Recombinant Mouse Prealbumin Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-10036P

Recombinant Mouse Prealbumin Protein (Tagged)

Beta LifeScience SKU/CAT #: BLA-10036P
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Product Overview

Host Species Mouse
Accession P07309
Synonym Amyloid polyneuropathy Amyloidosis I ATTR Carpal tunnel syndrome 1 CTS CTS1 Dysprealbuminemic euthyroidal hyperthyroxinemia Dystransthyretinemic hyperthyroxinemia Epididymis luminal protein 111 HEL111 HsT2651 PALB Prealbumin Prealbumin amyloidosis type I Prealbumin Thyroxine-binding Senile systemic amyloidosis TBPA Thyroxine binding prealbumin Transthyretin TTHY_HUMAN TTR TTR protein
Description Recombinant Mouse Prealbumin Protein (Tagged) was expressed in E.coli. It is a Protein fragment
Source E.coli
AA Sequence AGAGESKCPLMVKVLDAVRGSPAVDVAVKVFKKTSEGSWEPFASGKTAES GELHGLTTDEKFVEGVYRVELDTKSYWKTLGISPFHEFADVVFTANDSGH RHYTIAALLSPYSYSTTAVVSNPQN
Molecular Weight 41 kDa including tags
Purity >90% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target Function Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.
Subcellular Location Secreted.
Protein Families Transthyretin family
Database References
Tissue Specificity Detected in plasma (at protein level). Detected in liver.

