Recombinant Rat Transferrin Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-4627

Recombinant Rat Transferrin Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-4627
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Product Overview

Tag His
Host Species Rat
Accession NP_001013128.1
Background Transferrin is a glycoprotein with an approximate molecular weight of 76.5 kDa. This glycoprotein is thought to have been created as a result of an ancient gene duplication event that led to generation of homologous C and N-terminal domains each of which binds one ion of ferric iron. The function of Transferrin is to transport iron from the intestine, reticuloendothelial system, and liver parenchymal cells to all proliferating cells in the body. This protein may also have a physiologic role as granulocyte / pollen-binding protein (GPBP) involved in the removal of certain organic matter and allergens from serum. Transferrins are iron binding transport proteins which bind Fe3+ ion in association with the binding of an anion, usually bicarbonate. This transferrin binds only one Fe3+ ion per protein molecule. Transports iron ions from the hemolymph into the eggs during the vitellogenic stage. Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation. When a transferrin loaded with iron encounters with a transferring receptor on cell surface, transferring binds to it and, as a consequence, is transported into the cell in a visicle by receptor-mediated endocytosis. The PH is reduced by hydrogen iron pumps. The lower pH causes transferrin to release its iron ions. The receptor is then transported through the endocytic cycle back to the cell surface, ready for another round of iron uptake. Each transferrin molecule has the ability to carry two iron ions in the ferric form.
Description A DNA sequence encoding the rat TF (NP_001013128.1) (Met1-Ser698) was expressed with a His tag at the C-terminus.
Source HEK293
Predicted N Terminal Val 20
AA Sequence Met1-Ser698
Molecular Weight The recombinant rat TF comprises 690 a.a. and predicts a molecular mass of 76 kDa. The apparent molecular mass of the recombinant protein is approximately 89 kDa in SDS-PAGE under reducing conditions.
Purity >95% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured in a serum-free cell proliferation assay using MCF-7 human breast cancer cells. The ED50 for this effect is typically 0.02-1 ug/mL.
Formulation Lyophilized from sterile PBS, pH 7.2..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
Subcellular Location Secreted.
Protein Families Transferrin family
Database References
Tissue Specificity Expressed by the liver and secreted in plasma.

Gene Functions References

  1. our data establish that blood TSAT exerts a critical role in experimental stroke-induced brain damage. In addition, our findings suggest that the protective effect of iron-free transferrin (apotransferrin, ATf) at the neuronal level resides in preventing NMDA-induced HTf uptake and ROS production, which in turn reduces neuronal damage PMID: 29248829
  2. In brain interstitial fluid, transferrin-bound iron and non-transferrin-bound iron (NTBI) exist as potential iron sources PMID: 25649872
  3. Transferrin and thyroid hormone converge to regulate oligodendrocyte maturation and myelinogenesis. PMID: 25595122
  4. This evidence supports a key role of Tf on the generation of oligodendrocytes (OLs) from Neural stem and progenitor cells (NSC/NPCs)and highlights its potential in demyelinating disorder treatment. PMID: 22479482
  5. Transferrin is involved in the uptake of the radiopharmaceutical gallium-67 (67Ga) by regenerating liver tissue following partial hepatectomy but is not involved in the entry of 67Ga into hepatocytes. PMID: 11767098
  6. data show that brain cells have the capacity to maintain minimum iron levels during iron deficiency which may be associated with increased iron-Tf uptake, stabilization of TfR mRNA, or increased Tf mRNA translation efficiency in specific cell types PMID: 12608731
  7. effects of apotransferrin occur early in development during a narrow, transient "temporal window" within which oligodendroglia are sensitive to its action. PMID: 12730961
  8. first report describing presence of serotransferrin precursor protein homolog belonging to transferrin family and sharing epitopes with melanotransferrin in adrenal, its induction by ACTH, and sensitivity to ginkgolide B (adrenotransferrin). PMID: 14701678
  9. compared to transferrin, soluble melanotransferrin plays little or no role in Fe supply to the brain and erythropoietic tissue PMID: 15469901
  10. in addition to hemoglobin-bound iron, Tf-bound iron may contribute to intracerebral hemorrhage-induced brain injury and thrombin may contribute to the latter by facilitating cellular iron uptake PMID: 15637325
  11. Our studies suggest that AEC I is not just a simple barrier for gas exchange, but a functional cell that protects alveolar epithelium from injury. PMID: 16497717
  12. Plays role in maturation of Schwann cells(SC) in physiological conditions as well as in role in facilitating clearance of myelin debris and subsequent nerve regeneration and/or in SC phenotypic change, which led to survival after peripheral nerve injury. PMID: 17628542
  13. Apotransferrin added to oligodendroglial cell cultures can correct the effects of iron deficiency. PMID: 18459135
  14. serotransferrin levels were increased in diestrous as compared with proestrous, estrous, metestrous PMID: 18511206
  15. we have discovered a novel mitochondrial iron transport system that goes awry in Parkinson's disease, and which may provide a new target for therapeutic intervention. PMID: 19250966
  16. synthesis and secretion of transferrin in rat parotid acinar cells PMID: 19464997

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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