Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
host | mouse |
isotype | IgG2a |
clonality | monoclonal |
concentration | 1 mg/mL |
applications | ICC/IF, IHC, WB |
available sizes | 1 mg, 100 µg, 25 µg |
mouse anti-beta Tubulin monoclonal antibody (4E4) 1222
$100.00 – $2,600.00
Antibody summary
- Mouse monoclonal to beta Tubulin
- Suitable for: WB, ICC/IF, IHC
- Reacts with: human, mouse, rat
- Isotype: IgG2a
- 100 µg, 25 µg, 1 mg
mouse anti-beta Tubulin monoclonal antibody (4E4) 1222
target relevance |
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Beta tubulin is a structural component of microtubules, beta-tubulin plays a fundamental role in maintaining cell shape, supporting intracellular transport, and facilitating cell division. Due to its stable expression levels and essential cellular functions, beta-tubulin has become widely recognized as a valuable loading control in various experimental techniques, such as Western blotting and immunoblotting. Its consistent presence in most eukaryotic cells ensures that its expression remains relatively constant, making it an ideal reference protein for normalizing and quantifying target protein levels accurately. This antibody can be used as a loading control when run alongside proteins of interest with different and resolvable molecular weights and ideally in combination with antibodies of same host and when using a secondary antibody. Click for more on: loading controls and beta Tubulin |
Protein names Tubulin beta chain (Tubulin beta-5 chain) |
Gene names TUBB,TUBB TUBB5 OK/SW-cl.56 |
Protein family Tubulin family |
Mass 49671Da |
Function Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin. |
Subellular location Cytoplasm, cytoskeleton |
Tissues Ubiquitously expressed with highest levels in spleen, thymus and immature brain. |
Structure 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). Nascent tubulin polypeptide interacts (via beta-tubulin MREI motif) with TTC5/STRAP; this interaction results in tubulin mRNA-targeted degradation (PubMed:31727855). |
Post-translational modification Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866, PubMed:28576883). 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). Glutamylation is also involved in cilia motility (By similarity). ; 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 cilia and flagella axonemes, which is required for their stability and maintenance. Flagella glycylation controls sperm motility (Probable) (PubMed:28576883). Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally (Probable) (PubMed:28576883). ; 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. |
Target Relevance information above includes information from UniProt accession : P07437 |
The UniProt Consortium |
Data
Publications
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.There are 6 publications in our database for this antibody or clone. Here are the latest 5, for more click below.
pmid | title | authors | citation |
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33981285 | Pancreas Optical Clearing and 3-D Microscopy in Health and Diabetes | Campbell-Thompson M, Tang SC. | Front Endocrinol (Lausanne). 2021 Apr 26;12:644826. doi: 10.3389/fendo.2021.644826. eCollection 2021. |
27103327 | Microtubules: 50 years on from the discovery of tubulin | Borisy G, Heald R, Howard J, Janke C, Musacchio A, Nogales E. | Nat Rev Mol Cell Biol. 2016 Apr 22;17(5):322-8. doi: 10.1038/nrm.2016.45. |
26123245 | Physiologically relevant factors influence tau phosphorylation by leucine-rich repeat kinase 2 | Hamm M, Bailey R, Shaw G, Yen SH, Lewis J, Giasson BI. | J Neurosci Res. 2015 Oct;93(10):1567-80. doi: 10.1002/jnr.23614. Epub 2015 Jun 30. |
19671735 | Microtubule inhibitors: Differentiating tubulin-inhibiting agents based on mechanisms of action, clinical activity, and resistance | Perez EA. | Mol Cancer Ther. 2009 Aug;8(8):2086-95. doi: 10.1158/1535-7163.MCT-09-0366. Epub 2009 Aug 11. |
11441808 | Structural insight into microtubule function | Nogales E. | Annu Rev Biophys Biomol Struct. 2001;30:397-420. doi: 10.1146/annurev.biophys.30.1.397. |
Protocols
relevant to this product |
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Western blot IHC ICC |
Documents
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No results found |
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