G CSF Human
Granulocyte-Colony Stimulating Factor Human Recombinant
Cat. No.
BT60
Source
Escherichia Coli.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Lenograstim, G-CSF, MGC45931, GCSF.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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In Stock 
Description
Granulocyte Colony Stimulating Factor Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 175 amino acids and having a molecular mass of 18.8 KD.
GCSF is purified by proprietary chromatographic techniques.
GCSF is purified by proprietary chromatographic techniques.
Product Specs
Introduction
Granulocyte colony-stimulating factor (GCSF) is a cytokine that regulates the production, differentiation, and function of granulocytes, a type of white blood cell. This cytokine plays a crucial role in the immune system by stimulating the bone marrow to produce and release granulocytes into the bloodstream, where they fight infections. GCSF is primarily found in its active form outside of cells. There are three known transcript variants of the GCSF gene, which result in the production of three different isoforms of the protein. This cytokine belongs to a family of proteins called colony-stimulating factors, which are essential for the formation of blood cells (hematopoiesis). Specifically, GCSF promotes the production of both granulocytes and monocytes-macrophages.
Description
Recombinant Human Granulocyte Colony Stimulating Factor (GCSF) is produced in E.coli. This protein is a single, non-glycosylated polypeptide chain consisting of 175 amino acids. It has a molecular weight of 18.8 kilodaltons (kDa). Our GCSF undergoes purification using proprietary chromatographic techniques to ensure its high purity.
Physical Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Formulation
To prepare the lyophilized GCSF, it was extensively dialyzed against a 10mM sodium acetate buffer with a pH of 4. This process removes impurities and ensures stability during storage.
Solubility
To reconstitute the lyophilized GCSF, it is recommended to dissolve it in sterile 20mM acetic acid (AcOH) at a concentration of not less than 100 micrograms per milliliter (µg/ml). This solution can then be further diluted using other aqueous solutions as needed.
Stability
Lyophilized GCSF, while stable at room temperature for up to 3 weeks, should be stored in a dry environment below -18 degrees Celsius for optimal long-term preservation. Once reconstituted, GCSF should be stored at 4 degrees Celsius for 2-7 days. For extended storage, it is advisable to freeze the solution at -18 degrees Celsius. To prevent degradation, avoid repeated freezing and thawing of the reconstituted GCSF. For long-term storage, consider adding a carrier protein like albumin (HSA or BSA) at a concentration of 0.1%.
Purity
The purity of our GCSF is greater than 98%, as determined by two independent analytical methods: Reverse-Phase High-Performance Liquid Chromatography (RP-HPLC) and Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis (SDS-PAGE).
Biological Activity
The biological activity of our GCSF is measured by its ability to stimulate the proliferation of murine NFS-60 indicator cells. The ED50, which represents the concentration of GCSF required to achieve half-maximal cell proliferation, is determined to be less than 0.1 nanograms per milliliter (ng/ml) using a 3H-thymidine uptake assay. This corresponds to a Specific Activity of 100,000,000 International Units per milligram (IU/mg).
Protein Content
The protein content of our GCSF is quantified using two independent methods to ensure accuracy. The first method involves measuring the absorbance of a 0.1% (1mg/ml) GCSF solution at a wavelength of 280 nanometers (nm) using UV spectroscopy. An extinction coefficient of 0.815, calculated using the PC GENE computer analysis program (IntelliGenetics), is used to determine the protein concentration. The second method utilizes RP-HPLC analysis, comparing the GCSF sample to a calibrated Reference Standard solution.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Lenograstim, G-CSF, MGC45931, GCSF.
Source
Escherichia Coli.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids of GCSF was determined and was found to be Met-Thr-Pro-Leu-Gly.
Product Science Overview
Discovery and Development
G-CSF was first identified in the 1980s as a key regulator of neutrophil production. The recombinant form, rhG-CSF, was developed to provide a consistent and reliable source of this growth factor for clinical use. The recombinant technology involves inserting the gene responsible for G-CSF production into bacterial or mammalian cells, which then produce the protein in large quantities.
Mechanism of Action
G-CSF binds to specific receptors on the surface of hematopoietic stem cells and progenitor cells, stimulating their proliferation and differentiation into mature neutrophils. This process is essential for maintaining adequate neutrophil levels in the body, which are crucial for fighting infections.
Clinical Applications
rhG-CSF is widely used in clinical settings for several purposes:
- Neutropenia Treatment: It is commonly used to treat neutropenia, a condition characterized by low levels of neutrophils, which can result from chemotherapy, radiation therapy, or bone marrow transplantation.
- Stem Cell Mobilization: rhG-CSF is used to mobilize hematopoietic stem cells from the bone marrow into the peripheral blood, facilitating their collection for stem cell transplantation.
- Supportive Care in Cancer Therapy: It helps reduce the risk of infection in cancer patients undergoing chemotherapy by boosting their neutrophil counts.
Advances in Formulation
Safety and Efficacy
Clinical studies have demonstrated the efficacy and safety of rhG-CSF in various patient populations. It has been shown to significantly reduce the incidence of febrile neutropenia and improve outcomes in patients undergoing chemotherapy . The pegylated form has also been found to be effective in mobilizing hematopoietic stem cells for transplantation .
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