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T4132

holo-Transferrin human

≥98%

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Synonym(s):

Siderophilin, iron-saturated

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100 mg

Available to ship TODAYfromMILWAUKEE

$227.00
500 mg

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$654.00
1 g

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$1,130.00

About This Item

CAS Number:
UNSPSC Code:
12352202
EC Number:
234-318-8
NACRES:
NA.61
MDL number:
eCl@ss:
34058011
Form:
powder
Assay:
≥98%
Biological source:
human

$227.00

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biological source

human

Quality Segment

assay

≥98%

form

powder

Iron content

1100-1600 μg/g

technique(s)

cell culture | mammalian: suitable

impurities

HIV, hepatitis B and hepatitis C, none detected

UniProt accession no.

storage temp.

2-8°C

Gene Information

human ... TF(7018)

General description

Transferrin (TF) belongs to the family of bilobal glycoproteins, which bind ferric iron. The homologous N- and C-lobes of the protein have a single iron-binding site present in a deep cleft. The gene encoding TF is localized on human chromosome 3q22.1.

Application

Human holo-transferrin has been used:
  • in colony-forming assays
  • for transferrin uptake and recycling in transfected HEK-293 (human embryonic kidney) cells or bone marrow cells
  • for the preparation of luteinizing and non- luteinizing granulose cells

Biochem/physiol Actions

Transferrin (TF) is the iron transport protein in the blood. Iron is transported in the serum by binding to circulating transferrin, which in turn binds to receptors on the cell surface. At the alkaline extracellular pH of 7.4, TF binds one or two ferric ions. The iron-bound TF molecules can bind the dimeric transferrin receptor (TfR). At this pH, iron-free transferrin is not recognized by TfR. This is followed by an endocytotic pathway involving the TfR, where the entire complex is internalized by endocytosis. As the pH reduces in the cell, iron is released from TF. The complex then returns to the cell surface and the apo-TF molecules dissociate from the receptor.
Studies have shown that co-treatment of breast cancer cells with holo-transferrin, which increases iron levels within cells and derivatives of artemisinin results in increased cell death.

Analysis Note

Purity by agarose gel electrophoresis.

Disclaimer

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.

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T330990190T3705
description

≥98%

description

≥98%

description

≥95% (GE)

description

Optiferrin, recombinant, expressed in rice

biological source

human

biological source

human

biological source

human plasma

biological source

human

assay

≥98%

assay

≥98%

assay

≥95% (GE)

assay

≥95% (agarose gel electrophoresis)

technique(s)

cell culture | mammalian: suitable

technique(s)

cell culture | stem cell: suitable

technique(s)

tissue culture: suitable

technique(s)

immunoprecipitation (IP): suitable, tissue culture: suitable

form

powder

form

powder

form

powder or crystals

form

powder

impurities

HIV, hepatitis B and hepatitis C, none detected

impurities

≤1.0 EU/mg endotoxin

impurities

≤0.01% iron traces (AAS)

impurities

≤1.0 EU/mg Endotoxin

UniProt accession no.

P02787

UniProt accession no.

P02787

UniProt accession no.

P02787

UniProt accession no.

P02787


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Storage Class

11 - Combustible Solids

wgk

WGK 3



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Questions

1–4 of 4 Questions  
  1. Can this be resuspended in water at 50 mg/ml and stored at -20 for up to a year as is recommended in other products?

    1 answer
    1. This product is soluble in water at 50 mg/mL. Sterile solutions may be stored at 2–8 °C. The stability of this product in solution has not been investigated.

      However, supplements containing transferrin, such as I3146, ITS Supplement, are stable for 2 years from the date of quality release, when stored refrigerated at 2–8 °C. Transferrin is also a natural constituent of serum/plasma, which is typically stored frozen at -20 °C for extended periods. Similar stability is expected for stock solution of the Transferrin component in water.

      As a general rule, store frozen stock solutions in aliquots, avoid repeated freeze/thaw cycles.

      Please see the link below to review additional information available in the product datasheet:
      https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/130/436/t4132pis.pdf

      Helpful?

  2. Hi, does T4132 holo-Transferrin Human contain any native human biological materials (e.g., human serum, urine etc. Not a recombinant protein.)? If so, please confirm whether the native human biological materials are purified or not.

    1 answer
    1. This product is not recombinant. It is native holo-Transferrin from human plasma. The material is isolated by ammonium sulfate precipitation on plasma, followed by column chromatography purification steps. However, the compound has not been affinity purified and there is no additional testing to determine the presence of trace impurities. Please see an example or lot-specific Certificate of Analysis at the link below:
      https://www.sigmaaldrich.com/product/sigma/t4132#product-documentation

      Please see the link below to review the product datasheet:
      https://www.sigmaaldrich.com/deepweb/assets/sigmaaldrich/product/documents/130/436/t4132pis.pdf

      Helpful?

  3. What is the carbohydrate content of human transferrin?

    1 answer
    1. We have found the information on transferrin in a reference book:The Plasma Proteins, F.W. Putnam, ed, volume 2, chapter 4, Table II.According to the table, Transferrin is 6 percent carbohydrate, citing G.A. Jamieson, J. Biol. Chem. 240(7), 2914-2920 (1965).The table also gives information on the percentage of each type of monosaccharide that is present.

      Helpful?

  4. What is the Department of Transportation shipping information for this product?

    1 answer
    1. Transportation information can be found in Section 14 of the product's (M)SDS.To access the shipping information for this material, use the link on the product detail page for the product.

      Helpful?

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