Recombinant Rat Erythropoietin / EPO Protein (His Tag)

Name: Recombinant Rat Erythropoietin / EPO Protein (His Tag)
Brand: Beta LifeScience
SKU: BLPSN-1924
Availability: InStock

Collections: Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

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Product Overview

Tag	His
Host Species	Rat
Accession	P29676
Background	Erythropoietin is a member of the EPO / TPO family. It is a secreted, glycosylated cytokine composed of four alpha helical bundles. Erythropoietin can be found in the plasma and regulates red cell production by promoting erythroid differentiation and initiating hemoglobin synthesis. It also has neuroprotective activity against a variety of potential brain injuries and antiapoptotic functions in several tissue types. Erythropoietin is the principal hormone involved in the regulation of erythrocyte differentiation and the maintenance of a physiological level of circulating erythrocyte mass. It is produced by kidney or liver of adult mammals and by liver of fetal or neonatal mammals. Genetic variation in erythropoietin is associated with susceptbility to microvascular complications of diabetes type 2. These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new-onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. It has a longer circulating half-life in vivo. Erythropoietin is being much misused as a performance-enhancing drug in endurance athletes.
Description	A DNA sequence encoding the rat EPO (P29676-1) (Met 1-Arg 192) was fused with a His tag at the C-terminus.
Source	Baculovirus-Insect Cells
Predicted N Terminal	Ala 27
AA Sequence	Met 1-Arg 192
Molecular Weight	The recombinant rat EPO comprises 176 a.a. with and has a predicted molecular mass of 20 kDa. It migrates as an approximately 27 kDa band in reduced SDS-PAGE.
Purity	>90% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	1. Measured by its ability to bind human EPOR-Fc in a functional ELISA.2. Measured by its ability to bind biotinylated human EPOR-His in a functional ELISA.3. Measured by its ability to bind mouse EPOR-Fch in a functional ELISA.4. Measured by its ability to bind human EPOR & CD131-Fc in a functional ELISA.5. Measured by its ability to inhibit Epo-dependent proliferation of TF1 human erythroleukemic cells.The ED50 for this effect is 2-10ng/mL.
Formulation	Lyophilized from sterile 20mM Tris, 500mM NaCl, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.