Recombinant Human G-CSF Receptor/CD114 (carrier-free)

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Other Names
Colony Stimulating Factor 3 Receptor (CSF3R), Granulocyte Colony-Stimulating Factor Receptor (GCSFR), CD114, CD114 Antigen, G-CSF-R, SCN7
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Product Citations
publications
Human_GM-CSF_Receptor_CD114_CF_RECOM_1_012318
Human G-CSFR inhibits the proliferation of M-NFS-60 mouse myeloid cells induced by 0.4 ng/ml of human G-CSF.
  • Human_GM-CSF_Receptor_CD114_CF_RECOM_1_012318
    Human G-CSFR inhibits the proliferation of M-NFS-60 mouse myeloid cells induced by 0.4 ng/ml of human G-CSF.
  • Human_GM-CSF_Receptor_CD114_CF_RECOM_2_012318
    Stability testing for human G-CSFR. Human G-CSFR was aliquoted in PBS at 0.2 mg/ml and was treated as followed: one aliquot was kept at 4°C (control) and another was freeze-thawed four times (4 x freeze-thaws). After this procedure, the samples were tested for their ability to inhibit the proliferation of M-NFS-60 mouse myeloid cells induced by 0.4 ng/ml of human G-CSF.
Cat # Size Price Quantity Avail. Save
769902 10 µg $185
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769904 25 µg $375
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Description

Human G-CSF receptor (CSF3R) was initially isolated from the cDNA libraries of human U937 leukemia cells. The human G-CSF receptor is a type I cytokine receptor, possesses 836 amino acids, and has a clear homology (62.5%) with its murine counterpart. G-CSFR contains a conserved cytokine receptor homologous (CRH) domain, an Ig-like domain and three fibronectin type III-like domains in the extracellular region; a transmembrane region; and an intracellular region lacking intrinsic catalytic activity. Human G-CSF soluble receptor has been identified this form has a deletion of the transmembrane domain.  The complex G-CSF/G-CSFR has a 2:2 ligand:receptor stoichiometry. G-CSFR stimulates signals transduction proteins that induce granulocytic proliferation and differentiation such as the STAT 1, 3 and 5 transcription factors, the Ras/Mek/Erk1/2 pathway, the Src-related kinases Lyn and Hck, the serine/threonine kinase Akt, and the Syk tyrosine kinas. Also, G-CSFR is associated to pathways that negatively regulate granulopoiesis, including those mediated by the SHP-1 tyrosine phosphatase and the suppressor of cytokine signaling 3 (SOCS3) protein. Different mutations in the gene encoding the G-CSFR have been described with clinical consequences related to the myeloid lineage, including severe congenital neutropenia (SCN), myelodysplastic syndrome (MDS), acute myeloid leukemia (AML), and chronic neutrophilic leukemia (CNL).

Product Details
Technical data sheet

Product Details

Reactivity
Human
Source
Human G-CSFR, amino acids (Glu25-His627) (Accession # Q99062) was expressed in CHO cells. The carboxy terminus contains TGSR+hlgG-Fc+6His tag.
Molecular Mass
The 847 amino acid recombinant protein has a predicted molecular mass of approximately 94.7kD. The DTT-reduced and non-reduced protein migrate at approximately 115 kD and >200 kD respectively by SDS-PAGE. The predicted N-terminal amino acid is Glu.
Purity
>95% by SDS-PAGE gel as determined by Coomassie stained SDS-PAGE.
Formulation
0.22 µm filtered protein solution is in PBS pH7.2.
Endotoxin Level
Less than 0.1 EU per µg (0.01 ng/µg) cytokine as determined by the LAL method.
Concentration
10 and 25 µg sizes are bottled at 200 µg/mL.
Storage & Handling
Unopened vial can be stored between 2°C and 8°C for one month, at -20°C for six months, or at -70°C for one year. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C to -70°C. Stock solutions can also be prepared at 50 - 100 µg/mL in sterile buffer (PBS, HPBS, DPBS, or EBSS) containing carrier protein such as 0.2 - 1% BSA or HSA and stored in working aliquots at -20°C to -70°C. Avoid repeated freeze/thaw cycles.
Activity
Human G-CSFR inhibits the proliferation of M-NFS-60 mouse myeloid cells measured using Deep Blue Cell Viability™ Kit (Cat. No. 424701) and induced by 0.4 ng/ml of human G-CSF (Cat. No. 578602). The ED50 = 2 - 10 ng/ml.
Application

Bioassay

Application Notes

BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue-ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are validated in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at tech@biolegend.com.

Antigen Details

Structure
Cytokine receptor
Distribution

Neutrophils, hematopoietic progenitor cells, placenta neurons, adult neural stem cells, endothelial cells, and cardiomyocytes.

Function
Controls production, differentiation, and function of granulocytes. Integrin α9β1 augments receptor signaling and granulopoiesis in vivo.
Interaction
G-CSFR interacts with integrin α9β1.
Ligand Receptor
G-CSF
Bioactivity
G-CSFR inhibits the proliferation of M-NFS-60 cells.
Cell Type
Hematopoietic stem and progenitors, Embryonic Stem Cells
Biology Area
Stem Cells
Molecular Family
Soluble Receptors, Cytokine/Chemokine Receptors
Antigen References
  1. Fukunaga R, et al. 1990. PNAS USA. 87:8702.
  2. Larsen A, et al. 1990. J Exp Med. 172:1559-70.
  3. Tamada T, et al. 2006. PNAS USA. 103:3135.
  4. Chen C, et al. 2006. Immunity. 25:895.
  5. Panopoulos AD, Watowich SS. 2008. Cytokine. 42:277.
  6. Liongue C, Ward AC. 2014. Front Oncol. 4:93.
Gene ID
1441 View all products for this Gene ID
UniProt
View information about G-CSF on UniProt.org

Related FAQs

Does specific activity of a recombinant protein vary between lots?

Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.

Have your recombinants been tested for stability?

Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.

How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
Use formula Specific activity (Units/mg) = 10e6/ ED50 (ng/mL)
How does the activity of your recombinant proteins compare to competitors?

We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!

What is the specific activity or ED50 of my recombinant protein?

The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.

Go To Top Version: 0    Revision Date: 01/24/2018

For research use only. Not for diagnostic use. Not for resale. BioLegend will not be held responsible for patent infringement or other violations that may occur with the use of our products.

 

*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website, www.biolegend.com/ordering#license). BioLegend products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products, reverse engineer functionally similar materials, or to provide a service to third parties without written approval of BioLegend. By use of these products you accept the terms and conditions of all applicable Limited Use Label Licenses. Unless otherwise indicated, these products are for research use only and are not intended for human or animal diagnostic, therapeutic or commercial use.

 

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