What are the differences between Human Holo-Transferrin Protein, CF (Catalog # 2914-HT) and Human Apo-Transferrin Protein, CF (Catalog # 3188-AT)?

Human Transferrin has two different iron binding domains, one at the N-terminus and one at the C-terminus. Apo-transferrin (3188-AT) is not bound to any iron atoms and Holo-Transferrin (2914-HT) has an iron atom bound at both the N- and C-terminal domains.

What is the accession number associated with the Human Apo-Transferrin Protein, CF (Catalog # 3188-AT)?

Catalog # 3188-AT is derived from donor human plasma. It is not expressed recombinantly; therefore, no accession number is listed for this product.

Human Apo-Transferrin Protein, CF

Name: Human Apo-Transferrin Protein, CF
Brand: R&D Systems
SKU: 3188-AT

R&D Systems, Inc. a Bio-Techne Brand

Catalog # 3188-AT

Citations (5)

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Source:	Human Plasma
Applications:	Bioactivity

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Product Specifications for Human Apo-Transferrin Protein, CF

Source	Human plasma-derived Apo-Transferrin protein The human plasma used for the isolation of this product were certified by the supplier to be negative for HIV I and II antibodies, Hepatitis C antibody and Hepatitis B antigen at the time of shipment. Human blood products should always be treated in accordance with universal handling precautions.
Endotoxin level	<0.10 EU per 1 μg of the protein by the LAL method.
SDS-PAGE	76-81 kDa, reducing conditions
Activity	Measured in a serum-free cell proliferation assay using CHO-K1 cells. The ED₅₀ for this effect is <6.00 μg/mL.

Formulation, Preparation and Storage

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

3188-AT

Formulation	Lyophilized from a 0.2 μm filtered solution in deionized water.
Reconstitution	Reconstitute at 10 mg/mL in sterile, deionized water. Reconstitution Buffer Available: Size / Price Qty Loading... RB07:
Shipping	The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. • 12 months from date of receipt at -20 to -70 °C as supplied. • 1 month at 2-8 °C under sterile conditions after reconstitution. • 3 months at -20 to -70 °C under sterile conditions after reconstitution.

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Background: Apo-Transferrin

Human Transferrin (Tf) is a single chain, 80 kDa member of the anion-binding superfamily of proteins (1 - 5). It is a bilobed molecule that is the product of an ancient gene duplication event (1, 6). Transferrin is synthesized as a 698 amino acid (aa) precursor that is divided into a 19 aa signal sequence plus a 679 aa mature segment that contains 19 intrachain disulfide bonds. The crystal structure of Tf reveals a protein with two flanking 340 aa globular domains. Each are composed of a beta -sheet surrounded by series of alpha -helices (1, 7). The N- and C-terminal flanking regions (or domains) will bind ferric iron through the interaction of an obligate anion (usually bicarbonate) and four amino acids (His, Asp, and two Tyr) (7, 8). Apotransferrin (or iron-free) will initially bind one atom of iron at the C-terminus, and this is followed by subsequent iron binding by the N-terminus to form holotransferrin (diferric Tf) (8, 9). Through its C-terminal iron-binding domain, holotransferrin will interact with the type I Tf receptor (TfR) on the surface of cells where it is internalized into acidified endosomes. Iron dissociates from the Tf molecule within these endosomes, and is transported into the cytosol as ferrous iron. At physiological pH, iron-free Apotransferrin is not bound by TfR. But at acidic pH, such as exists in the endosome, Apotransferrin has considerable affinity for TfR. Thus, it remains bound to TfR and is recycled back to the cell surface where a neutral pH environment dissociates ligand from receptor. Each Tf molecule recycles 100 - 150 times during its lifetime (8 - 11). In addition to TfR, transferrin is reported to bind to cubulin, IGFBP3, microbial iron-binding proteins and liver-specific TfR2 (7, 12, 13, 14). Transferrin is variably glycosylated and the degree of sialylation is suggestive of certain clinical conditions (15). Finally, Tf is highly allelic and the gene codominant, with many single aa changes noted. Three general forms are known, based on standard electrophoretic mobility. Fast Tf is known as transferrin B, slow transferrin is transferrin D, and the middle migrating transferrin is type/variant C, the most common (16, 17). Mature human TF is 73% aa identical to both mouse and rat Tf, and 68% and 71% aa identical to bovine and equine Tf, respectively.

