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GW20009F

Sigma-Aldrich

Anti-Transferrin antibody produced in chicken

affinity isolated antibody, buffered aqueous solution

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Synonym(s):
Anti-Serotransferrin, Anti-Siderophilin

biological source

chicken

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

mouse, human, rat

manufacturer/tradename

Genway 15-288-20009F

technique(s)

indirect ELISA: suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... TF(7018)

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This Item
AB3487HPA005692GW20073F
Anti-Transferrin Antibody Chemicon®, from chicken

AB3487

Anti-Transferrin Antibody

biological source

chicken

biological source

chicken

biological source

rabbit

biological source

chicken

antibody form

affinity isolated antibody

antibody form

affinity purified immunoglobulin

antibody form

affinity isolated antibody

antibody form

affinity isolated antibody

UniProt accession no.

P02787

UniProt accession no.

P02787

UniProt accession no.

P02787

UniProt accession no.

P01024

shipped in

wet ice

shipped in

dry ice

shipped in

wet ice

shipped in

wet ice

species reactivity

mouse, human, rat

species reactivity

human

species reactivity

human

species reactivity

human

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Immunogen

Immunogen Sequence: GI # 4557871, sequence 1-698
Serotransferrin native protein.

Application

Anti-Transferrin antibody produced in chicken is suitable for western blotting at a working dilution of 1:500 and for cell staining at a working dilution of 1:200. It is also used for indirect ELISA.

Biochem/physiol Actions

Transferrin is a glycoprotein that binds to and transports Fe3+ ions from the intestine, reticuloendothelial system, and liver parenchymal cells to all proliferating cells in the body. It may also stimulate cell proliferation by supplying iron during DNA synthesis. Abnormal synthesis of transferrin may lead to accumulation of iron and microcytic hypochromic anemia.

Physical form

Solution in phosphate buffered saline containing 0.02% sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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The role of transferrin in the mechanism of cellular iron uptake.
K Thorstensen et al.
The Biochemical journal, 271(1), 1-9 (1990-10-01)
H A Huebers et al.
Blood, 61(2), 283-290 (1983-02-01)
A mechanism is proposed by which apotransferrin is secreted from mucosal cells, loaded with iron in the intestinal lumen, and then the intact complex is taken into the cell. Within the cell, iron is released and transferred to the blood
E D Letendre et al.
Infection and immunity, 44(2), 320-325 (1984-05-01)
Hypoferremia, the reduction of plasma transferrin iron levels during infection, has been shown to control Neisseria meningitidis infection in mice. The exact nature of the mechanism that regulates this response has been obscure. We have previously shown that hypoferremia does
J Laskey et al.
Experimental cell research, 176(1), 87-95 (1988-05-01)
Transferrin is essential for cell proliferation and it was suggested that it may trigger a proliferative response following its interaction with receptors, serving as a growth factor. However, since the only clearly defined function of transferrin is iron transport, it
Jérôme Clatot et al.
Nature communications, 8(1), 2077-2077 (2017-12-14)
Fast opening and closing of voltage-gated sodium channels are crucial for proper propagation of the action potential through excitable tissues. Unlike potassium channels, sodium channel α-subunits are believed to form functional monomers. Yet, an increasing body of literature shows inconsistency

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