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Mouse Anti-TUBA4A Recombinant Antibody (TUB-1A2) (CBMAB-A4935-YC)


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Summary

Host Animal
Mouse
Specificity
Human, Dog, Mouse
Clone
TUB-1A2
Antibody Isotype
IgG3
Application
ICC, IF, IHC, WB

Basic Information

Immunogen
Synthetic peptide corresponding to the C-terminal doamin of alpha tubulin
Specificity
Human, Dog, Mouse
Antibody Isotype
IgG3
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
0.1% sodium azide
Storage
Store at 4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
TUBA4A Gene(Protein Coding) Tubulin Alpha 4a
Introduction
Microtubules of the eukaryotic cytoskeleton perform essential and diverse functions and are composed of a heterodimer of alpha and beta tubulin. The genes encoding these microtubule constituents are part of the tubulin superfamily, which is composed of si
Entrez Gene ID
Human84790
Mouse22146
Dog478918
UniProt ID
HumanQ9BQE3
MouseP68373
DogA0A8C0MZ87
Alternative Names
TUBA1A; Tuba-1; ALS22; TUBA1; H2-ALPHA; M[a]4; Tuba4; Tuba1
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.
Biological Process
Biological Process microtubule cytoskeleton organization Source:GO_Central1 Publication
Biological Process mitotic cell cycle Source:GO_Central1 Publication
Cellular Location
Cytoplasm, cytoskeleton
Involvement in disease
Amyotrophic lateral sclerosis 22, with or without frontotemporal dementia (ALS22):
A neurodegenerative disorder affecting upper motor neurons in the brain and lower motor neurons in the brain stem and spinal cord, resulting in fatal paralysis. Sensory abnormalities are absent. The pathologic hallmarks of the disease include pallor of the corticospinal tract due to loss of motor neurons, presence of ubiquitin-positive inclusions within surviving motor neurons, and deposition of pathologic aggregates. The etiology of amyotrophic lateral sclerosis is likely to be multifactorial, involving both genetic and environmental factors. The disease is inherited in 5-10% of the cases. Patients with ALS22 may develop frontotemporal dementia.
PTM
Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866).
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. Both polyglutamylation and monoglycylation can coexist on the same protein on adjacent residues, and lowering glycylation levels increases polyglutamylation, and reciprocally.
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.
Although this tubulin does not encode a C-terminal tyrosine, a C-terminal tyrosine can be added post-translationally by the tubulin tyrosine ligase (TTL) (PubMed:35482892).
It can then undergo a detyrosination cycle by the tubulin tyrosine carboxypeptidase (KIAA0895L/MATCAP) (PubMed:35482892).
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For research use only. Not intended for any clinical use.

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