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AB164660

重组人 TUBA1C 蛋白 (GST tag N-Terminus)

Recombinant Human TUBA1C protein (GST tag N-Terminus)

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(1 Publication)

Recombinant Human TUBA1C protein (GST tag N-Terminus) is a Human Full Length protein, in the 1 to 449 aa range, expressed in Wheat germ, suitable for ELISA, WB.

查看别名

TUBA6, TUBA1C, Tubulin alpha-1C chain, Alpha-tubulin 6, Tubulin alpha-6 chain

1 Images
SDS-PAGE - Recombinant Human TUBA1C protein (AB164660)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human TUBA1C protein (AB164660)

ab164660 on a 12.5% SDS-PAGE stained with Coomassie Blue.

关键信息

表达系统

Wheat germ

标签

GST tag N-Terminus

应用

ELISA, WB

applications

生物活性

No

访问

Q9BQE3

不含动物源

No

不含载体蛋白

No

种属

Human

存储溶液

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

反应性数据

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

序列信息

[{"sequence":"MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLTVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAVAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGADSADGEDEGEEY","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":449,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"Q9BQE3","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

性能和储存信息

运输条件
Dry Ice
推荐的短期储存条件
-80°C
推荐的长期储存条件
-80°C
分装信息
Upon delivery aliquot
储存信息
Avoid freeze / thaw cycle
False

补充信息

This supplementary information is collated from multiple sources and compiled automatically.

TUBA1C also known as tubulin alpha-1C chain is a protein that functions as a component of microtubules which are integral parts of the cytoskeleton in eukaryotic cells. TUBA1C has a molecular mass of approximately 50 kDa. These proteins polymerize to form microtubules essential for various cellular processes such as axonal growth cell division and intracellular transport. TUBA1C is mainly expressed in brain tissues but can also be found in other organ systems indicating its role beyond neuronal function.
Biological function summary

The tubulin alpha-1C chain plays a significant role in stabilizing cellular structures and facilitating cell division by forming the mitotic spindle. It participates in forming a heterodimer with beta-tubulin a basic structural unit of microtubules. This heterodimer assembles into microtubule filaments which are critical for cell shape and transport mechanisms. TUBA1C as part of the microtubule network helps guide the signaling pathways that are important for neuron functionality and brain development.

Pathways

TUBA1C is an important player in the mitotic cell cycle and the intracellular transport pathway. It works closely with beta-tubulin to regulate the assembly and disassembly of microtubules which are important steps in cell division and transport within cells. Additionally TUBA1C interacts with MAPs (microtubule-associated proteins) which regulate the dynamics of microtubule systems impacting how cells react to environmental changes and signaling cues during the cell cycle.

Aberrant expression or dysfunction of TUBA1C has been linked to neurodevelopmental disorders and certain types of cancer. Disruption in TUBA1C function can lead to improper neuron migration resulting in conditions such as lissencephaly. Its involvement in cancer relates to its critical role in cell division where abnormal activity can contribute to uncontrolled proliferation. TUBA1C is often examined together with MAPs and other tubulin isoforms in studies related to these diseases to better understand their complex interactions and develop potential therapeutic interventions.

特殊说明

形式

Liquid

常规信息

功能

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.

序列相似性

Belongs to the tubulin family.

翻译后修饰

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.. Nitration of Tyr-449 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 (MATCAP1/KIAA0895L, VASH1 or VASH2) and tubulin tyrosine ligase (TTL), respectively.. Tubulin alpha-1C chain. Tyrosination promotes microtubule interaction with CAP-Gly domain-containing proteins such as CLIP1, CLIP2 and DCTN1 (By similarity). Tyrosination regulates the initiation of dynein-dynactin motility via interaction with DCTN1, which brings the dynein-dynactin complex into contact with microtubules (PubMed:26972003). In neurons, tyrosinated tubulins mediate the initiation of retrograde vesicle transport (By similarity).. Detyrosinated tubulin alpha-1C 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).

亚细胞定位

Cytoskeleton

产品实验方案

靶点信息

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 TUBA1C

文献 (1)

Recent publications for all applications. Explore the full list and refine your search

Scientific reports 12:10568 PubMed35732702

2022

SILAC kinase screen identifies potential MASTL substrates.

Applications

Unspecified application

Species

Unspecified reactive species

Kamila A Marzec,Samuel Rogers,Rachael McCloy,Benjamin L Parker,David E James,D Neil Watkins,Andrew Burgess
View all publications

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