Tubulin Alpha antibody | YL1/2

100% Secure


Rat anti Tubulin Alpha:HRP

Rat anti Tubulin Alpha

Rat anti Tubulin Alpha:DyLight®800

Rat anti Tubulin Alpha:DyLight®680

Rat anti Tubulin Alpha:DyLight®750

Product Type
Monoclonal Antibody
Clone
YL1/2
Isotype
IgG2a
Product CodeApplicationsDatasheetMSDSPack SizeList PriceQuantity
MCA77P C E WB 0.1 mg
MCA77G C E IF IP R WB 0.5 mg
MCA77D800 WB 0.1 mg
MCA77D680 WB 0.1 mg
MCA77D750 WB 0.1 mg
Rat anti Tubulin alpha antibody, clone YL1/2 recognizes the alpha subunit of tubulin, specifically binding tyrosylated Tubulin (Tyr-Tubulin) (Wehland et al. 1983). The epitope recognized by this antibody has been extensively studied and would appear to be a linear sequence requiring an aromatic residue at the C terminus, with the two adjacent amino acids being negatively charged (represented by Glu-Glu-Tyr in Tyr-Tubulin).

The antibody has been used in epitope tagging procedures to detect proteins tagged with a C-terminal Gly-Gly-Phe epitope. These sequence requirements have been reported to result in some cross-reactivity with other proteins in certain circumstances, including E. coli rec A and oxidized actin (Burns 1987).

This product is routinely tested in ELISA on Tubulin.

Product Details

Target Species
Yeast
Species Cross-Reactivity
Target SpeciesCross Reactivity
Ashbya
Birds Expected from Sequence
Echinoderm Expected from Sequence
Human
Mouse
Dog
Rat
Pig
Drosophila
Plants Expected from Sequence
Amphibia Expected from Sequence
Saccharomyces
Pleurobrachia
Caenorhabditis
Dictyostelium discoideum
Xenopus
Pig-tailed macaque
Clytia sp.
Arabidopsis
Strongylocentrotus purpuratus
Dendraster excentricus
Trypanosoma brucei
Potorous tridactylis
Bovine
Nephrotoma suturalis
Hemicentrotus pulcherrimus
Potato
Bombyx mori
Rhodnius prolixus
Fungal
N.B. Antibody reactivity and working conditions may vary between species.
Product Form
Purified IgG conjugated to Horseradish Peroxidase (HRP) - liquid
Product Form
Purified IgG - liquid
Product Form
Purified IgG conjugated to DyLight®800 - liquid
Product Form
Purified IgG conjugated to DyLight®680 - liquid
Product Form
Purified IgG conjugated to DyLight®750 - liquid
Preparation
Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant.
Preparation
Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant.
Preparation
Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant
Preparation
Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant.
Preparation
Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant.
Buffer Solution
Phosphate buffered saline
Buffer Solution
Phosphate buffered saline
Buffer Solution
Phosphate buffered saline
Buffer Solution
Phosphate buffered saline
Buffer Solution
Phosphate buffered saline
Preservative Stabilisers
0.01% Thiomersal
HRP Stabiliser (BUF052A)
Preservative Stabilisers
0.09%Sodium Azide
Preservative Stabilisers
0.09% Sodium Azide (NaN3)
Preservative Stabilisers
0.09% Sodium Azide (NaN3)
Preservative Stabilisers
0.09% Sodium Azide (NaN3)
Carrier Free
Yes
Immunogen
Yeast tubulin.
Approx. Protein Concentrations
IgG concentration 1.0 mg/ml
Approx. Protein Concentrations
IgG concentration 1.0 mg/ml
Approx. Protein Concentrations
IgG concentration 1.0 mg/ml
Approx. Protein Concentrations
IgG concentration 1.0 mg/ml
Approx. Protein Concentrations
IgG concentration 1.0 mg/ml
Fusion Partners
Spleen cells from immunised LOU rats were fused with cells of the Y3.Ag.1.2.3 rat myeloma cell line.

Storage Information

Storage
Store at +4oC. DO NOT FREEZE.
This product should be stored undiluted. Should this product contain a precipitate we recommend microcentrifugation before use.
Storage
Store at +4oC or at -20oC if preferred.

This product should be stored undiluted.

Storage in frost free freezers is not recommended. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use.
Storage
Store at +4oC or at -20oC if preferred.

This product should be stored undiluted.

Storage in frost free freezers is not recommended. This product is photosensitive and should be protected from light. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use
Storage
Store at +4oC or at -20oC if preferred.

This product should be stored undiluted.

Storage in frost free freezers is not recommended. This product is photosensitive and should be protected from light. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use
Storage
Store at +4oC or at -20oC if preferred.

This product should be stored undiluted.

