TBCEL Human

Tubulin Folding Cofactor E-Like Human Recombinant
Cat. No.
BT20282
Source
Escherichia Coli.
Synonyms

Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.

Appearance
Sterile filtered colorless solution.
Purity
Greater than 95% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

TBCEL  Recombinant Human produced in E.Coli is a single, non-glycosylated polypeptide chain containing 447 amino acids and having a molecular mass of 50.6kDa. 
The TBCEL is purified by proprietary chromatographic techniques.

Product Specs

Introduction
TBCEL is a crucial factor responsible for regulating cell behavior by influencing the microtubule cytoskeleton. Its primary function is to modulate tubulin stability. Although predominantly found in the testis, TBCEL is also present in various other tissues, albeit at lower levels. Structurally, TBCEL consists of seven leucine-rich (LRR) repeats, one LRRCT domain, and one ubiquitin-like domain. The gene encoding TBCEL spans 66,704 bases and is located on human chromosome 11q23.3. Chromosome 11, harboring over 1,400 genes, represents approximately 4% of the human genome. Notably, defects in genes located on chromosome 11 are linked to several disorders, including Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema, and Smith-Lemli-Opitz syndrome.
Description
Recombinant Human TBCEL, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 447 amino acids. It has a molecular weight of 50.6 kDa. The purification of TBCEL is achieved through proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution, sterilized by filtration.
Formulation
TBCEL is supplied as a 1 mg/ml solution in 20mM Tris-HCl buffer (pH 8.0), containing 0.15M NaCl, 20% glycerol, and 1mM DTT.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze at -20°C. The addition of a carrier protein like HSA or BSA (0.1%) is advisable for long-term storage. Repeated freeze-thaw cycles should be avoided.
Purity
The purity of TBCEL is determined to be greater than 95% by SDS-PAGE analysis.
Synonyms

Tubulin Folding Cofactor E-Like, E-Like, LRRC351, Leucine Rich Repeat Containing Catastrophin, Tubulin-Specific Chaperone E-Like.

Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDQPSGR SFMQVLCEKY SPENFPYRRG PGMGVHVPAT PQGSPMKDRL NLPSVLVLNS CGITCAGDEK EIAAFCAHVS ELDLSDNKLE DWHEVSKIVS NVPQLEFLNL SSNPLNLSVL ERTCAGSFSG VRKLVLNNSK ASWETVHMIL QELPDLEELF 
LCLNDYETVS CPSICCHSLK LLHITDNNLQ DWTEIRKLGV MFPSLDTLVL ANNHLNAIEE PDDSLARLFP NLRSISLHKS GLQSWEDIDK  LNSFPKLEEV RLLGIPLLQP YTTEERRKLV IARLPSVSKL NGSVVTDGER EDSERFFIRY YVDVPQEEVP FRYHELITKY GKLEPLAEVD 
LRPQSSAKVE VHFNDQVEEM SIRLDQTVAE LKKQLKTLVQ LPTSNMLLYY FDHEAPFGPE EMKYSSRALH SFGIRDGDKI YVESKTK.

Product Science Overview

Introduction

Tubulin Folding Cofactor E-Like (TBCEL) is a protein that plays a crucial role in the proper folding and stability of tubulin, a key component of the microtubule cytoskeleton. Microtubules are essential for various cellular functions, including cell division, intracellular transport, and maintenance of cell shape. TBCEL is a human recombinant protein that has been studied for its involvement in tubulin dynamics and its potential implications in various diseases.

Tubulin and Microtubule Dynamics

Microtubules are dynamic structures composed of α- and β-tubulin heterodimers. They undergo continuous phases of growth and shrinkage, a phenomenon known as dynamic instability. This dynamic behavior is regulated by various proteins, including tubulin-specific chaperones and microtubule-associated proteins (MAPs). Tubulin-specific chaperones, such as cofactors A to E, are responsible for the correct folding and assembly of tubulin dimers .

Role of TBCEL

TBCEL is a member of the tubulin-specific chaperone family and is closely related to Tubulin Folding Cofactor E (TBCE). It is involved in the post-chaperonin tubulin folding pathway and plays a role in the assembly and stability of the tubulin complex . TBCEL acts as a regulator of tubulin stability by binding to α-tubulin and promoting its degradation through the proteasomal pathway . This function is crucial for maintaining the balance between tubulin polymerization and depolymerization, which is essential for proper microtubule dynamics.

Mechanism of Action

TBCEL exerts its function by interacting with tubulin folding intermediates produced via the cytosolic chaperonin CCT (chaperonin containing TCP-1) complex. Upon overexpression, TBCEL depolymerizes microtubules by committing tubulin to proteasomal degradation . This process involves the disruption of the tubulin heterodimer, leading to an increase in the number of stable microtubules and a tight clustering of endocellular membranes around the microtubule-organizing center .

Biological Significance

The regulation of tubulin stability by TBCEL is vital for various cellular processes. Microtubules are involved in the formation of the mitotic spindle during cell division, and their dynamic instability is crucial for accurate chromosome segregation. Additionally, microtubules play a role in intracellular transport, cell motility, and maintenance of cell polarity. Dysregulation of tubulin dynamics can lead to various diseases, including cancer and neurodegenerative disorders .

Clinical Implications

Mutations or alterations in the expression of TBCEL have been associated with certain diseases. For example, TBCEL has been linked to nonsyndromic congenital nail disorders . Understanding the role of TBCEL in tubulin dynamics and its implications in disease can provide insights into potential therapeutic targets for conditions involving microtubule dysfunction.

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