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 >  Protein>Transferrin >TRN-H5216

Human Transferrin Protein, premium grade

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)

Transferrin Structure

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:

  1. -20°C to -70°C for 24 months in lyophilized state;
  2. -70°C for 3 months under sterile conditions after reconstitution.

质量管理控制体系(QMS)

  1. 质量管理体系(ISO, GMP)
  2. 质量优势
  3. 质控流程
 

电泳(SDS-PAGE)

Transferrin 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

Transferrin 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

Transferrin 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

Transferrin ELISA

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

Transferrin ELISA

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

Transferrin ELISA

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

 
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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.

 

前沿进展

The long noncoding RNA APR attenuates PPRV infection-induced accumulation of intracellular iron to inhibit membrane lipid peroxidation and viral replication
Wen, Chang, Yang et al
mBio (2025)
Abstract: Peste des petits ruminants virus (PPRV) is an important pathogen that has long been a significant threat to small ruminant productivity worldwide. Iron metabolism is vital to the host and the pathogen. However, the mechanism underlying host-PPRV interactions from the perspective of iron metabolism and iron-mediated membrane lipid peroxidation has not been reported thus far. In this study, we identified a novel host long-noncoding RNA (lncRNA), APR, that impairs PPRV infectivity by sponging miR-3955-5p, a negative microRNA (miRNA) that directly targets the gene encoding the ferritin-heavy chain 1 (FTH1) protein. Importantly, we demonstrated that PPRV infection causes aberrant cellular iron accumulation by increasing transferrin receptor (TFRC) expression and that iron accumulation induces reticulophagy and ferroptosis, which benefits PPRV replication. Moreover, PPRV infection enhanced the localization of cellular iron on the endoplasmic reticulum (ER) and caused ER membrane damage by promoting excess lipid peroxidation to induce reticulophagy. Interestingly, APR decreased PPRV infection-induced accumulation of intracellular Fe2+ via miR-3955-5p/FTH1 axis and ultimately inhibited reticulophagy and ferroptosis. Additionally, our results indicate that interferon regulatory factor 1 promotes APR transcription by positively regulating APR promoter activity after PPRV infection. Taken together, our findings revealed a new pattern of PPRV-host interactions, involving noncoding RNA regulation, iron metabolism, and iron-related membrane lipid peroxidation, which is critical for understanding the host defense against PPRV infection and the pathogenesis of PPRV.IMPORTANCEMany viruses have been demonstrated to engage in iron metabolism to facilitate their replication and pathogenesis. However, the mechanism by which PPRV interacts with host cells from the perspective of iron metabolism, or iron-mediated membrane lipid peroxidation, has not yet been reported. Our data provide the first direct evidence that PPRV infection induces aberrant iron accumulation to promote viral replication and reveal a novel host lncRNA, APR, as a regulator of iron accumulation by promoting FTH1 protein expression. In this study, PPRV infection increased cellular iron accumulation by increasing TFRC expression, and more importantly, iron overload increased viral infectivity as well as promoted ER membrane lipid peroxidation by enhancing the localization of cellular iron on the ER and ultimately induced ferroptosis and reticulophagy. Furthermore, a host factor, the lncRNA APR, was found to decrease cellular iron accumulation by sponging miR-3955-5p, which directly targets the gene encoding the FTH1 protein, thereby attenuating PPRV infection-induced ferroptosis and reticulophagy and inhibiting PPRV infection. Taken together, the results of the present study provide new insight into our understanding of host-PPRV interaction and pathogenesis from the perspective of iron metabolism and reveal potential targets for therapeutics against PPRV infection.
Evaluation of serum levels of calprotectin, lactoferrin and zinc in patients with type II diabetes mellitus
Hassan, Shamran, Albadry et al
Wiad Lek (2025) 78 (2), 288-294