Storage in frost free freezers is not recommended. This product is photosensitive and should be protected from light. Avoid repeated freezing and thawing as this may denature the antibody. Should this product contain a precipitate we recommend microcentrifugation before use.
Shelf Life
18 months from date of despatch.
Shelf Life
18 months from date of despatch.
Shelf Life
18 months from date of despatch
Shelf Life
18 months from date of despatch
Shelf Life
18 months from date of despatch.

More Information

Acknowledgements
DyLight® is a trademark of Thermo Fisher Scientific Inc. and its subsidiaries
Acknowledgements
DyLight® is a trademark of Thermo Fisher Scientific Inc. and its subsidiaries.
Acknowledgements
DyLight® is a trademark of Thermo Fisher Scientific Inc. and its subsidiaries.
Regulatory
For research purposes only

Applications of Tubulin Alpha antibody

This product has been reported to work in the following applications. This information is derived from testing within our laboratories, peer-reviewed publications or personal communications from the originators. Please refer to references indicated for further information. For general protocol recommendations, please visit the antibody protocols page.
Application Name Verified Min Dilution Max Dilution
ELISA
Immunohistology - Frozen
Western Blotting 1/100 1/1000
ELISA 1/100 1/1000
Immunofluorescence
Immunohistology - Frozen
Immunoprecipitation
Radioimmunoassays
Western Blotting
Western Blotting
Western Blotting
Western Blotting
Where this antibody has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. It is recommended that the user titrates the antibody for use in their own system using appropriate negative/positive controls.
Where this antibody has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. It is recommended that the user titrates the antibody for use in their own system using appropriate negative/positive controls.
Where this antibody has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. It is recommended that the user titrates the antibody for use in their own system using appropriate negative/positive controls
Where this antibody has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. It is recommended that the user titrates the antibody for use in their own system using appropriate negative/positive controls
Where this antibody has not been tested for use in a particular technique this does not necessarily exclude its use in such procedures. It is recommended that the user titrates the antibody for use in their own system using appropriate negative/positive controls.
Western Blotting
MCA77P is suitable for use as a loading control.
Western Blotting
MCA77G is suitable for use as a loading control.
Western Blotting
MCA77D800 is suitable for use as a loading control
Western Blotting
MCA77D680 is suitable for use as a loading control
Western Blotting
MCA77D750 is suitable for use as a loading control.

Secondary Antibodies Available

Description Product Code Pack Size Applications List Price Quantity
Goat anti Rat IgG:Alk. Phos. (Mouse Adsorbed) STAR131A 1 ml C E P WB
Goat anti Rat IgG:Biotin (Mouse Adsorbed) STAR131B 0.5 mg C E IF P WB
Rabbit F(ab')2 anti Rat IgG:Dylight®800 STAR16D800GA 0.1 mg F IF WB
Rabbit F(ab')2 anti Rat IgG:FITC STAR17B 1 mg F
Rabbit F(ab')2 anti Rat IgG:HRP STAR21B 1 mg C E P RE
Goat F(ab')2 anti Rat IgG:FITC (Mouse Adsorbed) STAR69 0.5 ml F
Goat anti Rat IgG:DyLight®649 (Mouse Adsorbed) STAR71D649GA 0.1 mg F IF
Goat anti Rat IgG:Dylight®800 (Mouse Adsorbed) STAR71D800GA 0.1 mg F IF WB
Goat anti Rat IgG:HRP (Mouse Adsorbed) STAR72 0.5 mg C E P
Goat F(ab')2 anti Rat IgG:RPE (Mouse Adsorbed) STAR73 0.5 ml F

Useful Reagents Available

Description Product Code Pack Size Applications List Price Quantity
AbGUARD® HRP Stabilizer Plus BUF052A 100 ml C E P WB
AbGUARD® HRP Stabilizer Plus BUF052B 500 ml C E P WB
AbGUARD® HRP Stabilizer Plus BUF052C 1000 ml C E P WB
TMB Signal+ BUF054A 100 ml E
TMB Core BUF056A 100 ml E
TMB Core+ BUF062A 100 ml E

