Recombinant Human G-CSFR/CD114 Protein

Product Discontinued

Recombinant Human G-CSFR/CD114 Protein Summary

• Description: A biologically active protein to CSF3R.
• Specificity: G-CSF R - Fc HEX Chimera contains N-linked oligosaccharides and may contain O-linked oligosaccharides. Under reducing conditions G-CSF R - Fc HEX Chimera migrates as a broad band between 100 and 130 kDa in SDS-PAGE due to post-translation modifications, in particular glycosylation. This compares with unmodified TRAIL R1 - Fc Chimera that has a predicted monomeric molecular mass of 93.9 kDa.
• Preparation Method: A DNA sequence encoding the signal peptide and extracellular domain of human G-CSF R (aa 1-621) was fused to the Fc region of human IgG1 (aa 90-330). The chimeric protein was expressed in modified human 293 cells.
• Details of Functionality: The ED50 of G-CSF R - Fc HEX Chimera is typically 2-3 ng/ml as measured by its ability to
  neutralize G-CSF mediated proliferation of the murine myeloblastic m-NFS-60 cell line.
• Protein/Peptide Type: Biologically Active Protein
• Gene: CSF3R

Applications/Dilutions

• Dilutions:
  • Block/Neutralize
  • Functional
  • Western Blot
• Application Notes: This protein is functionally active and can be used for Blocking and Neutralizing. It can also be used for Western Blot. The unmodified G-CSF R - Fc Chimera has a predicted pI of 6.6.

Reactivity Notes

This is a Human protein

Packaging, Storage & Formulations

• Storage: Store at -80C. Avoid freeze-thaw cycles.
• Concentration: LYOPH
• Reconstitution Instructions: Reconstitute with 0.5 ml sterilized PBS containing 1% human serum albumin and 10% trehalose.

Alternate Names for Recombinant Human G-CSFR/CD114 Protein

• CD114 antigen
• CD114
• colony stimulating factor 3 receptor (granulocyte)
• CSF3R
• Csfgr
• G-CSF R
• G-CSF receptor
• GCSFR
• G-CSFR
• GCSFRG-CSF-R
• granulocyte colony-stimulating factor receptor

Background

G-CSF R, also known as granulocyte colony-stimulating factor receptor and CD114 antigen, is a member of the cytokine receptor superfamily. Members of this family, which also includes the receptors for IL-2 to IL-7, GM-CSF, EPO, TPO and GH, are characterised by the presence of four conserved cysteine residues in their extracellular domains. The G CSF R extracellular domain has a composite structure containing an Ig-like domain, a cytokine receptor homologous region and fibronectin type III domains. The human G-CSF R mediates the biological activity of G-CSF which is unique in its ability to not only stimulate the proliferation but also potently induces the terminal maturation of myeloid progenitor cells to neutrophilic granulocytes. G-CSF R is produced as an ECD-Fc fusion protein with the aim of enhancing its activity. ECD-Fc fusion proteins have an advantage over soluble receptors because many receptors are only functional in dimeric form. Fusion to the Fc domain of IgG1 induces dimerization due to the ability of the Fc domain to form disulfide bonds. The resulting dimeric receptor ECD-Fc mimics the activated form of the receptor and possess enhanced affinity for its cognate ligand relative to its monomeric form. This is a HCX protein. HCX Expression System Details HCX proteins mimic the proteins in the human body because they are expressed from human, rather than animal, insect or bacterial cells. This process gives them human post-translational modifications. Recombinant DNA techniques allow a human protein with the correct amino acid sequence to be expressed in a non-human cell line. However, non-human cells lack the appropriate cellular machinery, such as specific glycosyltransferases, necessary to produce the correct human post-translational modifications of a protein. An extreme example is seen in E. coli cells, which produce recombinant proteins with no glycosylation, as the above figure illustrates. Rodent and yeast cells are able to glycosylate proteins, but they are still different from glycosylation in human cells. Expression System Resultant Proteins Human (e.g. K562, HEK293) Correct amino acid sequence Human post-translational modifications Rodent (e.g. CHO, NSO) Correct amino acid sequence Some natural glycosylation - not human-like Yeast (e.g. Pichia) Correct amino acid sequence Some natural glycosylation - not human-like E.Coli Correct amino acid sequence No PTMs Although there have been significant attempts to make non-human cell derived cytokines more human-like, there is a growing awareness that in many instances, particularly in therapeutics, cytokines should mimic those found in the body as closely as possible. Purified G-CSF R - Fc HEX Chimera consists of 5-30% carbohydrate by weight.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 1 year from date of receipt.

Bioinformatics

• Gene Symbol: CSF3R