantification of the protein expression of Nlrc3 in PI and DI; J and K The relative gene expression of foxo3 and cyclinD1 in PI and DI (n = 6). Data are represented as mean ± SEM. Asterisk refers to the significant difference (ANOVA with Tukey’s test; *P 
5). UCP2 promotes NSCLC proliferation and glycolysis via the mTOR/HIF-1α signaling. Cancer medicine, 2024 (PubMed: 38217303) [IF=2.9]

Application: WB    Species: human    Sample: PC9, H1975, and A549 cell

FIGURE 4 UCP2 promoted NSCLC progression through the mTOR/HIF-1α pathway. (A) Western blotting assay underwent conduct after PC9, H1975, and A549 cell lines were transfected. (B) ImageJ software was used to quantify the protein expression. **p 

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