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Merck

T0523

Sigma-Aldrich

apo-Transferrin from mouse

≥98%

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About This Item

Número de CAS:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

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)


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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)
Cells: Molecules and Mechanisms (2009)
Transferrin: structure, function and potential therapeutic actions
Gomme PT, et al.
Drug Discovery Today, 10(4), 267-273 (2005)
Quantitative serum proteomics from surface plasmon resonance imaging
Lausted C, et al.
Molecular and Cellular Proteomics, 7(12), 2464-2474 (2008)
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.

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