SRP6472

Sigma-Aldrich

Transferrin human

recombinant, expressed in HEK 293 cells, ≥95% (SDS-PAGE)

Sinónimos:
PRO2086, DKFZp781D0156, PRO1557, TF
NACRES:
NA.32
En este momento no podemos mostrarle ni los precios ni la disponibilidad

biological source

human

recombinant

expressed in HEK 293 cells

assay

≥95% (SDS-PAGE)

form

lyophilized

mol wt

calculated mol wt 76 kDa
observed mol wt 74 kDa by SDS-PAGE (DTT-reduced.)

packaging

pkg of 100 μg
pkg of 20 μg

impurities

<1 EU/μg endotoxin (LAL test)

conjugate

6-His tagged (C-terminus)

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... TF(7018)

General description

Transferrin is encoded by the TF gene that is mapped to human chromosome 3q22.1. It is a glycoprotein containing homologous iron-binding domains at N-terminal and C-terminal ends. Transferrin has a molecular weight of 80,000 Da and belongs to the transferrin superfamily, the members of which include lactoferrin, melanotransferrin, and ovotransferrin.

Application

To supplement neurosphere culture medium and sphere differentiation medium.

Biochem/physiol Actions

Transferrin is an iron-binding glycoprotein that primarily functions in the transport of plasma iron in vertebrates. It may also have a secondary function of facilitating cell proliferation. The binding of ferric iron to transferrin requires the presence of an anion, that functions as a bridge between the metal and the protein.

Physical form

Lyophilized from 0.22 μm filtered solution in 50 mM tris, 100 mM glycine, pH 7.0. Normally Mannitol or Trehalose is added as protectants before lyophilization.

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 μg/mL. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.

RIDADR

NONH for all modes of transport

WGK Germany

WGK 3

Certificado de Análisis
Phylogenetic analyses uncover a novel clade of transferrin in nonmammalian vertebrates.
Mohd-Padil H
Molecular Biology and Evolution, 30, 894-905 (2013)
The physiology of transferrin and transferrin receptors.
Huebers HA and Finch CA
Physiological Reviews, 67, 520-582 (1987)
Evolution of the mammary gland from the innate immune system?
Vorbach C
Bioessays, 28, 606-616 (2006)
Anion binding by human lactoferrin: results from crystallographic and physicochemical studies.
Shongwe MS
Biochemistry, 31, 4451-4458 (1992)
Surgical management of atheroma of the aortic dome and origin of supra-aortic trunks.
Thevenet A
World Journal of Surgery, 3, 187-195 (1979)

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