Transferrin, Rat, Western Blot Positive Control control product blog
Tags: Control; Transferrin, Rat, Western Blot Positive Control; Transferrin, Rat, Western Blot Positive Control control;
The Transferrin, Rat, Western Blot Positive Control n/a (Catalog #MBS652618) is an Immunoglobulin produced from Rat and is intended for research purposes only. The product is available for immediate purchase. MyBioSource\'s Transferrin, Rat, Western Blot Positive Control can be used in a range of immunoassay formats including, but not limited to, Western Blot (WB).Suitable for use in Western Blot.
Dilution: Western Blot: 10ul/lane
Optimal dilution to be determined by researcher. Researchers should empirically determine the suitability of the Transferrin, Rat, Western Blot Positive Control n/a for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process.
To buy or view more detailed product information and pricing, please click on the technical datasheet page below:
Please refer to the product datasheet for known applications of a given immunoglobulin. We\'ve tested the Transferrin, Rat, Western Blot Positive Control (Tf) with the following immunoassay(s):
Testing Data (Transferin, TF, Apotransferrin, Beta-1 Metal-binding Globulin, DKFZp781D0156, PRO1400, PRO1557, PRO2086, Serotransferrin Precursor, Siderophilin)
Elemental iron is required for a variety of normal cellular functions and vital for proper growth and development. However, natural iron is quite insoluble and excess iron is harmful, since it can catalyze the formation of potentially damaging reactive oxygen species. The major pool of body iron (~85%; 40-50 mg/kg) is found in circulating hemoglobin and muscle myoglobin. Iron absorption occurs primarily in the intestine (duodenum) and inversely related to body iron reserve. Several proteins including Ferritin, transferrin (Tf), transferrin receptors (TfRs), and iron regulatory proteins (IRPs) etc play a key role in iron metabolism.
Transferrin (Tf, human chromosome 3, 679 aa), a serum glycoprotein of ~80kD and synthesized in the liver, is the primary protein of inter-organ transport of nonheme iron. Tf can bind two iron atoms. Tf binds to membrane Transferrin receptors (TfRs) and taken up by endocytosis. Iron is released from Tf, within acidic endosomes, into the cytoplasm apparently through the action of DMT1. The apoTf-TfR complex is returned to the cell surface, where, apo-Tf dissociates from TfR at the extracellular pH. The classical TfR, now termed TfR1, is a homodimeric (95kD subunits) type II membrane glycoprotein that binds two molecules of Tf. Human TfR1 (human 760 aa; mouse 763 aa) has a cytoplasmic domain 1-67aa, 68-88 aa TM, and 89-760 aa as extracellular domains. A monomeric serum form or soluble TfR1 (~80kD) also exists that lacks residues 1-100 aa. Recently, a second Tf receptor, TfR2, has been cloned and characterized. TfR2 shares 45% identity with TfR1, and 27% with PMSA. Several variants of Tf have been identified with varying iron binding ability.