TPPP Human

Tubulin Polymerization Promoting Protein Human Recombinant
Cat. No.
BT26321
Source
Escherichia Coli.
Synonyms
Tubulin polymerization-promoting protein, TPPP, 25 kDa brain-specific protein, TPPP/p25, p24, p25-alpha, TPPP1, p25, p25alpha.
Appearance
Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 85.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

TPPP Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 229 amino acids including a 10 a.a N-terminal His tag. The total molecular mass is 24.9kDa (calculated).

Product Specs

Introduction
Tubulin Polymerization Promoting Protein (TPPP) is believed to be involved in the process of tubulin polymerization, which forms microtubules. It may also contribute to microtubule bundling and stabilization, thereby preserving the microtubule network's integrity. Additionally, TPPP might play a role in mitotic spindle assembly and the breakdown of the nuclear envelope. Notably, the levels of TPPP/p235 are significantly elevated in the cerebrospinal fluid of individuals with multiple sclerosis.
Description
Recombinant human TPPP, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 229 amino acids, including a 10 amino acid N-terminal His tag. It has a calculated molecular mass of 24.9kDa.
Physical Appearance
White powder, filtered and lyophilized.
Formulation
TPPP was filtered at a pore size of 0.4 µm and subsequently lyophilized from a solution containing 0.5 mg/ml TPPP in a buffer of 0.05 M phosphate and 0.075 M NaCl, at pH 7.4.
Solubility
To prepare a working stock solution, add deionized water to the lyophilized pellet to achieve a concentration of approximately 0.5 mg/ml. Allow the pellet to dissolve completely. Note that TPPP is not sterile. Before use in cell culture, ensure sterility by filtering the product through an appropriate sterile filter.
Stability
The lyophilized protein should be stored at -20°C. After reconstitution, aliquot the product to prevent repeated cycles of freezing and thawing. The reconstituted protein remains stable at 4°C for a limited period; no changes were observed after two weeks at this temperature.
Purity
Purity is determined to be greater than 85.0% using SDS-PAGE analysis.
Synonyms
Tubulin polymerization-promoting protein, TPPP, 25 kDa brain-specific protein, TPPP/p25, p24, p25-alpha, TPPP1, p25, p25alpha.
Source
Escherichia Coli.
Amino Acid Sequence
MKHHHHHHASMADKAKPAKA ANRTPPKSPG DPSKDRAAKR LSLESEGAGE GAAASPELSA LEEAFRRFAV HGDARATGRE MHGKNWSKLC KDCQVIDGRN VTVTDVDIVF SKIKGKSCRT ITFEQFQEAL EELAKKRFKD KSSEEAVREV HRLIEGKAPI ISGVTKAISS PTVSRLTDTT KFTGSHKERF DPSGKGKGKA GRVDLVDESG YVSGYKHAGT YDQKVQGGK.

Product Science Overview

Introduction

Tubulin Polymerization Promoting Protein (TPPP), also known as p25alpha, is a member of a newly identified eukaryotic protein superfamily. This protein family is characterized by the presence of the p25alpha domain (Pfam05517, IPR008907) and is named after the first identified member, TPPP/p25 . TPPP/p25 was originally discovered as a brain-specific protein with an unknown function and is mainly expressed in differentiated oligodendrocytes .

Structure and Function

TPPP/p25 plays a crucial role in the stabilization and polymerization of microtubules, which are essential components of the cytoskeleton. Microtubules provide structural support to cells and are involved in various cellular processes, including cell division, intracellular transport, and maintenance of cell shape . TPPP/p25 facilitates microtubule elongation and regulates tubulin acetylation by inhibiting cytosolic deacetylase enzymes . This regulation is vital for maintaining microtubule stability and function.

Physiological and Pathological Roles

TPPP/p25 is involved in several physiological processes, particularly in the development and function of the brain and the musculoskeletal system . It has been implicated in the regulation of microtubule dynamics, which is essential for proper neuronal function and development . Additionally, TPPP/p25 has been associated with various diseases, including neurodegenerative disorders such as Parkinson’s disease. The pathological association of TPPP/p25 with alpha-synuclein, a protein involved in the etiology of synucleinopathies, highlights its potential role in disease mechanisms .

Recombinant TPPP

Human recombinant TPPP is produced using recombinant DNA technology, which involves inserting the gene encoding TPPP into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of TPPP for research and therapeutic purposes. Recombinant TPPP retains the structural and functional properties of the native protein, making it a valuable tool for studying its role in cellular processes and disease mechanisms.

Research and Therapeutic Potential

Research on TPPP/p25 has provided valuable insights into its role in microtubule dynamics and its potential as a therapeutic target. Inhibiting tubulin polymerization has been shown to be an effective strategy for inhibiting the proliferation of cancer cells . Additionally, understanding the mechanisms by which TPPP/p25 regulates microtubule stability and function could lead to the development of novel therapeutic approaches for neurodegenerative diseases and other conditions associated with microtubule dysfunction .

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