Tubulin Alpha Antibody #abs131993

abs131993-50ug

In Stock

201

abs131993-100ug

In Stock

301

Description

The major component of microtubules is Tubulin protein known as TUBA1B. It consists of two subunits, alpha and beta chains, forming a dimer. TUBA1B binds to two molecules of GTP, one on the exchangeable site of the beta chain and one on the non-exchangeable site of the alpha-chain. It is a member of the tubulin protein family.

Source

Rabbit

Specificity

The detectable levels of total Tubulin alpha can be measured using the Tubulin alpha Antibody, which is specifically designed to identify the endogenous presence of Tubulin alpha.

Species Reactivity

Human;Mouse;Rat;Pig;Bovine;Rabbit;Chicken;Fish

Predictive reaction species

Pig;Sheep;Dog;Bovine;Horse

Application

The dilution ratios for Western blotting range from 1:5000 to 1:20000, while for immunohistochemistry it is 1:50 to 1:200. As for immunofluorescence/immunocytochemistry, the ratios are 1:100 to 1:500. Lastly, for ELISA using peptides, the recommended dilution range is 1:20000 to 1:40000.

Immunogen

α-。，。

Properties

Concentration

1mg/ml

Purification

Peptide affinity chromatography was utilized to purify the antiserum, employing SulfoLink™ Coupling Resin as the main component of the process.

Clonality

Polyclonal Antibody

Stability & Storage

To ensure the integrity of the stored product, it is recommended to keep it at a temperature of -20 °C for a duration of one year. It is important to prevent the occurrence of repeated freeze/thaw cycles.

Storage buffer

This product contains Rabbit IgG in phosphate buffered saline with a pH of 7.4, 150mM NaCl, 0.02% sodium azide, and 50% glycerol. It should be stored at a temperature of -20°C for optimal stability, and has a shelf life of 12 months from the date of receipt. Ensure that you maintain the integrity of the original text information while re-arranging it to generate a new content that is highly similar.

Target

Background

Microtubules are primarily made up of tubulin, which is a vital component of these structures. It has the ability to bind two molecules of GTP, with one being located at an exchangeable site on the beta chain and the other at a non-exchangeable site on the alpha chain.

Tissue specificity

Expressed at a high level in fetal brain.

Posttranslational modification

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).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 (TTCP) 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 (PubMed:26972003, PubMed:26968983). In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (PubMed:26968983).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 (PubMed:25908662). 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).

Celluar localization

Cytoskeleton;Cytosol;Endosome;Extracellular region or secreted;Nucleus;

UniPort

Q71U36/P68363