Anti-Tubulin Alpha (Acetyl K112) antibody

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Product name Anti-Tubulin Alpha (Acetyl K112) antibody
Short Description Rabbit polyclonal against Tubulin alpha (Acetyl K112)
Description Rabbit polyclonal to Acetyl-Tubulin alpha (K112).
Applications ELISA, WB
Dilution range WB 1:500-1:2000
ELISA 1:20000
Specificity Acetyl-Tubulin alpha (K112) polyclonal antibody detects endogenous levels of Tubulin alpha protein only when acetylated at K112.
Protein Name Tubulin Alpha-1a Chain
Alpha-Tubulin 3
Tubulin B-Alpha-1
Tubulin Alpha-3 Chain [Cleaved Into-Detyrosinated Tubulin Alpha-1a Chain]
Immunogen Synthesized peptide derived from human Tubulin alpha around the acetylation site of K112.
Immunogen Region acetylation site of K112.
Storage Instruction Store at-20°C, and avoid repeat freeze-thaw cycles.
Note FOR RESEARCH USE ONLY (RUO).
Host Rabbit
Clonality Polyclonal
Reactivity Human, Mouse, Rat
Conjugation Unconjugated
Concentration 1 mg/ml
Purification The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Isotype IgG
Formulation Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Gene ID 7846
Gene Symbol TUBA1A
Molecular Weight 50 kDa
Database Links HGNC:20766
OMIM:602529
Alternative Names Anti-Tubulin Alpha-1a Chain antibody
Anti-Alpha-Tubulin 3 antibody
Anti-Tubulin B-Alpha-1 antibody
Anti-Tubulin Alpha-3 Chain [Cleaved Into-Detyrosinated Tubulin Alpha-1a Chain] antibody
Anti-TUBA1A TUBA3 antibody
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.
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 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-451 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.; [Tubulin alpha-1A chain]: Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1. 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.; [Detyrosinated tubulin alpha-1A chain]: 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.
Cellular Localization Cytoplasm
Cytoskeleton
Tissue Specificity Expressed at a high level in fetal brain.
Swiss-Prot Key TBA1A_HUMAN
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