Recombinant Human CSF1R Protein

Name: Recombinant Human CSF1R Protein
Brand: Beta LifeScience
SKU: BLPSN-1443
Availability: InStock

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Colony-stimulating factors and receptors (csfs), Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Accession	NP_005202.2
Synonym	C-FMS, CD115, CSF-1R, CSFR, FIM2, FMS, HDLS, M-CSF-R, MCSF Receptor
Background	M-CSFR encoded by the proto-oncogene c-fms is the receptor for colony stimulating factor 1 (CSF1R), a cytokine involved in the proliferation, differentiation, and activation of macrophages. This cell surface glycoprotein is consisted by an extracellular ligand-binding domain, a single membrane-spanning segment, and an intracellular tyrosine kinase domain. Binding of CSF1 activates the receptor kinase, leading to "autophosphorylation" of receptor subunits and the concomitant phosphorylation of a series of cellular proteins on tyrosine residues. CSF1R is a tyrosine kinase receptor that is absolutely required for macrophage differentiation and thus occupies a central role in hematopoiesis. CSF1 and its receptor (CSF1R, product of c-fms proto-oncogene) were initially implicated as essential for normal monocyte development as well as for trophoblastic implantation. This apparent role for CSF1/CSF1R in normal mammary gland development is very intriguing because this receptor/ligand pair has also been found to be important in the biology of breast cancer in which abnormal expression of CSF1 and its receptor correlates with tumor cell invasiveness and adverse clinical prognosis. Tumor cell expression of CSF1R is under the control of several steroid hormones (glucocorticoids and progestins) and the binding of several bHLH transcription factors, while tumor cell expression of CSF-1 appears to be regulated by other hormones, some of which are involved in normal lactogenic differentiation. However, studies have demonstrated that CSF1 and CSF1R have additional roles in mammary gland development during pregnancy and lactation. The role of CSF1 and CSF1R in normal and neoplastic mammary development that may elucidate potential relationships of growth factor-induced biological changes in the breast during pregnancy and tumor progression.
Description	The mature form of human M-CSFR (NP_005202.2) extracellular domain (Met 1-Glu 512) with quinary-aa peptide (DDDDK) at the C-terminus was expressed and purified.
Source	HEK293
Predicted N Terminal	Ile 20
AA Sequence	Met 1-Glu 512
Molecular Weight	The recombinant mature human M-CSF R comprises 499 a.a. with a calculated molecular mass of 55.1 kDa. Due to glycosylation, the apparent molecular mass of rhM-CSFR is approximately 80-90 kDa in SDS-PAGE under reducing conditions.
Purity	>90% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	1. Immobilized sMCSFR at 10 ug/ml (100 ul/well) can bind biotinylated human CSF1-His, The EC50 of biotinylated human CSF1-His is 32-74.8 ng/ml.2. Measured by its ability to inhibit the human CSF-induced proliferation of M-NFS-60 mouse myelogenous leukemia lymphoblast cells. The ED50 for this effect is typically 0.3-1.5 ug/mL in the presence of 3 ng/mL of rhM-CSF.
Formulation	Lyophilized from sterile 100mM Glycine, 10mM NaCl, 50mM Tris, pH 7.5.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.