Recombinant Human Tubulin Polymerization-Promoting Protein (TPPP) Protein (GST)

Name: Recombinant Human Tubulin Polymerization-Promoting Protein (TPPP) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-09129P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Tubulin Polymerization-Promoting Protein (TPPP) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O94811
Target Symbol	TPPP
Synonyms	25 kDa brain specific protein ; 25 kDa brain-specific protein; Brain specific protein p25 alpha; Glycogen synthase kinase 3 (GSK3) inhibitor p24; OTTHUMP00000161630; p24; p25; p25-alpha; p25alpha ; TPPP; TPPP/p25; TPPP_HUMAN; TPPP1; Tubulin polymerization promoting protein; Tubulin polymerization-promoting protein
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MADKAKPAKAANRTPPKSPGDPSKDRAAKRLSLESEGAGEGAAASPELSALEEAFRRFAVHGDARATGREMHGKNWSKLCKDCQVIDGRNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGKAPIISGVTKAISSPTVSRLTDTTKFTGSHKERFDPSGKGKGKAGRVDLVDESGYVSGYKHAGTYDQKVQGGK
Expression Range	1-219aa
Protein Length	Full Length
Mol. Weight	50.7kDa
Research Area	Signal Transduction
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath. Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubule nucleation, an important step for elongation of the myelin sheath. Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes. Shows magnesium-dependent GTPase activity; the role of the GTPase activity is unclear. In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network. Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6. Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility. Plays a role in cell proliferation by regulating the G1/S-phase transition. Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis; this process is regulated by phosphorylation by LIMK2.
Subcellular Location	Golgi outpost. Cytoplasm, cytoskeleton, microtubule organizing center. Cytoplasm, cytoskeleton. Nucleus. Cytoplasm, cytoskeleton, spindle.
Protein Families	TPPP family
Database References	HGNC: 24164 OMIM: 608773 KEGG: hsa:11076 STRING: 9606.ENSP00000353785 UniGene: Hs.481466
Tissue Specificity	Widely expressed.