Abstract: Aim: The current study aimed to evaluate the role of serum calprotectin, lactoferrin and serum zinc in patients with type II diabetes mellitus.Materials and Methods: Sixty subjects have been investigated in this study, (40) patients with T2DM and 20 apparently healthy participants (control group) during the period between October 2021 to January 2022. Zinc was measured using a calorimetric method, while calprotectin and lactoferrin were measured by ELISA.Results: The findings also revealed that levels of serum calprotectin and lactoferrin have significantly increased in in patients with T2DM as compared to healthy subjects. The result also showed that serum zin is decreased in patients groups. The correlation matrix exhibited that there was a strong positive correlation between calprotectin and lactoferrin, a significant negative correlation between zinc and calprotectin.Conclusions: It was concluded that high serum calprotectin and lactoferrin indicated a strong inflammatory status in T2DM patients. Zinc is likely to be negative affected by the high inflammatory response indicated by that high serum calprotectin.
Altered chaperone-nonmuscle myosin II interactions drive pathogenicity of the UNC45A c.710T>C variant in osteo-oto-hepato-enteric syndrome
Waich, Kreidl, Vodopiutz et al
JCI Insight (2025) 10 (6)
Abstract: The osteo-oto-hepato-enteric (O2HE) syndrome is a severe autosomal recessive disease ascribed to loss-of-function mutations in the Unc-45 myosin chaperone A (UNC45A) gene. The clinical spectrum includes bone fragility, hearing loss, cholestasis, and life-threatening diarrhea associated with microvillus inclusion disease-like enteropathy. Here, we present molecular and functional analysis of the UNC45A c.710T>C (p.Leu237Pro) missense variant, which revealed a unique pathogenicity compared with other genetic variants causing UNC45A deficiency. The UNC45A p.Leu237Pro mutant retained chaperone activity, prevented myosin aggregation, and supported proper nonmuscle myosin II (NMII) filament formation in patient fibroblasts and human osteosarcoma (U2OS) cells. However, the mutant formed atypically stable oligomers and prevented chaperone-myosin complex dissociation, thereby inhibiting NMII functions. Similar to biallelic UNC45A deficiency, this resulted in impaired intracellular trafficking, defective recycling, and abnormal retention of transferrin at various endocytic sites. In particular, coexpression of wild-type protein attenuated the pathogenic effects of the variant by inhibiting excessive oligomer formation. Our results elucidate the pathogenic mechanisms and recessive characteristics of this variant and may aid in the development of targeted therapies.
Wolf in Sheep's Clothing: Taming Cancer's Resistance with Human Serum Albumin?
Stukan, Żuk, Pukacka et al
Int J Nanomedicine (2025) 20, 3493-3525
Abstract: Human serum albumin (HSA) has emerged as a promising carrier for nanodrug delivery, offering unique structural properties that can be engineered to overcome key challenges in cancer treatment, especially resistance to chemotherapy. This review focuses on the cellular uptake of albumin-based nanoparticles and the modifications that enhance their ability to bypass resistance mechanisms, particularly multidrug resistance type 1 (MDR1), by improving targeting to cancer cells. In our unique approach, we integrate the chemical properties of albumin, its interactions with cancer cells, and surface modifications of albumin-based delivery systems that enable to bypass resistance mechanisms, particularly those related to MDR1, and precisely target receptors on cancer cells to improve treatment efficacy. We discuss that while well-established albumin receptors such as gp60 and gp18/30 are crucial for cellular uptake and transcytosis, their biology remains underexplored, limiting their translational potential. Additionally, we explore the potential of emerging targets, such as cluster of differentiation 44 (CD44), cluster of differentiation (CD36) and transferrin receptor TfR1, as well as the advantages of using dimeric forms of albumin (dHSA) to further enhance delivery to resistant cancer cells. Drawing from clinical examples, including the success of albumin-bound paclitaxel (Abraxane) and new formulations like Pazenir and Fyarro (for Sirolimus), we identify gaps in current knowledge and propose strategies to optimize albumin-based systems. In conclusion, albumin-based nanoparticles, when tailored with appropriate modifications, have the potential to bypass multidrug resistance and improve the targeting of cancer cells. By enhancing albumin's ability to efficiently deliver therapeutic agents, these carriers represent a promising approach to addressing one of oncology's most persistent challenges, with substantial potential to improve cancer treatment outcomes.© 2025 Stukan et al.
Showing 1-4 of 47227 papers.
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Transferrin靶点信息
英文全称:Transferrin receptor protein 1
中文全称:转铁蛋白受体1
种类:Homo sapiens
上市药物数量:1详情
临床药物数量:12详情
最高研发阶段:批准上市
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