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AB195584

alpha Tubulin peptide

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(0 Publication)

alpha Tubulin peptide is a Synthetic blocking peptide.

View Alternative Names

TUBA1, TUBA4A, Tubulin alpha-4A chain, Alpha-tubulin 1, Testis-specific alpha-tubulin, Tubulin H2-alpha, Tubulin alpha-1 chain

Key facts

Tags

Tag free

Applications

BL

applications

Biologically active

No

Accession

P68366

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.2 Preservative: 0.02% Sodium azide Constituents: 99.88% PBS, 0.1% BSA

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "BL": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Product details

This is the blocking peptide for ab106375

Sequence info

[{"sequence":"","proteinLength":null,"predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Synthetic","expressionSystem":null,"accessionNumber":"P68366","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
False

Specifications

Form

Liquid

General info

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.

Sequence similarities

Belongs to the tubulin family.

Post-translational modifications

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 (MATCAP1/KIAA0895L) (PubMed:35482892).

Subcellular localisation

Cytoskeleton

Product protocols

Target data

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.
See full target information TUBA4A

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