Application Based External Images

Immunofluorescence

Western Blotting

Product Specific References

References for Tubulin Alpha antibody

  1. Kilmartin, J.V. et al. (1982) Rat monoclonal antitubulin antibodies derived by using a new nonsecreting rat cell line.
    J Cell Biol. 93 (3): 576-82.
  2. Wehland, J. et al. (1983) A rat monoclonal antibody reacting specifically with the tyrosylated form of alpha-tubulin. I. Biochemical characterization, effects on microtubule polymerization in vitro, and microtubule polymerization and organization in vivo.
    J Cell Biol. 97 (5 Pt 1): 1467-75.
  3. Wallace, S.W. et al. (2010) Cdc42 regulates apical junction formation in human bronchial epithelial cells through PAK4 and Par6B.
    Mol Biol Cell. 21 (17): 2996-3006.
  4. Wehland, J. et al. (1984) Amino acid sequence requirements in the epitope recognized by the alpha-tubulin-specific rat monoclonal antibody YL 1/2.
    EMBO J. 3 (6): 1295-300.
  5. Burns, R. (1987) Cytoskeleton. Tubulin's terminal tyrosine.
    Nature. 327 (6118): 103-4.
  6. Skinner, R.H. et al. (1991) Use of the Glu-Glu-Phe C-terminal epitope for rapid purification of the catalytic domain of normal and mutant ras GTPase-activating proteins.
    J Biol Chem. 266 (22): 14163-6.
  7. Abe, Y. et al. (2010) A single starfish Aurora kinase performs the combined functions of Aurora-A and Aurora-B in human cells.
    J Cell Sci. 123: 3978-88.
  8. Cheishvili, D. et al. (2011) Involvement in Cytoskeleton Regulation and Implication for Familial Dysautonomia.
    Hum Mol Genet. 20: 1585-94.
  9. Berrueta, L. et al. (1998) The adenomatous polyposis coli-binding protein EB1 is associated with cytoplasmic and spindle microtubules.
    Proc Natl Acad Sci U S A. 95: 10596-601.
  10. Bruce, E.A. et al. (2010) The Rab11 pathway is required for influenza A virus budding and filament formation.
    J Virol. 84: 5848-59.
  11. Jager, M. et al. (2008) Insights into the early evolution of SOX genes from expression analyses in a ctenophore.
    J Exp Zool B Mol Dev Evol. 310: 650-67.
  12. Wise, H.M. et al. (2011) Overlapping signals for translational regulation and packaging of influenza A virus segment 2.
    Nucleic Acids Res. 39: 7775-90.
  13. Zenner, H.L. et al. (2011) Analysis of Rab GTPase-Activating Proteins Indicates that Rab1a/b and Rab43 Are Important for Herpes Simplex Virus 1 Secondary Envelopment.
    J Virol. 85: 8012-21.
  14. Timm, T. et al. (2011) Microtubule affinity regulating kinase (MARK) activity in living neurons examined by a genetically encoded FRET/FLIM based biosensor: Inhibitors with therapeutic potential.
    J Biol Chem. 286: 41711-22.
  15. Virágh, E. et al. (2012) Specific Cooperation Between Imp-α2 and Imp-β/Ketel in Spindle Assembly During Drosophila Early Nuclear Divisions.
    G3 (Bethesda). 2 (1): 1-14.
  16. Courtois, A. et al. (2012) The transition from meiotic to mitotic spindle assembly is gradual during early mammalian development.
    J Cell Biol. 198: 357-70.
  17. Feau, S. et al. (2013) SLAT Regulates CD8+ T Cell Clonal Expansion in a Cdc42- and NFAT1-Dependent Manner.
    J Immunol. 190: 174-83.
  18. Wise, H.M. et al. (2012) Identification of a novel splice variant form of the influenza A virus M2 ion channel with an antigenically distinct ectodomain.
    PLoS Pathog. 8(11): e1002998.
  19. Dayraud, C. et al. (2012) Independent specialisation of myosin II paralogues in muscle vs. non-muscle functions during early animal evolution: a ctenophore perspective.
    BMC Evol Biol. 12: 107.
  20. Ligon, L.A. et al. (2003) The microtubule plus-end proteins EB1 and dynactin have differential effects on microtubule polymerization.
    Mol Biol Cell. 14: 1405-17.
  21. Smertenko, A.P. et al. (2008) The C-terminal variable region specifies the dynamic properties of Arabidopsis microtubule-associated protein MAP65 isotypes.
    Plant Cell. 20: 3346-58.
  22. Li, Y. et al. (2010) The type II Arabidopsis formin14 interacts with microtubules and microfilaments to regulate cell division.
    Plant Cell. 22: 2710-26.
  23. Brunk, K. et al. (2007) Microcephalin coordinates mitosis in the syncytial Drosophila embryo.
    J Cell Sci. 120: 3578-88.
  24. Gordon-Weeks, R. et al. (2003) Restricted spatial expression of a high-affinity phosphate transporter in potato roots.