Gene Functions References

TPPP/p25 is co-enriched and co-localized with alpha-synuclein in brain inclusions of Parkinson's disease patients. Interaction of alpha-synuclein with various deletion mutants and fragments of TPPP/p25 were characterized. PMID: 27671864
The objective of this paper is to highlight a critical point of a recently published Skoufias's paper in which the crucial role of the microtubules in TPPP/p25 dimerization leading to microtubule bundling was suggested. PMID: 28074911
This study demonstrated that the AAV9-mediated p25 overexpression mouse model, which is a practical model exhibiting neurodegeneration-like pathological and behavioral changes. PMID: 27258419
The knowledge accumulated so far underlines the key roles of the multifunctional TPPP/p25 in both physiological and diverse pathological processes, consequently its validation as drug target sorely needs a new innovative strategy that is briefly reviewed here. PMID: 28271739
TPPP may have a role in poor prognosis in hepatocellular carcinoma PMID: 27630306
the central folded domain of TPPP/p25 following binding to microtubules can drive s homotypic protein-protein interactions leading to bundled microtubules. PMID: 26289831
Results reveal a link between p25 and BACE1 in Alzheimer disease (AD) brains and suggest that upregulated Cdk5 activation by p25 accelerates AD pathogenesis by enhancing BACE1 activity via phosphorylation. PMID: 26317805
Epigenetic changes in TPPP, in combination with experiences of maltreatment, may confer risk for depression in children. PMID: 24655651
suggest that the zinc as a specific divalent cation could be involved in the fine-tuning of the physiological TPPP/p25 level counteracting both the enrichment and the lack of this protein leading to distinct central nervous system diseases PMID: 25445539
GSK3 promotes the mitochondrial translocation of p53, enabling its interaction with Bcl2 to allow Bax oligomerization and the subsequent release of cytochrome C. PMID: 23161404
dual Rock and Cdk phosphorylation of Tppp1 inhibits its regulation of the cell cycle to increase cell proliferation PMID: 23355470
The RhoA-ROCK-LIMK2-TPPP pathway controls metaphase spindle-orientation; TPPP colocalizes with LIMK2 at the mitotic spindle. PMID: 22328514
Although serine-129 phosphorylation of alpha-synuclein facilitates TPPP-mediated alpha-SYN oligomerization, this modification does not seem to play an inevitable role in the early step of alpha-SYN oligomer formation in a cellular model of multiple system atrophy. PMID: 20849899
The authors conclude that the modest structural changes that p25alpha undergoes can promote weak intermolecular contacts and that polyanions such as heparin play a central role in stabilizing these aggregates. PMID: 22326478
Wnt induces the phosphorylation of LRP6 which consequently access the catalytic pocket of GSK3 as pseudo-substrates, thus directly blocking its activity against beta-catenin. PMID: 22083140
GSK3 has a significant role in maintaining repression of growth factor-inducible genes during quiescence. CREB, NFkB and AP-1 mediate this regulation of gene expression by GSK-3. PMID: 21900749
Data show that TPPP may work as a protective factor for cells against the damage effects of the accumulation of abnormal forms of PrPs, besides its function as an agent for dynamic stabilization of microtubular ultrastructures. PMID: 21857997
Binding of Zn(2) bivalent cation to structurally disordered TPPP/p25 influences TPPP/p25-promoted tubulin polymerization and GTPase activity. PMID: 21995432
Interactions of pathological hallmark proteins: tubulin polymerization promoting protein/p25, beta-amyloid, and alpha-synuclein. PMID: 21832049
This study demonistrated that p25 is generated during spatial memory formation. PMID: 21616478
these investigations suggest the CSF-TPPP/p25 level could become diagnostic marker of MS and other demyelination-related diseases. PMID: 21565174
The RING domain of XIAP (and probably cIAP-1 and cIAP-2) associates with GSK3, GSK3 acts upstream of the apoptosome to promote intrinsic apoptosis, and the association between XIAP and GSK3 may block the pro-apoptotic function of GSK3. PMID: 19698783
TPPP/p25 has a role in stabilization of physiological microtubular ultrastructures and cell survival PMID: 15564385
perhaps p25alpha plays a pro-aggregatory role in the common neurodegenerative disorders hall-marked by alpha-synuclein aggregates PMID: 15590652
Recombinant TPPP plays an important role for tubulin-related transport in developing, myelinating oligodendrocytes. PMID: 16879710
identified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a new interacting partner of TPPP/p25 within the alpha-synuclein positive Lewy body PMID: 17027006
ERK2 can regulate TPPP activity via the phosphorylation of Thr(14) and/or Ser(18) in its unfolded N-terminal tail PMID: 17693641
Myelin basic protein and p25alpha colocalize in myelin in normal human brains. PMID: 17823288
data suggest that gain of 5p15.33 (TPPP and ZDHHC11) may become a potential biomarker identifying high-risk patients with disease progression in bladder cancer. PMID: 18025801
LIMK1 phosphorylation of p25 blocks p25 activity, thus promoting microtubule disassembly. PMID: 18028908
we review evidence pertaining to the role of GSK3 in the myocardium and discuss effects of genetic manipulation of GSK3 activity in vivo--REVIEW PMID: 18204489
GSK-3 is involved in the regulation of, and cross-talk between, two major forms of synaptic plasticity, N-methyl-D-aspartate receptor dependent long-term potentiation and NMDAR-dependent long-term depression--REVIEW PMID: 18311157
contribution of GSK3 in growth regulation of myeloma cells PMID: 18728964
Data suggest that the intracellular level of TPPP/p25 influences the cell differentiation, proliferation and the formation of protein aggregates, and consequently, the etiology of central nervous system diseases. PMID: 19382230

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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