Mouse Transferrin (TF) Protein

Product specifications

Proteins and Peptides

Transferrin (TRF)

E. coli

Mouse

Unconjugated

Molecular Weight: Calculated MW: 41.1 kDa
Concentration: Prior to lyophilization: 200 µg/ml
Sequence Fragment: Val360-Lys682
Tag: N-terminal His tag

Recombinant

> 95%

1 mg

5 mg

Lyophilized To keep the original salt concentration, we recommend reconstituting to the original concentration prior to lyophilization (see Concentration) in ddH2O. If a lower concentration is required, dilute in PBS, pH 7.4. If a higher concentration is required, the product can be reconstituted directly in PBS, pH 7.4, though please note that this will change the overall salt concentration. The stock concentration should be between 0.1-1.0 mg/ml. Do not vortex.

WB, SDS-PAGE

Prior to lyophilization: PBS, pH 7.4, containing 0.01% Sarcosyl, 1 mM DTT, 5% Trehalose and Proclin-300.

Shipped within 1-2 months.

Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles.

No

Q921I1

PRO1557,PRO2086,TFQTL1,HEL-S-71p

Protein TF

RUO

This product is for research use only.   Not for human consumption, cosmetic, therapeutic or diagnostic use.

Descripción

Transferrin (TF) is a glycoprotein that plays a central role in iron homeostasis by binding and transporting iron ions in the blood to various tissues, including the liver, bone marrow, and brain. It interacts with transferrin receptors (TFR1 and TFR2) on cell surfaces to mediate iron uptake through receptor-mediated endocytosis, ensuring iron availability for critical cellular processes such as hemoglobin synthesis, DNA replication, and energy metabolism. TF is produced primarily in the liver and is widely distributed in blood plasma. Dysregulation of transferrin leads to iron-related disorders, such as anemia, iron overload (hemochromatosis), and neurodegenerative diseases like Alzheimer’s, where altered iron metabolism contributes to oxidative stress and neuronal damage. Elevated transferrin levels are also associated with liver disease and systemic inflammation. Knockout studies demonstrate impaired iron transport, reduced erythropoiesis, and disrupted metabolic processes, emphasizing its essential role in systemic iron regulation, cellular function, and red blood cell production.

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TF antibody

Serotransferrin(TF) is a 77 kDa secreted protein which is also named as transferrin, siderophilin, beta-1 metal-binding globulin and belongs to a family of homologous iron-binding glycoproteins that encompasses lactoferrin(found both intracellular and in secretions, including milk), melanotrasferrin(present on melanoma cells) and ovotransferrin(present in egg white). TF is a multi-function protein with a primary role in transporting iron in a safe, redox-inactive state from absorption to utilization or storage sites around the body. The association of Tf with the immune system derives from its ability to restrict serum free-iron levels, creating low-iron environments where the infection capacity of pathogenic microorganisms is limited. TF is expressed predominantly in the liver and secreted in plasma, but lower amounts can be synthesized in other tissues such as the brain and the testis

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