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Rabbit Polyclonal Acetyl-Tubulin alpha (K352) antibody (STJ90155)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, ELISA
Recommended dilution: WB 1:500-1:2000; ELISA 1:20000;
Recommended protocols: check protocols
Click or hover above images to see image description for Tubulin alpha (Acetyl Lys352) Polyclonal Antibody.
Check alternative names for the antibodyExpand
TUBA1A antibody, TUBA3 antibody,|Alpha tubulin 3 antibody|Alpha-tubulin 3 antibody|B alpha 1 antibody|FLJ25113 antibody|LIS3 antibody|TBA1A_HUMAN antibody|TUBA1A antibody|TUBA3 antibody|Tubulin alpha 1a antibody|Tubulin alpha 1A chain antibody|Tubulin alpha 3 antibody|Tubulin alpha 3 chain antibody|Tubulin alpha brain specific antibody|Tubulin alpha-1A chain antibody|Tubulin alpha-3 chain antibody|Tubulin B alpha 1 antibody|Tubulin B-alpha-1 antibody|Anti-TUBA1A antibody – C-terminal (ab200216)
SCBT cat No: sc-134237|sc-135659|
Tubulin alpha (Acetyl Lys352) Polyclonal Antibody
|Catalogue No.|| |
Human, Mouse, Rat
Acetyl-Tubulin alpha (K352) Polyclonal Antibody detects endogenous levels of Tubulin alpha protein only when acetylated at K352.
Synthesized acetyl-peptide derived from the human Tubulin alpha around the acetylation site of K352
|Recommended dilution|| |
WB 1:500-1:2000; ELISA 1:20000;
|Molecular weight|| |
Tubulin alpha (Acetyl Lys352) Antibody was tube-contained. Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Tubulin alpha (Acetyl Lys352) Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
Tubulin alpha-1A chain antibody, Alpha-tubulin 3 antibody, Tubulin B-alpha-1 antibody, Tubulin alpha-3 chain antibody
|Protein names|| |
Tubulin alpha-1A chain , Alpha-tubulin 3 , Tubulin B-alpha-1 , Tubulin alpha-3 chain
|Protein 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.
|Protein tissue specificity|| |
Expressed at a high level in fetal brain.
|Involvement in disease|| |
Lissencephaly 3 (LIS3) [MIM:611603]: A classic type lissencephaly associated with psychomotor retardation and seizures. Features include agyria or pachygyria or laminar heterotopia, severe mental retardation, motor delay, variable presence of seizures, and abnormalities of corpus callosum, hippocampus, cerebellar vermis and brainstem. . Note: The disease is caused by mutations affecting the gene represented in this entry.
|Protein sequence and domain|| |
Belongs to the tubulin family.
|Protein post-translational modifications|| |
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 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarity). / Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively.
|Protein cellular localization|| |
Cytoplasm > cytoskeleton
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St John’s Laboratory Ltd.
|Product type|| |
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