Anti-Transferrin/TF Antibody Picoband® (monoclonal, 7I11B10)

Transferrins are iron-binding blood plasma glycoproteins that control the level of free iron in biological fluids. In humans, it is encoded by the TF gene. Transferrin consists of a polypeptide chain containing 679 amino acids in humans. The protein is composed of alpha helices and beta sheets to form two domains. The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site. Transferrin is a glycoprotein that binds iron very tightly but reversibly. 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) . And Transferrin has a molecular weight of around 80 kDa and contains 2 specific high-affinity Fe (III) binding sites. The affinity of transferrin for Fe (III) is extremely high (1023 M1 at pH 7.4) but decreases progressively with decreasing pH below neutrality.

A synthetic peptide corresponding to a sequence at the N-terminus of human Transferrin, different from the related mouse and rat sequences by five amino acids.

Cadherins, Calcium Binding Proteins, Calcium Signaling, Cancer, Cell Adhesion, Cytoskeleton/ECM, Invasion/Microenvironment, Signal Transduction, Signaling Pathway

Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V (D) J recombination, DNA repair and genome stability. Proposed to be an universal biosensor for nucleic acids. Promotes host inflammatory response to sterile and infectious signals and is involved in the coordination and integration of innate and adaptive immune responses. In the cytoplasm functions as sensor and/or chaperone for immunogenic nucleic acids implicating the activation of TLR9-mediated immune responses, and mediates autophagy. Acts as danger associated molecular pattern (DAMP) molecule that amplifies immune responses during tissue injury. Released to the extracellular environment can bind DNA, nucleosomes, IL-1 beta, CXCL12, AGER isoform 2/sRAGE, lipopolysaccharide (LPS) and lipoteichoic acid (LTA), and activates cells through engagement of multiple surface receptors. In the extracellular compartment fully reduced HMGB1 (released by necrosis) acts as a chemokine, disulfide HMGB1 (actively secreted) as a cytokine, and sulfonyl HMGB1 (released from apoptotic cells) promotes immunological tolerance. Has proangiogdenic activity. May be involved in platelet activation. Binds to phosphatidylserine and phosphatidylethanolamide. Bound to RAGE mediates signaling for neuronal outgrowth. May play a role in accumulation of expanded polyglutamine (polyQ) proteins such as huntingtin (HTT) or TBP.

1. Asada-Senju, M., Maeda, T., Sakata, T., Hayashi, A., Suzuki, T.Molecular analysis of the transferrin gene in a patient with hereditary hypotransferrinemia.J. Hum. Genet. 47: 355-359, 2002. 2. Delanghe, J., Verstraelen, H., Pynaert, I., Debels, L., Taes, Y., Verhasselt, B., De Henauw, S., Temmerman, M.Human transferrin G277S mutation and iron deficiency in pregnancy. (Letter) Brit. J. Haemat. 132: 249-250, 2005. 3. Pang, H., Koda, Y., Soejima, M., Kimura, H.Identification of a mutation (A1879G) of transferrin from cDNA prepared from peripheral blood cells.Ann. Hum. Genet. 62: 271-274, 1998.

At -20°C for one year from date of receipt. After reconstitution, at 4°C for one month. It can also be aliquotted and stored frozen at -20°C for six months. Avoid repeated freezing and thawing.

Nucleus. Endosome. Secreted. Cell membrane. Peripheral membrane protein. Extracellular side. Chromosome. Cytoplasm. Endoplasmic reticulum-Golgi intermediate compartment.