Recombinant Human Tubulin polymerization-promoting protein (TPPP)
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中文名稱：人TPPP重組蛋白
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貨號：CSB-EP024115HU-B
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說明書：
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規格：
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來源：E.coli
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共軛：Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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其他：
產品詳情
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純度：>85% (SDS-PAGE)
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基因名：TPPP
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Uniprot No.：
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別名：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
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種屬：Homo sapiens (Human)
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蛋白長度：Full length protein
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表達區域：1-219
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氨基酸序列MADKAKPAKA ANRTPPKSPG DPSKDRAAKR LSLESEGAGE GAAASPELSA LEEAFRRFAV HGDARATGRE MHGKNWSKLC KDCQVIDGRN VTVTDVDIVF SKIKGKSCRT ITFEQFQEAL EELAKKRFKD KSSEEAVREV HRLIEGKAPI ISGVTKAISS PTVSRLTDTT KFTGSHKERF DPSGKGKGKA GRVDLVDESG YVSGYKHAGT YDQKVQGGK
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蛋白標簽：Tag?type?will?be?determined?during?the?manufacturing?process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially. -
產品提供形式：Lyophilized powder Warning: in_array() expects parameter 2 to be array, null given in /www/web/cusabio_cn/public_html/caches/caches_template/default/content/show_product_protein.php on line 662
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand. -
復溶：We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
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儲存條件：Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
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保質期：The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C. -
貨期：Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
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注意事項：Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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Datasheet ：Please contact us to get it.
產品評價
相關產品
靶點詳情
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功能：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.
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基因功能參考文獻：
- 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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亞細胞定位：Golgi outpost. Cytoplasm, cytoskeleton, microtubule organizing center. Cytoplasm, cytoskeleton. Nucleus. Cytoplasm, cytoskeleton, spindle.
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蛋白家族：TPPP family
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組織特異性：Widely expressed.
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