Recombinant Human Alpha-Tocopherol Transfer Protein (TTPA) Protein (His-SUMO)

Name: Recombinant Human Alpha-Tocopherol Transfer Protein (TTPA) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03987P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Alpha-Tocopherol Transfer Protein (TTPA) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P49638
Target Symbol	TTPA
Synonyms	Alpha-tocopherol transfer protein; Alpha-TTP; AlphaTTP; ATTP; AVED; Tocopherol (alpha) transfer protein (ataxia (Friedreich-like) with vitamin E deficiency); TTP1; TTPA; TTPA_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MAEARSQPSAGPQLNALPDHSPLLQPGLAALRRRAREAGVPLAPLPLTDSFLLRFLRARDFDLDLAWRLLKNYYKWRAECPEISADLHPRSIIGLLKAGYHGVLRSRDPTGSKVLIYRIAHWDPKVFTAYDVFRVSLITSELIVQEVETQRNGIKAIFDLEGWQFSHAFQITPSVAKKIAAVLTDSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKERIHMHGNNYKQSLLQHFPDILPLEYGGEEFSMEDICQEWTNFIMKSEDYLSSISESIQ
Expression Range	1-278aa
Protein Length	Full Length
Mol. Weight	47.7kDa
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	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.
Subcellular Location	Cytoplasm.
Database References	HGNC: 12404 OMIM: 277460 KEGG: hsa:7274 STRING: 9606.ENSP00000260116 UniGene: 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

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.