ELISA with Human G-CSF R/CD114?Protein 2932

Human G-CSF R/CD114 Protein 2932

$203.00 – $675.00

Summary

Expression: HEK293
Functional: Yes (ELISA)
Amino Acid Range: Glu25-His627

SKU: 2932parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	Q99062
express system	HEK293
product tag	C-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	The Granulocyte Colony-Stimulating Factor (G-CSF) receptor, a member of the hematopoietin cytokine receptor superfamily, functions as a homodimer and requires the recruitment of cytosolic protein tyrosine kinases (PTKs) to transduce its signal.
molecular weight	The protein has a predicted MW of 68.29 kDa. Due to glycosylation, the protein migrates to 90-110 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human G-CSF R/CD114 Protein 2932

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
The Granulocyte Colony-Stimulating Factor (G-CSF) receptor, a member of the hematopoietin cytokine receptor superfamily, functions as a homodimer and requires the recruitment of cytosolic protein tyrosine kinases (PTKs) to transduce its signal.
Protein names Granulocyte colony-stimulating factor receptor (G-CSF receptor) (G-CSF-R) (CD antigen CD114)
Gene names CSF3R,CSF3R GCSFR
Protein family Type I cytokine receptor family, Type 2 subfamily
Mass 92156Da
Function FUNCTION: Receptor for granulocyte colony-stimulating factor (CSF3), essential for granulocytic maturation. Plays a crucial role in the proliferation, differentiation and survival of cells along the neutrophilic lineage. In addition it may function in some adhesion or recognition events at the cell surface. {ECO:0000269\|PubMed:7514305}.
Subellular location SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: Cell membrane {ECO:0000269\|PubMed:24753537}; Single-pass type I membrane protein {ECO:0000255}.
Tissues TISSUE SPECIFICITY: One or several isoforms have been found in myelogenous leukemia cell line KG-1, leukemia U-937 cell line, in bone marrow cells, placenta, and peripheral blood granulocytes. Isoform GCSFR-2 is found only in leukemia U-937 cells. Isoform GCSFR-3 is highly expressed in placenta.
Structure SUBUNIT: Homodimer. The dimeric receptor binds two CSF3 molecules. Interacts with CEACAM1; down-regulates the CSF3R-STAT3 pathway through recruitment of PTPN6 that dephosphorylates CSF3R (By similarity). {ECO:0000250\|UniProtKB:P40223, ECO:0000269\|PubMed:16492764}.
Post-translational modification PTM: N-glycosylated. {ECO:0000269\|PubMed:24753537}.
Domain DOMAIN: The WSXWS motif appears to be necessary for proper protein folding and thereby efficient intracellular transport and cell-surface receptor binding. {ECO:0000269\|PubMed:1717255}.; DOMAIN: The box 1 motif is required for JAK interaction and/or activation. {ECO:0000269\|PubMed:1717255}.
Target Relevance information above includes information from UniProt accession: Q99062
The UniProt Consortium

Data

Immobilized Human G-CSF R, His Tag at 1µg/ml (100µl/Well) on the plate. Dose response curve for Human G-CSF, hFc Tag with the EC50 of 6.0ng/ml determined by ELISA.

The purity of Human G-CSF R is greater than 95% as determined by SEC-HPLC.

SDS-PAGE gel of Human G-CSF R/CD114~-Protein

Human G-CSF R on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.