GM-CSF Receptor alpha Protein, Human, Recombinant (His Tag)

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GM-CSF Receptor alpha Protein, Human, Recombinant (His Tag): Product Information

Purity
> 90 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
Measured in a cell proliferation assay using TF1 human erythroleukemic cells. The ED50 for this effect is 3-10 μg/mL in the presence of 0.4ng/mL GMCSF.
Protein Construction
A DNA sequence encoding the extracellular domain (Met 1-Gly 320) of human GM-CSFRα (P15509-1) was expressed with the C-terminal fused polyhistidine tag.
Accession#
Expressed Host
HEK293 Cells
Species
Human
Predicted N Terminal
Glu 23
Molecule Mass
The recombinant human GM-CSFRα consists of 309 amino acids and has a predicted molecular mass of 36 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh GM-CSFRα is approximately 60-65 kDa due to glycosylation.
Formulation
Lyophilized from sterile PBS, pH 7.4
1. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
2. Please contact us for any concerns or special requirements.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -70℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

GM-CSF Receptor alpha Protein, Human, Recombinant (His Tag): Images

GM-CSF Receptor alpha Protein, Human, Recombinant (His Tag): Alternative Names

CD116 Protein, Human; CDw116 Protein, Human; CSF2R Protein, Human; CSF2RAX Protein, Human; CSF2RAY Protein, Human; CSF2RX Protein, Human; CSF2RY Protein, Human; GM-CSF-R-alpha Protein, Human; GMCSFR Protein, Human; GMR Protein, Human; SMDP4 Protein, Human

GM-CSF Receptor alpha Background Information

CD116/GM-CSFR has been preferentially associated with M4, M5 subtype of AML but is not specific. The cluster of differentiation (cluster of designation) (often abbreviated as CD) is a protocol used for the identification and investigation of cell surface molecules present on white blood cells initially but found in almost any kind of cell of the body, providing targets for immunophenotyping of cells. Physiologically, CD molecules can act in numerous ways, often acting as receptors or ligands (the molecule that activates a receptor) important to the cell. A signal cascade is usually initiated, altering the behavior of the cell (see cell signaling). Some CD proteins do not play a role in cell signaling, but have other functions, such as cell adhesion. CD116/GM-CSFR is the alpha subunit of the heterodimeric receptor for colony stimulating factor 2, a cytokine which controls the production, differentiation, and function of granulocytes and macrophages. The encoded protein is a member of the cytokine family of receptors. CD116/GM-CSFR is found in the pseudoautosomal region (PAR) of the X and Y chromosomes.
Full Name
colony stimulating factor 2 receptor, alpha, low-affinity (granulocyte-macrophage)
References
  • Sjöblom C, et al. (2002) Granulocyte-macrophage colony-stimulating factor (GM-CSF) acts independently of the beta common subunit of the GM-CSF receptor to prevent inner cell mass apoptosis in human embryos. Biol Reprod. 67(6): 1817-23.
  • Goldstein JI, et al. (2011) Defective leukocyte GM-CSF receptor (CD116) expression and function in inflammatory bowel disease. Gastroenterology. 141(1): 208-16.
  • Saulle E, et al. (2009) Colocalization of the VEGF-R2 and the common IL-3/GM-CSF receptor beta chain to lipid rafts leads to enhanced p38 activation. Br J Haematol. 145(3): 399-411.
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