T0523
apo-Transferrin from mouse
≥98%
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About This Item
Numéro CAS:
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.61
Produits recommandés
Source biologique
mouse
Niveau de qualité
Essai
≥98%
Forme
powder
Technique(s)
protein quantification: suitable
Solubilité
H2O: 20 mg/mL
Numéro d'accès UniProt
Température de stockage
2-8°C
Informations sur le gène
mouse ... Trf(22041)
Description générale
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.
Actions biochimiques/physiologiques
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.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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Les clients ont également consulté
Hasmik Grigoryan et al.
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
Barroso A, et al.
Journal of proteomics, 173, 22-31 (2018)
Transferrin: structure, function and potential therapeutic actions
Gomme PT, et al.
Drug Discovery Today, 10(4), 267-273 (2005)
Cells: Molecules and Mechanisms (2009)
Quantitative serum proteomics from surface plasmon resonance imaging
Lausted C, et al.
Molecular and Cellular Proteomics, 7(12), 2464-2474 (2008)
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