Alpha-tocopherol transfer protein; Alpha-TTP; AlphaTTP; ATTP; AVED; Tocopherol (alpha) transfer protein (ataxia (Friedreich-like) with vitamin E deficiency); TTP1; TTPA; TTPA_HUMAN
種屬:
Homo sapiens (Human)
蛋白長度:
Full Length
來源:
E.coli
分子量:
47.7kDa
表達(dá)區(qū)域:
1-278aa
氨基酸序列
MAEARSQPSAGPQLNALPDHSPLLQPGLAALRRRAREAGVPLAPLPLTDSFLLRFLRARDFDLDLAWRLLKNYYKWRAECPEISADLHPRSIIGLLKAGYHGVLRSRDPTGSKVLIYRIAHWDPKVFTAYDVFRVSLITSELIVQEVETQRNGIKAIFDLEGWQFSHAFQITPSVAKKIAAVLTDSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKERIHMHGNNYKQSLLQHFPDILPLEYGGEEFSMEDICQEWTNFIMKSEDYLSSISESIQ Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
蛋白標(biāo)簽:
N-terminal 6xHis-SUMO-tagged
產(chǎn)品提供形式:
Liquid or Lyophilized powder 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.
緩沖液:
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Note: If you have any special requirement for the glycerol content, please remark when you place the order. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
儲(chǔ)存條件:
Store at -20°C/-80°C upon receipt, aliquoting is necessary for
mutiple use. Avoid repeated freeze-thaw cycles.
保質(zhì)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:
3-7 business days
注意事項(xiàng):
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Binds alpha-tocopherol, enhances its transfer between separate membranes, and stimulates its release from liver cells. Binds both phosphatidylinositol 3,4-bisphosphate and phosphatidylinositol 4,5-bisphosphate; the resulting conformation change is important for the release of the bound alpha-tocopherol.
基因功能參考文獻(xiàn):
alphaTTP does not appear to regulate the uptake and intracellular localization of different vitamin E congeners in cultured liver cells. PMID: 30098456
These findings provide the basis for a proposed mechanistic model that describes TTP-facilitated trafficking of alpha-tocopherol through hepatocytes. PMID: 27307040
Current results show that alphaTTP plays a role in endometrial carcinoma. Possibly endometrial cancer cells attempt to protect themselves from increasing oxidative stress by up-regulating alphaTTP. PMID: 28213729
Single-nucleotide polymorphisms that are commonly found in healthy humans dramatically affect promoter activity of the TTPA gene. PMID: 23079030
The crystal structure of the alpha-TTP-phosphatidylinositol phosphates (PIPs) complex revealed that the familial vitamin E deficiency-related arginine residues interacted with phosphate groups of the PIPs and that the PIPs binding caused the lid of the alpha-tocopherol-binding pocket to open. PMID: 23599266
study demonstrated that alpha -TTP can be upregulated in case of oxidative stress in BeWo trophoblast cells; speculate that possibly, alpha -TTP is notonly involved in normal pregnancy, but also in cases of pregnancy disorders with intense oxidative stress PMID: 22752767
Data show that reduction ("knockdown") of tocopherol transfer protein (TTP) expression resulted in resistance to the vitamin E. PMID: 20826775
Substitution of residues in helices A8 (F165A and F169A) and A10 (I202A, V206A and M209A) decreased the rate of intermembrane ligand transfer as well as protein adsorption to phospholipid bilayers. PMID: 21110980
First case of a mutated form of the TTPA gene in a patient also carrying a spinocerebellar ataxia type 8 expansion. PMID: 12470185
crystal structure reveals two conformations PMID: 12899840
the positively charged surface of TTPA may serve to orient an interacting protein, which might function to regulate the release of alpha-T through an induced change in conformation of ATTP PMID: 14657365
Findings suggest the possibility that ataxia with vitamin E deficiency syndrome (AVED) may not arise from an inability of TTP to bind or to transfer alpha tocopherol, but rather from defects in other activities of the protein. PMID: 15065857
Nuclear localization of TTPA in in trophoblast, fetal capillaries' endothelium and amnion epithelium of human term placentamay represent a novel function of TTPA PMID: 15190938
In Ataxia with vitamin E deficiency two TTPA mutations were identified: a truncating mutation in a homozygous patient, and a Gly246Arg missense mutation in a compound heterozygous patient associated with a mild and slowly progressive form of the disease. PMID: 15300460
The physiological role of TTP is anchored in its ability to direct vitamin E trafficking from the endocytic compartment to transport vesicles that deliver the vitamin to the site of secretion at the plasma membrane. PMID: 16819822
analysis of ligand transfer by the hepatic tocopherol transfer protein PMID: 18458085
in first-trimester extravillous trophoblast, syncytiotrophoblast and amniotic epithelium PMID: 18511174
The vitamin E deficiency with hereditary motor neuropathy was found to be homozygous for a 513insTT mutation in exon 3 of the alpha-tocopherol transfer protein gene. PMID: 18984846
Total deletion of the TTPA gene is expected to be associated with severe phenotype in AVED patients. PMID: 19102053
Genetic variation in TTPA and SEC14L2 is associated with serum alpha-tocopherol but does not have a direct effect on prostate cancer when vitamin E is administered. PMID: 19190344
Hydrophobic features of alpha-TTP dominating the binding energy between protein and membrane. PMID: 19458973