膜杰作
Star Staining
分子别名（Synonym）
Transferrin,TF,DKFZp781D0156,PRO1557,PRO2086
表达区间及表达系统（Source）
Human Transferrin Protein, premium grade (TRN-H5216) is expressed from human 293 cells (HEK293). It contains AA Val 20 - Pro 698 (Accession # AAH59367).
Predicted N-terminus: Val 20
It is produced under our rigorous quality control system that incorporates a comprehensive set of tests including sterility and endotoxin tests. Product performance is carefully validated and tested for compatibility for cell culture use or any other applications in the early preclinical stage. When ready to transition into later clinical phases, we also offer a custom GMP protein service that tailors to your needs. We will work with you to customize and develop a GMP-grade product in accordance with your requests that also meets the requirements for raw and ancillary materials use in cell manufacturing of cell-based therapies.
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蛋白结构（Molecular Characterization）
This protein carries no "tag".
The protein has a calculated MW of 75.2 kDa. The protein migrates as 71 kDa±3 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under non-reducing (NR) condition (SDS-PAGE).
内毒素（Endotoxin）
Less than 0.01 EU per μg by the LAL method.
无菌（Sterility）
Negative
支原体（Mycoplasma）
Negative.
纯度（Purity）
>95% as determined by SDS-PAGE.
>98% as determined by SEC-MALS.
制剂（Formulation）
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4 with trehalose as protectant.
Contact us for customized product form or formulation.
重构方法（Reconstitution）
Please see Certificate of Analysis for specific instructions.
For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
存储（Storage）
For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
- -20°C to -70°C for 24 months in lyophilized state;
- -70°C for 3 months under sterile conditions after reconstitution.
电泳（SDS-PAGE）
Human Transferrin Protein, premium grade on SDS-PAGE under non-reducing (NR) condition. The gel was stained with Coomassie Blue. The purity of the protein is greater than 95% (With Star Ribbon Pre-stained Protein Marker).
SEC-MALS
The purity of Human Transferrin Protein, premium grade (Cat. No. TRN-H5216) is more than 98% and the molecular weight of this protein is around 75-95 kDa verified by SEC-MALS.
Report
活性（Bioactivity）-ELISA
Immobilized Human Transferrin Protein, premium grade (Cat. No. TRN-H5216) at 2 μg/mL (100 μL/well) can bind Biotinylated Human Transferrin R, Avitag,His Tag (Cat. No. TFR-H82E5) with a linear range of 1-16 ng/mL (QC tested).
Protocol
Immobilized Human Transferrin Protein, premium grade (Cat. No. TRN-H5216) at 2 μg/mL (100 μL/well) can bind Biotinylated Human Transferrin R, His Tag, primary amine labeling (Cat. No. TFR-H8243) with a linear range of 4-63 ng/mL (Routinely tested).
Protocol
Immobilized Human Transferrin Protein, premium grade (Cat. No. TRN-H5216) at 2 μg/mL (100 μL/well) can bind Human Transferrin R, His Tag (Cat. No. CD1-H5243) with a linear range of 0.039-0.313 μg/mL (Routinely tested).
Protocol
Immobilized Human Transferrin Protein, premium grade (Cat. No. TRN-H5216) at 2 μg/mL (100 μL/well) can bind Biotinylated Human Transferrin R Protein, Fc,Avitag (Cat. No. TFR-H82F3) with a linear range of 10-78 ng/mL (Routinely tested).
Protocol
背景（Background）
Transferrin is also known as Serotransferrin, Beta-1 metal-binding globulin, TF, and is iron-binding blood plasma glycoproteins that control the level of free iron in biological fluids. Although iron bound to transferrin is less than 0.1% (4 mg) of the total body iron, it is the most important iron pool, with the highest rate of turnover (25 mg/24 h). The affinity of transferrin for Fe(III) is extremely high (1023 M−1 at pH 7.4) but decreases progressively with decreasing pH below neutrality.When not bound to iron, it is known as "apo-transferrin”. In humans, transferrin consists of a polypeptide chain containing 679 amino acids. It is a complex composed of alpha helices and beta sheets to form two domains (the first situated in the N-terminus and the second in the C-terminus). The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site. The liver is the main source of manufacturing transferrin, but other sources such as the brain also produce this molecule . Transferrin is also associated with the innate immune system. Transferrin is found in the mucosa and binds iron, thus creating an environment low in free iron that impedes bacteria survival in a process called iron withholding. The level of transferrin decreases in inflammation. The metal binding properties of transferrin have a great influence on the biochemistry of plutonium in humans. Transferrin has a bacteriocidal effect on bacteria, in that it makes Fe3+ unavailable to the bacteria.Carbohydrate deficient transferrin increases in the blood with heavy ethanol consumption and can be monitored via laboratory testing.
