G CSF Human, His

Granulocyte-Colony Stimulating Factor Human Recombinant, His Tag
Cat. No.
BT239
Source
Escherichia Coli.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Appearance
Sterile Filtered clear solution.
Purity
Greater than 95.0% as determined by:
(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.
Shipped with Ice Packs
In Stock

Description

Granulocyte Colony Stimulating Factor-His Tag Human Recombinant produced in E.coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids, fragment (31-204) and having a molecular mass of 23.19 kDa with an amino-terminal hexahistidine tag.
G-CSF-His is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Granulocyte-colony stimulating factor (G-CSF) is a cytokine secreted by macrophages, endothelial cells, and other immune cells. G-CSF stimulates the bone marrow to produce granulocytes and promotes the survival, proliferation, differentiation, and function of neutrophil granulocyte progenitors and mature neutrophils.
Description
Recombinant human granulocyte colony stimulating factor (G-CSF) with a C-terminal hexahistidine tag was expressed in E. coli. It is a single, non-glycosylated polypeptide chain containing the amino acids 31-204 of the mature G-CSF protein, resulting in a molecular mass of 23.19 kDa. The protein was purified using proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
G-CSF His is supplied in a buffer of 1x PBS and 50% glycerol.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For long-term storage, the product should be stored at -20°C. Avoid repeated freeze-thaw cycles.
Purity
The purity is greater than 95.0% as determined by: (a) RP-HPLC and (b) SDS-PAGE.
Synonyms
CSF-3, MGI-1G, GM-CSF beta, Pluripoietin, Filgrastim, Lenograstim, G-CSF, MGC45931, GCSF.
Source
Escherichia Coli.

Product Science Overview

Introduction

Granulocyte-Colony Stimulating Factor (G-CSF) is a glycoprotein that plays a crucial role in hematopoiesis, the process of forming blood cellular components. It specifically stimulates the bone marrow to produce granulocytes and stem cells and release them into the bloodstream . The recombinant form of G-CSF, tagged with a histidine (His) tag, is widely used in research and clinical applications.

Structure and Production

The human recombinant G-CSF with a His tag is produced in Escherichia coli (E. coli). It is a single, non-glycosylated polypeptide chain containing 174 amino acids, with a molecular mass of approximately 23.19 kDa . The His tag, typically consisting of six histidine residues, is added to the N-terminus of the protein to facilitate purification through affinity chromatography.

Biological Function

G-CSF functions as a cytokine and hormone, promoting the proliferation and differentiation of neutrophils, a type of white blood cell essential for combating infections . It binds to the G-CSF receptor on the surface of hematopoietic cells, triggering a cascade of intracellular signaling pathways that lead to the production and release of neutrophils from the bone marrow .

Clinical Applications

Recombinant human G-CSF is used to manage neutropenia, a condition characterized by an abnormally low count of neutrophils. Neutropenia can result from chemotherapy, radiation therapy, or certain diseases . By increasing neutrophil counts, G-CSF reduces the risk of infections in patients undergoing these treatments .

Research Applications

The His-tagged version of recombinant human G-CSF is particularly valuable in research settings. The His tag allows for easy purification and detection of the protein, facilitating studies on its structure, function, and interactions with other molecules . Researchers use this recombinant protein to investigate the mechanisms of hematopoiesis and to develop new therapeutic strategies for treating neutropenia and other related conditions .

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