Recombinant Human Granulocyte Colony Stimulating Factor (rHuG-CSF)

SKU:BHP11300345
Overview
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Recombinant human G-CSF produced in Escherichia coli as a single non-glycosylated polypeptide chain of 174 amino acids (~18.7 kDa). Fully biologically active (ED50 <0.1 ng/mL in NFS-60 proliferation assays) with >98% purity by SDS-PAGE and HPLC. Suitable for cell-based assays, binding studies, and assay development.
Expression System E. coli
Species Human
Purity >98%
Molecular Weight 18.7 kDa
Form Lyophilized
Biological Activity ED50 <0.1 ng/mL
Endotoxin Level <1 EU/mg
Options selector
Catalog no. Size
PR1034-2UG 2 ug
PR1034-10UG 10 ug
PR1034-1MG 1 mg
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options: Size: 2 ug, 10 ug, 1 mg
  • Lead time: options listed in "Availability Content"; other statuses may take longer.
  • Storage: This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
  • Shipping: Please contact us to confirm shipping conditions for this product.
  • Upon receipt: store at recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Target CSF3
Species Human
Expression system
  • E. coli
Source Escherichia coli
Molecular weight Approximately 18.7 kDa, a single non-glycosylated polypeptide chain containing 174 amino acids.
Purity >98% by SDS-PAGE and HPLC analyses.
Biological activity Fully biologically active when compared to standard. The ED50 as calculated by the dose-dependant proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake) is less than 0.1 ng/ml, corresponding to a Specific Activity of >1 x 10^8 IU/mg.
Endotoxin level Less than 1EU/mg of rHuG-CSF as determined by LAL method.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
Formulation Lyophilized from a 0.2mm filtered concentrated solution in 10mM sodium acetate buffer pH 4.0.
Form Lyophilized
Storage This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
Catalog no. (Mfr.) PR1034
Main SKU BHP11300345
Recombinant Protein

Scientific Background

Granulocyte colony-stimulating factor (G-CSF) is a pleiotropic cytokine best known for its specific effects on the proliferation, differentiation, and activation of hematopoietic cells of the neutrophilic granulocyte lineage. It is produced mainly by monocytes and macrophages upon activation by endotoxin, TNF-α and IFN-γ, and it plays a central role in regulating neutrophil production during steady-state granulopoiesis and in emergency responses to infection.

Product Description

Expression System: E. coli

Recombinant human G-CSF is expressed in Escherichia coli as a single non-glycosylated polypeptide chain containing 174 amino acids with an approximate molecular weight of 18.7 kDa. The protein is purified to >98% as determined by SDS-PAGE and HPLC analyses and is supplied as a sterile-filtered, white lyophilized powder.

Protein Specifications

Source Escherichia coli
Molecular Weight Approximately 18.7 kDa, a single non-glycosylated polypeptide chain containing 174 amino acids.
Amino Acid Sequence TPLGPASSLP QSFLLKCLEQ VRKIQGDGAA LQEKLCATYK LCHPEELVLL GHSLGIPWAP LSSCPSQALQ LAGCLSQLHS GLFLYQGLLQ ALEGISPELG PTLDTLQLDV ADFATTIWQQ MEELGMAPAL QPTQGAMPAF ASAFQRRAGG VLVASHLQSF LEVSYRVLRH LAQP
Purity >98% by SDS-PAGE and HPLC analyses.
Endotoxin Level Less than 1EU/mg of rHuG-CSF as determined by LAL method.
Formulation Lyophilized from a 0.2mm filtered concentrated solution in 10mM sodium acetate buffer pH 4.0.
Physical Appearance Sterile Filtered White lyophilized (freeze-dried) powder.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at <-20°C. Further dilutions should be made in appropriate buffered solutions.
Storage This lyophilized preparation is stable at 2-8°C, but should be kept at -20°C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8°C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20°C to -70°C. Avoid repeated freeze/thaw cycles.

Functional Activity

Fully biologically active when compared to standard. The ED50, as calculated by the dose-dependent proliferation of murine NFS-60 indicator cells (measured by 3H-thymidine uptake), is less than 0.1 ng/mL, corresponding to a specific activity of >1 × 108 IU/mg.

Safety & Handling

This product is for research use only (RUO) and is not intended for human or veterinary diagnostic or therapeutic use. Handle using standard laboratory safety practices.

Related Products

Explore additional recombinant cytokines and growth factors from Bioworld Technology Inc, or contact us for matched antibodies and ELISA kits for G-CSF research.

Q.Which expression system is used to produce this protein?
A.This recombinant human G-CSF is produced in Escherichia coli as a single non-glycosylated polypeptide chain, yielding a highly pure, tag-free protein suitable for functional studies.
Q.How is biological activity validated?
A.Activity is confirmed in a cell-based proliferation assay with an ED50 of <0.1 ng/mL (NFS-60 proliferation assay), indicating the protein is fully functional after lyophilization and reconstitution.
Q.How should I reconstitute and store this protein?
A.Briefly centrifuge the vial, then reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to 0.1-1.0 mg/mL. Store the lyophilized powder at -20°C (desiccated) for long-term storage; reconstituted protein is stable for up to one week at 2-8°C, or aliquot and store at -20°C.
Q.What is the endotoxin level?
A.Endotoxin is <1 EU/mg of protein as determined by the LAL method, which is suitable for sensitive cell-based applications.
Q.Is this product suitable for in vivo or clinical use?
A.No. This product is for research use only (RUO) and must not be used in humans or for diagnostic or therapeutic procedures.

Can't Find What You're Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.

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