    J Cell Sci.116: 3135-44.
  25. Bodor, D.L. et al. (2013) Assembly in G1 phase and long-term stability are unique intrinsic features of CENP-A nucleosomes.
    Mol Biol Cell. 24: 923-32.
  26. De Faveri, L.E. et al. (2013) Putative tumour suppressor gene necdin is hypermethylated and mutated in human cancer.
    Br J Cancer. 108: 1368-77.
  27. Machado, E. et al. (2007) Prostaglandin signaling and ovarian follicle development in the silkmoth, Bombyx mori.
    Insect Biochem Mol Biol. 37: 876-85.
  28. Meseroll, R.A. et al. (2012) Septin ring size scaling and dynamics require the coiled-coil region of Shs1p.
    Mol Biol Cell. 23: 3391-406.
  29. Vafopoulou, X. (2009) Ecdysteroid receptor (EcR) is associated with microtubules and with mitochondria in the cytoplasm of prothoracic gland cells of Rhodnius prolixus (Hemiptera).
    Arch Insect Biochem Physiol. 72: 249-62.
  30. Levy, G.V. et al. (2015) Depletion of the SR-Related Protein TbRRM1 Leads to Cell Cycle Arrest and Apoptosis-Like Death in Trypanosoma brucei.
    PLoS One. 10 (8): e0136070.
  31. Iwasaki, D. et al. (2016) The MRX Complex Ensures NHEJ Fidelity through Multiple Pathways Including Xrs2-FHA-Dependent Tel1 Activation.
    PLoS Genet. 12 (3): e1005942.
  32. Zasadil, L.M. et al. (2016) High rates of chromosome missegregation suppress tumor progression but do not inhibit tumor initiation.
    Mol Biol Cell. 27 (13): 1981-9.
  33. Vafopoulou, X. & Steel, C.G. (2012) Cytoplasmic travels of the ecdysteroid receptor in target cells: pathways for both genomic and non-genomic actions.
    Front Endocrinol (Lausanne). 3: 43.
  34. Vafopoulou, X. & Steel, C.G. (2016) Mitochondria and the insect steroid hormone receptor (EcR): A complex relationship.
    Gen Comp Endocrinol. pii: S0016-6480(16)30224-6. [Epub ahead of print]
  35. Turnbull, M.L. et al. (2016) The Role of the B-Allele of the Influenza A Virus Segment 8 in Setting Mammalian Host Range and Pathogenicity.
    J Virol. Aug 3. pii: JVI.01205-16. [Epub ahead of print]
  36. Vargas, P. et al. (2016) Innate control of actin nucleation determines two distinct migration behaviours in dendritic cells.
    Nat Cell Biol. 18 (1): 43-53.
  37. Kerr, G.W. et al. (2016) PP2A(Cdc55)'s role in reductional chromosome segregation during achiasmate meiosis in budding yeast is independent of its FEAR function.
    Sci Rep. 6: 30397.
  38. Schlicher, L. et al. (2016) SPATA2 promotes CYLD activity and regulates TNF-induced NF-κB signaling and cell death.
    EMBO Rep. Jul 25. pii: e201642592. [Epub ahead of print]
  39. Gholkar AA et al. (2016) Fatostatin inhibits cancer cell proliferation by affecting mitotic microtubule spindle assembly and cell division.
    J Biol Chem. Aug 12 [Epub ahead of print].
  40. Takáč, T. et al. (2016) Actin depolymerization-induced changes in proteome of Arabidopsis roots.
    J Proteomics. Jun 14. pii: S1874-3919(16)30251-2. [Epub ahead of print]
  41. Kono, K. et al. (2016) Plasma membrane/cell wall perturbation activates a novel cell cycle checkpoint during G1 in Saccharomyces cerevisiae.
    Proc Natl Acad Sci U S A. 113 (25): 6910-5.
  42. Koparir, A. et al. (2015) Novel POC1A mutation in primordial dwarfism reveals new insights for centriole biogenesis.
    Hum Mol Genet. 24 (19): 5378-87.
  43. Liz, M.A. et al. (2014) Neuronal deletion of GSK3β increases microtubule speed in the growth cone and enhances axon regeneration via CRMP-2 and independently of MAP1B and CLASP2.
    BMC Biol. 12: 47.
  44. Jonasson, E.M. et al. (2016) Zds1/Zds2-PP2ACdc55 complex specifies signaling output from Rho1 GTPase.
    J Cell Biol. 212 (1): 51-61.
  45. Nunan, R. et al. (2015) Ephrin-Bs Drive Junctional Downregulation and Actin Stress Fiber Disassembly to Enable Wound Re-epithelialization.
    Cell Rep. 13 (7): 1380-95.
  46. Gaudet, A.D. et al. (2015) Galectin-1 in injured rat spinal cord: implications for macrophage phagocytosis and neural repair.
    Mol Cell Neurosci. 64: 84-94.
  47. Klinger, P. et al. (2017) PEDF Is Associated with the Termination of Chondrocyte Phenotype and Catabolism of Cartilage Tissue.
    Biomed Res Int. 2017: 7183516.
  48. Gao, L. et al. (2017) Afadin orients cell division to position the tubule lumen in developing renal tubules.
    Development. 144 (19): 3511-20.