EPO a Fc Human

Erythropoietin-Alpha Fc-Chimera Human Recombinant

Erythropoietin-alpha Fc-Chimera Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a dimeric, glycosilated, polypeptide chain consisting of two mature human EPO molecules linked to the Fc portion of human IgG1. The Fc component contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 140 kDa in non-reducing SDS-PAGE.
Shipped with Ice Packs
Cat. No.
BT4933
Source
Chinese Hamster Ovary Cells(CHO).
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

EPO a Human

Erythropoietin-Alpha Human Recombinant

Erythropoietin-alpha Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a single, polypeptide chain containing 166 amino acids and having a predicted molecular mass of 21,000 Dalton and apparent glycosylated molecular mass of 36-40kDa. EPO-a is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5071
Source
Chinese Hamster Ovary Cells(CHO).
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

EPO a Human, HEK

Erythropoietin-alpha Human Recombinant, HEK

EPO-a Human Recombinant produced in HEK cells is a glycosylated monomer, having a total molecular weight of 36kDa.
The EPO-alpha is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5127
Source
HEK.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

EPO a Human, His

Erythropoietin-alpha Human Recombinant, His Tag

EPO a Human Recombinant produced in Baculovirus is a single, glycosylated polypeptide chain containing 174 amino acids (28-193a.a.) and having a molecular mass of 19.5kDa.
EPO a is fused to an 8 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT5245
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered clear solution.

EPO a Human, Sf9

Erythropoietin-alpha Human Recombinant, Sf9

Erythropoietin-alpha Human Recombinant produced in Sf9 Insect cells is a single, glycosylated polypeptide chain containing 174 amino acids (28-193a.a.) and having a molecular mass of 19.5kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).
EPO-a is expressed with an 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5302
Source
Sf9, Insect cells.
Appearance
Sterile filtered colorless solution.

EPO Mouse

Erythropoietin Mouse Recombinant

EPO Mouse Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 176 amino acids (27-192 aa) and having a molecular mass of 19.8kDa.
EPO is fused to a 9 amino acid His tag at C-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT5362
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.

EPO Rat

Erythropoietin Rat Recombinant

EPO Rat Recombinant produced in HEK293 cells is a single, glycosylated polypeptide chain (27-192 a.a) containing 175 amino acids and having a molecular mass of 19.6 kDa. EPO is fused to a 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT5429
Source

HEK293 cells.

Appearance
Sterile Filtered colorless solution.

EPOR Human

Erythropoietin Receptor Human Recombinant

EPOR Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 232 amino acids (25-250 a.a) and having a molecular mass of 25.6kDa. (Migrates at 28-40kDa on SDS-PAGE under reducing conditions). EPOR is fused to an 6 amino acid His-tag at C-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5498
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered clear solution.

EPOR Human, Active

Erythropoietin Receptor Human Recombinant, Active

EPOR produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 232 amino acids (25-250a.a.) and having a molecular mass of 25.6kDa (Molecular size on SDS-PAGE will appear at approximately 28-40kDa).
EPOR is expressed with a 6 amino acid His-tag at C-Terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5567
Source
Sf9, Baculovirus cells.
Appearance
Sterile Filtered clear solution.
Definition and Classification

Erythropoietin (EPO) is a glycoprotein cytokine primarily produced by the kidneys in response to cellular hypoxia. It stimulates the production of red blood cells (erythropoiesis) in the bone marrow . EPO is also known as erythropoetin, haematopoietin, or haemopoietin .

Biological Properties

Key Biological Properties: EPO is highly glycosylated, with approximately 40% of its molecular weight attributed to carbohydrate content . It has a half-life of around 5 hours in the bloodstream .

Expression Patterns: EPO is produced mainly by interstitial fibroblasts in the kidneys and, to a lesser extent, by perisinusoidal cells in the liver . During fetal development, the liver is the primary site of EPO production .

Tissue Distribution: EPO is found in the kidneys, liver, and bone marrow. It is also present in the central nervous system and uterus, where it has paracrine functions .

Biological Functions

Primary Biological Functions: EPO’s main role is to regulate red blood cell production by promoting the survival, proliferation, and differentiation of erythroid progenitor cells . It protects these cells from apoptosis (cell death) .

Role in Immune Responses and Pathogen Recognition: While EPO’s primary function is erythropoiesis, it also has roles in immune modulation and tissue protection. It has been shown to have anti-inflammatory effects and can protect tissues from ischemic damage .

Modes of Action

Mechanisms with Other Molecules and Cells: EPO exerts its effects by binding to the erythropoietin receptor (EPO-R) on the surface of erythroid progenitor cells . This binding triggers several intracellular signaling pathways, including the JAK2/STAT5, PI3K/AKT, and MAPK pathways .

Binding Partners and Downstream Signaling Cascades: The activation of EPO-R leads to the phosphorylation of JAK2, which in turn activates STAT5. Activated STAT5 translocates to the nucleus and promotes the transcription of genes involved in erythroid differentiation and survival .

Regulatory Mechanisms

Control of Expression and Activity: EPO production is primarily regulated by oxygen levels. Hypoxia induces the stabilization of hypoxia-inducible factor 1 (HIF-1), which binds to the EPO gene promoter and enhances its transcription .

Transcriptional Regulation: HIF-1 is a key transcription factor that regulates EPO expression under low oxygen conditions . Other factors, such as GATA2, can inhibit EPO transcription during normoxia .

Post-Translational Modifications: EPO undergoes glycosylation, which is crucial for its stability and activity in the bloodstream .

Applications

Biomedical Research: EPO is used extensively in research to study erythropoiesis and hypoxia-related pathways .

Diagnostic Tools: EPO levels are measured to diagnose and manage conditions like anemia and polycythemia .

Therapeutic Strategies: Recombinant human EPO (rhEPO) is used to treat anemia associated with chronic kidney disease, chemotherapy, and certain chronic diseases . It is also used to reduce the need for blood transfusions in surgical patients .

Role in the Life Cycle

Development: During fetal development, EPO is primarily produced by the liver and plays a crucial role in ensuring adequate red blood cell production .

Aging and Disease: In adults, EPO production shifts to the kidneys. Its levels can be affected by various conditions, including chronic kidney disease and anemia . EPO also has protective roles in tissues undergoing ischemic stress .

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