Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | CAA49634 |
express system | HEK293 |
product tag | C-His |
purity | > 95% as determined by Tris-Bis PAGE |
background | Macrophage-stimulating protein (MSP) is a serum protein belonging to the plasminogen-related growth factor family. The specific receptor for MSP is the RON (recepteur d'origine nantais) receptor tyrosine kinase – a member of the MET proto-oncogene family. Activation of RON by MSP exerts dual functions on macrophages. |
molecular weight | The protein has a predicted MW of 59.71 kDa. Due to furin cleavage, the protein migrates to 70-80 kDa (full length) and 40-50 kDa (alpha chain) and 35-40 kDa (partial beta chain) based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human MSPR/Ron Protein 2523
$315.00 – $1,050.00
Summary
- Expression: HEK293
- Pure: Yes (SDS-PAGE)
- Amino Acid Range: Glu25-Leu571
Human MSPR/Ron Protein 2523
protein |
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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 |
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Macrophage-stimulating protein (MSP) is a serum protein belonging to the plasminogen-related growth factor family. The specific receptor for MSP is the RON (recepteur d'origine nantais) receptor tyrosine kinase - a member of the MET proto-oncogene family. Activation of RON by MSP exerts dual functions on macrophages. |
Protein names Macrophage-stimulating protein receptor (MSP receptor) (EC 2.7.10.1) (CDw136) (Protein-tyrosine kinase 8) (p185-Ron) (CD antigen CD136) [Cleaved into: Macrophage-stimulating protein receptor alpha chain; Macrophage-stimulating protein receptor beta chain] |
Protein family Protein kinase superfamily, Tyr protein kinase family |
Mass 152241Da |
Function Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to MST1 ligand. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces autophosphorylation of RON on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with the PI3-kinase subunit PIK3R1, PLCG1 or the adapter GAB1. Recruitment of these downstream effectors by RON leads to the activation of several signaling cascades including the RAS-ERK, PI3 kinase-AKT, or PLCgamma-PKC. RON signaling activates the wound healing response by promoting epithelial cell migration, proliferation as well as survival at the wound site. Also plays a role in the innate immune response by regulating the migration and phagocytic activity of macrophages. Alternatively, RON can also promote signals such as cell migration and proliferation in response to growth factors other than MST1 ligand. {ECO:0000269|PubMed:18836480, ECO:0000269|PubMed:7939629, ECO:0000269|PubMed:9764835}. |
Catalytic activity CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10028}; |
Subellular location Membrane; Single-pass type I membrane protein. |
Tissues Expressed in colon, skin, lung and bone marrow. {ECO:0000269|PubMed:8062829}. |
Structure Heterodimer of an alpha chain and a beta chain which are disulfide linked. Binds PLXNB1. Associates with and is negatively regulated by HYAL2. Interacts when phosphorylated with downstream effectors including PIK3R1, PCLG1, GRB2 and GAB1. Interacts with integrin beta1/ITGB1 in a ligand-independent fashion. {ECO:0000269|PubMed:10222149, ECO:0000269|PubMed:10514476, ECO:0000269|PubMed:12676986, ECO:0000269|PubMed:15184888, ECO:0000269|PubMed:20726546, ECO:0000269|PubMed:21784853, ECO:0000269|PubMed:7687741}. |
Post-translational modification Proteolytic processing yields the two subunits.; Autophosphorylated in response to ligand binding on Tyr-1238 and Tyr-1239 in the kinase domain leading to further phosphorylation of Tyr-1353 and Tyr-1360 in the C-terminal multifunctional docking site. {ECO:0000269|PubMed:15632155, ECO:0000269|PubMed:20726546}.; Ubiquitinated. Ubiquitination by CBL regulates the receptor stability and activity through proteasomal degradation. {ECO:0000269|PubMed:12802274}.; O-mannosylation of IPT/TIG domains on Thr or Ser residues by TMEM260 is required for protein maturation (PubMed:37186866). O-mannosylated residues are composed of single mannose glycans that are not elongated or modified (PubMed:37186866). {ECO:0000269|PubMed:37186866}. |
Target Relevance information above includes information from UniProt accession: Q04912 |
The UniProt Consortium |
Publications
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