Item	Value
References	Brus, C.M. et al. (2001) Nat. Struct. Biol. 4:919. Schaeffer, E. et al. (1987) Gene 56:109. MacGillivray, R.T.A. et al. (1983) J. Biol. Chem. 258:3543. Yang, F. et al. (1984) Proc. Natl. Acad. Sci. USA 81:2752. Uzan, G. et al. (1984) Biochem. Biophys. Res. Commun. 119:273. Zak, O. et al. (2002) Biochemistry 41:7416. Gomme, P.T. and K. B. McCann (2005) Drug Discov. Today 10:267. Liu, R. et al. (2003) Biochemistry 42:12447. Pakdaman, R. et al. (1999) J. Mol. Biol. 293:1273. Hemadi, M. et al. (2004) Biochemistry 43:1736. Aisen, P. et al. (2001) Int. J. Biochem. Cell Biol. 33:940. Kozyraki, R. et al. (2001) Proc. Natl. Acad. Sci. USA 98:12941. Boulton, I.C. et al. (1998) Biochem. J. 334:269. Robb, A. and M. Wessling-Resnick (2004) Blood 104:4294. Landberg, E. et al. (1995) Biochem. Biophys. Res. Commun. 210:267. Gorg, A. et al. (1983) Hum. Genet. 64:222. Bean, P. and J.B. Peter (1994) Clin. Chem. 40:2078.
Alternate Names	Apo-Transferrin, ApoTransferrin, CD71, T9, TFR, TFR1, TFRC, TR, TRFR, p90, transferrin receptor (p90, CD71)

References

Brus, C.M. et al. (2001) Nat. Struct. Biol. 4:919.
Schaeffer, E. et al. (1987) Gene 56:109.
MacGillivray, R.T.A. et al. (1983) J. Biol. Chem. 258:3543.
Yang, F. et al. (1984) Proc. Natl. Acad. Sci. USA 81:2752.
Uzan, G. et al. (1984) Biochem. Biophys. Res. Commun. 119:273.
Zak, O. et al. (2002) Biochemistry 41:7416.
Gomme, P.T. and K. B. McCann (2005) Drug Discov. Today 10:267.
Liu, R. et al. (2003) Biochemistry 42:12447.
Pakdaman, R. et al. (1999) J. Mol. Biol. 293:1273.
Hemadi, M. et al. (2004) Biochemistry 43:1736.
Aisen, P. et al. (2001) Int. J. Biochem. Cell Biol. 33:940.
Kozyraki, R. et al. (2001) Proc. Natl. Acad. Sci. USA 98:12941.
Boulton, I.C. et al. (1998) Biochem. J. 334:269.
Robb, A. and M. Wessling-Resnick (2004) Blood 104:4294.
Landberg, E. et al. (1995) Biochem. Biophys. Res. Commun. 210:267.
Gorg, A. et al. (1983) Hum. Genet. 64:222.
Bean, P. and J.B. Peter (1994) Clin. Chem. 40:2078.

Alternate Names

Apo-Transferrin, ApoTransferrin, CD71, T9, TFR, TFR1, TFRC, TR, TRFR, p90, transferrin receptor (p90, CD71)

Citations for Human Apo-Transferrin Protein, CF (5)

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Citations are publications that use Bio-Techne products. Selected citations for Human Apo-Transferrin Protein, CF include:

Species: Human
Sample Types: Reference Standard

C Agliardi et al. (2021), The VDR FokI (rs2228570) polymorphism is involved in Parkinson's disease Journal of the neurological sciences, 428(0):117606.
PMID: 34365149
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

RM Giadone et al. (2020), Expression of Amyloidogenic Transthyretin Drives Hepatic Proteostasis Remodeling in an Induced Pluripotent Stem Cell Model of Systemic Amyloidï¿½Disease Stem Cell Reports, 0(0).
PMID: 32735824
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

KRQ Lim et al. (2020), DUX4 transcript knockdown with antisense 2'-O-methoxyethyl gapmers for the treatment of facioscapulohumeral muscular dystrophy Mol Ther, 0(0).
PMID: 33068777
Species: Human
Sample Types: Protein
Applications: Reference Standard

WF Zeno et al. (2019), Molecular Mechanisms of Membrane Curvature Sensing by a Disordered Protein J. Am. Chem. Soc., 0(0).
PMID: 31180661
Species: Human
Sample Types: Whole Cells
Applications: Bioassay

Staquicini FI et al. (2011), Systemic combinatorial peptide selection yields a non-canonical iron-mimicry mechanism for targeting tumors in a mouse model of human glioblastoma. J. Clin. Invest., 121(1):161-73.
PMID: 21183793

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Showing 1 - 5 of 5 citations Showing All

FAQs for Human Apo-Transferrin Protein, CF

What are the differences between Human Holo-Transferrin Protein, CF (Catalog # 2914-HT) and Human Apo-Transferrin Protein, CF (Catalog # 3188-AT)?

Human Transferrin has two different iron binding domains, one at the N-terminus and one at the C-terminus. Apo-transferrin (3188-AT) is not bound to any iron atoms and Holo-Transferrin (2914-HT) has an iron atom bound at both the N- and C-terminal domains.
What is the accession number associated with the Human Apo-Transferrin Protein, CF (Catalog # 3188-AT)?

Catalog # 3188-AT is derived from donor human plasma. It is not expressed recombinantly; therefore, no accession number is listed for this product.

Human Apo-Transferrin Protein, CF

R&D Systems, Inc. a Bio-Techne Brand

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Product Specifications for Human Apo-Transferrin Protein, CF

Formulation, Preparation and Storage

Carrier Free

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Background: Apo-Transferrin

Citations for Human Apo-Transferrin Protein, CF (5)

FAQs for Human Apo-Transferrin Protein, CF

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