T0523
apo-Transferrin from mouse
≥98%
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About This Item
Productos recomendados
biological source
mouse
Quality Level
assay
≥98%
form
powder
technique(s)
protein quantification: suitable
solubility
H2O: 20 mg/mL
UniProt accession no.
storage temp.
2-8°C
Gene Information
mouse ... Trf(22041)
General description
Transferrin is a 79 kDa protein and possesses two lobes, an N-terminal and a C-terminal lobe, interconnected by a short spacer. The domains interact to form metal ion-binding site.
Application
Apo-Transferrin from mouse has been used in serum protein quantification using surface plasmon resonance (SPR) microarray and serum protein cross-reactivity analysis. It has also been used in the analytical approaches for glycosylation studies like intact glycoprotein analysis, glycopeptide analysis and glycan analysis.
Biochem/physiol Actions
Apo-Transferrin from mouse is a serum protein involved in the transfer of iron to the cells. Apotransferrin can bind two Fe3+ ions. In the iron bound state, it is referred to as transferrin. It binds to transferrin receptors in the extracellular surface of cell membrane, internalizes and releases iron in the cytoplasm. Apotransferrin is cycled back to the serum for iron transport.
Storage Class
11 - Combustible Solids
wgk_germany
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Certificados de análisis (COA)
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Los clientes también vieron
Cells: Molecules and Mechanisms (2009)
Quantitative serum proteomics from surface plasmon resonance imaging
Molecular and Cellular Proteomics, 7(12), 2464-2474 (2008)
Analytical biochemistry, 394(1), 92-100 (2009-07-15)
Organophosphate (OP) esters bind covalently to the active site serine of enzymes in the serine hydrolase family. Recently, mass spectrometry identified covalent binding of OPs to tyrosine in a wide variety of proteins when purified proteins were incubated with OPs.
Evaluation of ion mobility for the separation of glycoconjugate isomers due to different types of sialic acid linkage, at the intact glycoprotein, glycopeptide and glycan level
Journal of proteomics, 173, 22-31 (2018)
Transferrin: structure, function and potential therapeutic actions
Drug Discovery Today, 10(4), 267-273 (2005)
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