Beta II tubulin antibody - #BF0716
Product: | Beta II tubulin antibody |
Catalog: | BF0716 |
Description: | Mouse monoclonal antibody to Beta II tubulin |
Application: | WB IP |
Reactivity: | Human, Mouse, Rat |
Mol.Wt.: | 55kDa; 50kD(Calculated). |
Uniprot: | Q13885 |
RRID: | AB_2846193 |
Product Info
*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.
Cite Format: Affinity Biosciences Cat# BF0716, RRID:AB_2846193.
Fold/Unfold
β II Tubulin;Beta2;TBB4B_HUMAN;TUBB 2;TUBB2 ;Tubb4b;Tubulin beta 2;
Immunogens
Purified recombinant fragment of human Beta II tubulin expressed in E. Coli.
- Q13885 TBB2A_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MREIVHIQAGQCGNQIGAKFWEVISDEHGIDPTGSYHGDSDLQLERINVYYNEAAGNKYVPRAILVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDSVLDVVRKESESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTFSVMPSPKVSDTVVEPYNATLSVHQLVENTDETYSIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDSKNMMAACDPRHGRYLTVAAIFRGRMSMKEVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMSATFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATADEQGEFEEEEGEDEA
PTMs - Q13885 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
R2 | Methylation | Uniprot | |
K19 | Acetylation | Uniprot | |
K19 | Methylation | Uniprot | |
T33 | Phosphorylation | Uniprot | |
S35 | Phosphorylation | Uniprot | |
Y36 | Phosphorylation | Uniprot | |
Y50 | Phosphorylation | Uniprot | |
K58 | Ubiquitination | Uniprot | |
T72 | Phosphorylation | Uniprot | |
S75 | Phosphorylation | Uniprot | |
S78 | Phosphorylation | Uniprot | |
S95 | Phosphorylation | Uniprot | |
K103 | Acetylation | Uniprot | |
K103 | Sumoylation | Uniprot | |
K103 | Ubiquitination | Uniprot | |
Y106 | Phosphorylation | Uniprot | |
T107 | Phosphorylation | Uniprot | |
S115 | Phosphorylation | Uniprot | |
K122 | Ubiquitination | Uniprot | |
S126 | Phosphorylation | Uniprot | |
K154 | Ubiquitination | Uniprot | |
Y159 | Phosphorylation | Uniprot | |
R162 | Methylation | Uniprot | |
T166 | Phosphorylation | Uniprot | |
S168 | Phosphorylation | Uniprot | |
S172 | Phosphorylation | Uniprot | |
Y183 | Phosphorylation | Uniprot | |
Y208 | Phosphorylation | Uniprot | |
K216 | Ubiquitination | Uniprot | |
T218 | Phosphorylation | Uniprot | |
T219 | Phosphorylation | Uniprot | |
T221 | Phosphorylation | Uniprot | |
Y222 | Phosphorylation | Uniprot | |
S234 | Phosphorylation | Uniprot | |
K252 | Sumoylation | Uniprot | |
K252 | Ubiquitination | Uniprot | |
T274 | Phosphorylation | Uniprot | |
S275 | Phosphorylation | Q5TCY1 (TTBK1) | Uniprot |
R276 | Methylation | Uniprot | |
S278 | Phosphorylation | Uniprot | |
Y281 | Phosphorylation | Uniprot | |
T290 | Phosphorylation | Uniprot | |
K297 | Ubiquitination | Uniprot | |
S322 | Phosphorylation | Uniprot | |
K324 | Acetylation | Uniprot | |
K324 | Sumoylation | Uniprot | |
K324 | Ubiquitination | Uniprot | |
K336 | Acetylation | Uniprot | |
K336 | Ubiquitination | Uniprot | |
S338 | Phosphorylation | Uniprot | |
S339 | Phosphorylation | Uniprot | |
Y340 | Phosphorylation | Uniprot | |
K350 | Sumoylation | Uniprot | |
K350 | Ubiquitination | Uniprot | |
T351 | Phosphorylation | Uniprot | |
K362 | Ubiquitination | Uniprot | |
T366 | Phosphorylation | Uniprot | |
K379 | Acetylation | Uniprot | |
K379 | Ubiquitination | Uniprot | |
S382 | Phosphorylation | Uniprot | |
T386 | Phosphorylation | Uniprot | |
K392 | Ubiquitination | Uniprot | |
T399 | Phosphorylation | Uniprot |
Research Backgrounds
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 (By similarity).
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.
Cytoplasm>Cytoskeleton.
High expression in brain, where it represents 30% of all beta-tubulins.
Interacts with ZNRF1 (By similarity). Part of a complex composed at least of ASCL2, EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5, TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-specific methyltransferase activity (By similarity). Dimer 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.
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.
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