Gene Functions References

  1. A C57BL/6 mouse line carrying the transthyretin (TTR) Gly83Arg gene mutation was successfully established. This strain of mice can be used for the study of hereditary vitreous amyloidosis. PMID: 29360446
  2. Results indicate that TTR stability is important for its recently described functions in assisting Abeta transport at the BBB and at the liver and also in regulating LRP1 levels and activity. TTR stabilization can serve as an avenue to increase both Abeta elimination and LRP1 levels, which in turn will further participate in Abeta clearance. PMID: 28570028
  3. This study reports a possible mechanism for Rhabdomyolysis-Induced Acute Kidney Injury and suggests that reductions in TTR could increase the generation of Reactive Oxygen Species and induce apoptosis. PMID: 29040977
  4. TTR neuritogenic activity is mediated by the megalin receptor and is lost in megalin-deficient neurons. PMID: 27518433
  5. New insights into ghrelin cell physiology, and given the known functions of RBP4 and TTR, support an emerging role for the ghrelin cell in blood glucose handling and metabolism. PMID: 23840311
  6. Transthyretin (TTR) deposition in the peripheral nervous system is the hallmark of familial amyloidotic polyneuropathy (FAP). PMID: 27568093
  7. TTR mediated transport of thyroxine represents a survival mechanism necessary for the myogenic program. PMID: 28075349
  8. provide evidence of a new role of Transthyretin as a transcription inducer of insulin-like growth factor receptor I in central nervous system, unveiling a new role in neuroprotection PMID: 25084758
  9. data also indicate that it is unlikely that the behaviors seen in Ttr(-/-) mice are related to its function PMID: 24956283
  10. Native transthyretin inhibits all preeclampsia-like features in the humanized mouse model. PMID: 24035612
  11. Transthyretin silencing (TTRkd) significantly reduced myogenin expression. PMID: 23717457
  12. Amyloid fibrils formed by a mutant form of TTR, A25T, activate microglia, leading to the secretion of tumor necrosis factor-alpha (TNF-alpha), interleukin-6 (IL-6) and nitric oxide. PMID: 24008733
  13. Hsf-1 affects podocyte markers NPHS1, NPHS2 and WT1 in a transgenic mouse model of TTRVal30Met-related amyloidosis. PMID: 23829269
  14. Fibroblasts endocytose and degrade transthyretin aggregates in transthyretin-related amyloidosis. PMID: 23817086
  15. Increased degradation of 14-3-3zeta in lysosomes in the absence of TTR, increasing autophagy. PMID: 23523922
  16. our data demonstrate that the increased expression of Ttr in ob/ob mice does not cause (but rather attenuates) their phenotypic abnormalities. PMID: 22849972
  17. TTR has an important and nonredundant role in influencing the development of several organs. PMID: 23092911
  18. Results suggest that TTR expressed in pancreatic alpha cells may play important roles in glucose homeostasis via regulating the expression of glucagon. PMID: 23108050
  19. TTR binds to Grp78 at the plasma membrane, is internalized into the beta-cell via a clathrin-dependent pathway, and that this internalization is necessary for the effects of TTR on beta-cell function. PMID: 22183612
  20. the expression of transthyretin and protein kinase Cgamma were increased in the prefrontal cortex but not in the hippocampus of naltrexone-treated mice PMID: 21111029
  21. Cerebrospinal fluid transthyretin contributes to control of neuronal cell death, edema and inflammation which influences the survival of endangered neurons in cerebral ischemia. PMID: 21044072
  22. Results identify transthyretin and Klotho as physiological targets of amyloid precursor protein that are regulated by soluble APPsbeta independent of developmental APP functions. PMID: 20855613
  23. TTR mRNA is dramatically up-regulated in the preimplantation mouse uterus as well as the progesterone-treated ovariectomized mouse uterus. PMID: 20188365
  24. Using transthyretin (TTR) KO mice as a model of augmented NPY levels, we showed that this strain has increased NPY content in the bone, further validating the expression of this neuropeptide by bone cells. PMID: 19954489
  25. Transthyretin is not required for thyroid hormone access to or distribution within the mouse brain. PMID: 12182890
  26. Levels of noradrenaline were significantly increased in the limbic forebrain of TTR-null mice. This report represents the first clear indication that TTR plays a role in behaviour, probably by modulation of the noradrenergic system PMID: 15009661
  27. Mice overexpressing mutant APP have high levels of sAPPalpha & transthyretin & do not develop the tau phosphorylation or neuronal loss characteristic of human AD. Anti-transthyretin antibodies reverse this, showing that transthyretin is neuroprotective. PMID: 15342738
  28. Transthyretin is clearly not produced in the brain parenchyma of wild-type mice nor in transgenic mouse models of Alzheimer's disease. PMID: 16698124
  29. The effect of chronic ethanol treatment on transthyretin expression was analyzed because gamma-PKC mutants do not develop tolerance to chronic ethanol treatment. PMID: 16767509
  30. proliferation and apoptosis in the SVZ neural stem cell niche are differentially affected by the lack of TTR synthesis. PMID: 17574756
  31. Our results strongly suggest that TTR plays a critical role in modulating Abeta deposition in vivo. PMID: 17596449
  32. the absence of transthyretin does not seem to influence the regulation of lipid and glucose metabolism PMID: 17611908
  33. data show that the absence of TTR seems to accelerate the poorer cognitive performance normally associated with aging PMID: 17698379
  34. TTR participates in nerve physiology and enhances nerve regeneration PMID: 17897357
  35. Lowering TTR levels or interfering with retinol binding protein 4-TTR binding may enhance insulin sensitivity in obesity and type 2 diabetes PMID: 18285525
  36. TCDD can induce memory deficits by altering the estrogen pathways and a main route of TTR-mediated retinol transport. PMID: 18294692
  37. In mouse DRG, TTR mRNA was localized in the peripheral glial cells. PMID: 18406527
  38. Data show that the degree of total and vascular Abeta burdens in the aged Tg2576/TTR(-/-) mice is significantly reduced relative to the age-matched Tg2576/TTR(+/-) mice. PMID: 18429966
  39. TTR deposited in peripheral nervous system of familial amyloiditic polyneuropathy should be regarded as having blood or CSF origin PMID: 18835560
  40. Results suggest that transthyretin is up-regulated by estradiol via a pathway involving estrogen receptors alpha and beta. PMID: 19130215
  41. TTR has natural substrates in the nervous system PMID: 19138167
  42. Transthyretin, a gene previously suggested to play a role in the reduction of Alzheimer disease, has been identified as a leftward gene asymmetrically expressed in the brains of adult male mice. PMID: 19167467
  43. Axonal retrograde transport is impaired in transthyretin knock-out mice, in addition to neurite outgrowth impairment. PMID: 19279259
  44. Using both GFP-based and LacZ-based Cre reporter strains, we demonstrate that in Ttr::Cre transgenics, Cre-mediated recombination occurs throughout the visceral endoderm PMID: 19415627
  45. he alleged neuroprotective role of TTR in the nervous system should be regarded with caution and should not be generalized to all types of insults PMID: 19595729
  46. rat and murine TTR have a lower intrinsic beta-aggregation propensity and a similar native beta-structure stability compared with human TTR. PMID: 19602727

FAQs

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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.

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