EPO a Fc Human

Erythropoietin-Alpha Fc-Chimera Human Recombinant

Erythropoietin-alpha Fc-Chimera Human Recombinant, produced in Chinese hamster ovary (CHO) cells using recombinant DNA technology, is a dimeric, glycosylated polypeptide chain. It consists of two mature human EPO molecules linked to the Fc portion of human IgG1. The Fc component includes the CH2 domain, the CH3 domain, and the hinge region, but excludes the CH1 domain of IgG1. Due to glycosylation, the recombinant protein exhibits 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 powder.

EPO a Human

Erythropoietin-Alpha Human Recombinant

Recombinant human erythropoietin-alpha, a single polypeptide chain containing 166 amino acids, is produced in Chinese hamster ovary (CHO) cells using recombinant DNA technology. With a predicted molecular mass of 21 kDa and an apparent glycosylated molecular mass of 36-40 kDa, EPO-a is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5071
Source
Chinese Hamster Ovary Cells(CHO).
Appearance
White, lyophilized (freeze-dried) powder, sterile filtered.

EPO Rat

Erythropoietin Rat Recombinant

Recombinant Rat EPO, expressed in HEK293 cells, is a single, glycosylated polypeptide chain consisting of 175 amino acids (27-192 a.a). With a molecular weight of 19.6 kDa, this EPO protein features a 6-amino acid His-tag at the C-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5429
Source

HEK293 cells.

Appearance
A clear, colorless solution that has been sterilized by filtration.

EPOR Human

Erythropoietin Receptor Human Recombinant

Recombinant human EPOR, produced in Sf9 insect cells using a baculovirus expression system, is a single glycosylated polypeptide chain. This protein consists of 232 amino acids (25-250 a.a), has a molecular weight of 25.6 kDa, and appears as a band between 28-40 kDa on SDS-PAGE under reducing conditions. This discrepancy in observed versus calculated molecular weight is attributed to glycosylation. The EPOR protein is engineered with a 6-amino acid His-tag at the C-terminus to facilitate purification using chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5498
Source
Sf9, Baculovirus cells.
Appearance
The purified EPOR protein solution is clear and sterile-filtered.

EPOR Human, Active

Erythropoietin Receptor Human Recombinant, Active

Produced in Sf9 insect cells using baculovirus expression system, this recombinant EPOR is a single, glycosylated polypeptide chain. It consists of 232 amino acids (25-250a.a.), resulting in a molecular mass of 25.6 kDa. However, on SDS-PAGE, it appears as a band at approximately 28-40 kDa due to glycosylation. This EPOR protein features a 6-amino acid His-tag at its C-terminus, facilitating purification through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5567
Source
Sf9, Baculovirus cells.
Appearance
A clear, sterile-filtered solution.

EPO a Human, HEK

Erythropoietin-alpha Human Recombinant, HEK

Recombinant Human EPO-alpha, produced in HEK cells, is a glycosylated monomer with a molecular weight of 36kDa. Purification of EPO-alpha is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5127
Source
HEK.
Appearance
The product appears as a sterile, filtered, white powder that has been lyophilized (freeze-dried).

EPO a Human, His

Erythropoietin-alpha Human Recombinant, His Tag

Recombinant human EPO a, expressed in Baculovirus, is a single, glycosylated polypeptide chain comprising 174 amino acids (28-193a.a.) with a molecular weight of 19.5 kDa. It features an 8 amino acid His-tag fused at the C-terminus and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5245
Source

Sf9, Baculovirus cells.

Appearance
The product is provided as a clear solution that has been sterilized by filtration.

EPO a Human, Sf9

Erythropoietin-alpha Human Recombinant, Sf9

Produced in Sf9 Insect cells, Erythropoietin-alpha Human Recombinant is a single, glycosylated polypeptide chain. It comprises 174 amino acids (28-193a.a.) and has a molecular mass of 19.5kDa. However, on SDS-PAGE, its molecular size appears to be approximately 28-40kDa. This EPO-a is characterized by an 8 amino acid His tag at the C-Terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5302
Source
Sf9, Insect cells.
Appearance
The product appears as a sterile, filtered solution that is colorless.

EPO Mouse

Erythropoietin Mouse Recombinant

Recombinant Mouse EPO, expressed in a baculovirus system, is a single glycosylated polypeptide chain with a molecular weight of 19.8 kDa. It comprises 176 amino acids (residues 27-192) and features a 9-amino acid His tag at the C-terminus. Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT5362
Source

Sf9, Baculovirus cells.

Appearance
A sterile, filtered solution that is colorless.
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 .

© Copyright 2024 Thebiotek. All Rights Reserved.