Product: TUBA3C/E Antibody
Catalog: DF4727
Description: Rabbit polyclonal antibody to TUBA3C/E
Application: WB IF/ICC
Reactivity: Human, Mouse, Rat
Mol.Wt.: 50 KD; 50kD(Calculated).
Uniprot: Q13748 | Q6PEY2
RRID: AB_2837078

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 100ul $280 In stock
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Product Info

Source:
Rabbit
Application:
WB 1:500-1:1000, 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:
TUBA3C/E Antibody detects endogenous levels of total TUBA3C/E.
RRID:
AB_2837078
Cite Format: Affinity Biosciences Cat# DF4727, RRID:AB_2837078.
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 2; Alpha-tubulin 3C/D; alpha-tubulin isotype H2-alpha; H2-ALPHA; TBA3C_HUMAN; TUBA2; TUBA3C; TUBA3D; Tubulin alpha 2; Tubulin alpha 2 chain; Tubulin alpha 3c; Tubulin alpha-2 chain; Tubulin alpha-3C/D chain; Alpha-tubulin 3; H2 ALPHA; TBA1A_HUMAN; TUBA1A; TUBA3C; TUBA3D; TUBA3E; Tubulin alpha 3E chain; Tubulin alpha-1A chain; Tubulin alpha-3 chain; Tubulin B-alpha-1; Tubulin, alpha 1a; Tubulin, alpha 1b; Tubulin, alpha 1c; Tubulin, alpha 3c; Tubulin, alpha 3e;

Immunogens

Immunogen:

A synthesized peptide derived from human TUBA3C/E, corresponding to a region within C-terminal amino acids.

Uniprot:
Gene(ID):
Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAASNYARGHYTIGKEIVDLVLDRIRKLADLCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYSKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLVHKFDLMYAKWAFVHWYVGEGMEEGEFSEAREDLAALEKDCEEVGVDSVEAEAEEGEAY

PTMs - Q13748/Q6PEY2 As Substrate

Site PTM Type Enzyme
S6 Phosphorylation
Y24 Phosphorylation
S38 Phosphorylation
K40 Acetylation
K40 Ubiquitination
T41 Phosphorylation
S48 Phosphorylation
T51 Phosphorylation
S54 Phosphorylation
T56 Phosphorylation
K60 Acetylation
K60 Sumoylation
K60 Ubiquitination
R79 Methylation
T80 Phosphorylation
T82 Phosphorylation
T94 Phosphorylation
R105 Methylation
Y108 Phosphorylation
T109 Phosphorylation
R156 Methylation
Y185 Phosphorylation
S187 Phosphorylation
T190 Phosphorylation
T193 Phosphorylation
T194 Phosphorylation
S198 Phosphorylation
Y210 Phosphorylation
T223 Phosphorylation
Y224 Phosphorylation
T225 Phosphorylation
S236 Phosphorylation
S237 Phosphorylation
T253 Phosphorylation
T257 Phosphorylation
Y262 Phosphorylation
T271 Phosphorylation
Y272 Phosphorylation
S277 Phosphorylation
K280 Ubiquitination
Y282 Phosphorylation
S287 Phosphorylation
T292 Phosphorylation
K304 Ubiquitination
K326 Acetylation
K326 Sumoylation
K326 Ubiquitination
T334 Phosphorylation
K336 Acetylation
K336 Sumoylation
K336 Ubiquitination
T337 Phosphorylation
K338 Methylation
K338 Ubiquitination
T340 Phosphorylation
T349 Phosphorylation
K352 Acetylation
K352 Sumoylation
K352 Ubiquitination
Y357 Phosphorylation
T361 Phosphorylation
K370 Acetylation
K370 Sumoylation
K370 Ubiquitination
S379 Phosphorylation
Y399 Phosphorylation
K401 Ubiquitination
Y408 Phosphorylation
S419 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 (By similarity).

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-450 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
Subunit Structure:

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.

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.

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