Product Details

Purity

>85% (SDS-PAGE)

Uniprot No.

P02789

Alternative Names

Ovotransferrin; Allergen Gal d III; Conalbumin; Serum transferrin; allergen Gal d 3

Species

Gallus gallus (Chicken)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Target Background

Function

Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. Responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. There are two forms of hen transferrin, ovotransferrin, found in the ovoducts and, serum transferrin, secreted by the liver. Serum transferrin may also have a role in stimulating cell proliferation and is regulated by iron levels. Ovotransferrin has a bacteriostatic function and, is not controlled by iron levels.

Gene References into Functions

unfolding pathway and conformational stability of conalbumin PMID: 21833676
glycosylation of fetal & hen ovotransferrin differs; hypothesized to alter ovotransferrin recognition by carbohydrate binding lectins PMID: 7881176
studied the carbohydrate and amino acid compositions of the ovotransferrin glycopeptides PMID: 574451
The exon structure of the ovotransferrin gene confirms the duplication event to produce two homologous domains that make up ovotransferrin PMID: 3658709
evidence suggests that conalbumin (ovotransferrin) and transferrin are products of the same gene, differing only in carbohydrate content PMID: 4907959
show both lobes are required for efficient iron binding and calculate binding kinetics. PMID: 6319414
ovotransferrin folds into two compact, iron-binding domains; the authors demonstrate that the duplicated domain structure is necessary to retain ovotransferrin in plasma and stop immediate loss via kidney filtration PMID: 6805466
The structure of ovotransferrin shows that the iron-binding site is located in the interdomain cleft in each lobe; differences in ovotransferrin structure cause changes to iron binding & uptake/release compared to lactotransferrin & transferrin. PMID: 7490743
At a pH where the protein net charge is negative (pH 8.0), the behavior of ovotransferrin at the air-water interface is more influenced by charge effects rather than bulk concentration effects. PMID: 21316692
Trp-Asn-Ile-Pro and Gly-Trp-Asn-Ile peptides of ovotransferrin showed the highest antioxidant activity. PMID: 20568771
Marked stabilization effects by amino(N)- and carboxyl(C)-terminal lobes of ovotransferrin are induced during iron binding, primarily upon N-lobe iron binding in the iron-free C-lobe and secondarily upon C-lobe iron binding in the monoferric N-lobe. PMID: 15323571
Ovotransferrin is able to cleave itself through the unique chemical reactivity of four tripeptides motifs, HTT (residues 209-211), HST (residues 542-544) and two CHT (residues 115-117 and 454-456). PMID: 16442235
Several proteins associated with the egg shell membranes (ESM) with antibacterial activity have been identified including ovotransferrin, in addition, pure fractions of ovotransferrin were obtained from egg white. PMID: 16721662

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Subcellular Location

Secreted.

Protein Families

Transferrin family

Tissue Specificity

Expressed in the magnum of the oviduct (at protein level).

Database Links

KEGG: gga:396241

UniGene: Gga.2551

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