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Recombinant Human PDGFRB, Fc-tagged

Cat.No.: PDGFRB-184H
Product Overview: Recombinant Human PDGFRb /CD140b Protein, With C-Fc Tag (rh PDGFRB Fc Chimera) Leu 33 - Phe 530 (Accession # NP_002600) was produced in human 293 cells (HEK293).
Description: Human platelet-derived growth factor receptor, beta polypeptide (PDGFRB) is also called J03278, M21616, CD140B, JTK12, PDGF-R-beta and PDGFR, is receptor that binds specifically to PDGFB and has a tyrosine-protein kinase activity. Is a cell surface tyrosine kinase receptor for members of the platelet-derived growth factor (PDGF) family. The PDGFR/PDGF system includes two receptors (PDGFRA and PDGFRB) and four ligands (A, B, C and D). The receptors PDGFRA and PDGFRB are related in sequence and both are members of the class III subtype of receptor tyrosine kinases (RTKs). Other class III RTKs are CSF1R, KIT and FLT3. PDGF binding induces receptor homo- and heterodimerization and signal transduction. The expression of the α and β receptors is independently regulated in various cell types. Recombinant soluble PDGFRB binds PDGF with high affinity and is potent PDGF antagonist. The ligands form either homo- or heterodimers (PDGF-AA, -AB, -BB, -CC, -DD). The four PDGFs are inactive in their monomeric forms. The PDGFs bind to the protein tyrosine kinase receptors PDGF receptor-α and -β. These two receptor isoforms dimerize upon binding the PDGF dimer, leading to three possible receptor combinations, namely -αα, -ββ and -αβ. PDGF-CC specifically interacts with PDGFR-αα and -αβ, but not with –ββ, and thereby resembles PDGF-AB. PDGF-DD binds to PDGFR-ββ with high affinity, and to PDGFR-αβ to a much lower extent and is regarded as PDGFR-ββ specific. PDGF-AA binds only to PDGFR-αα, while PDGF-BB is the only PDGF that can bind all three receptor combinations with high affinity.
Source: HEK293
Species: Human
Tag: Fc
Form: Lyophilized from 0.22 μm filtered solution in 50 mM tris, 100 mM glycine, pH7.5. Normally Mannitol or Trehalose are added as protectants before lyophilization.
Molecular Mass: rh PDGFRB Fc Chimera is fused with a human IgG1 Fc tag at the C-terminus, and has a calculated MW of 82.8 kDa. The predicted N-terminus is Leu 33. DTT-reduced Protein migrates as 120-140 kDa in SDS-PAGE due to glycosylation.
Endotoxin: Less than 1.0 EU per μg of the rh PDGFRB Fc Chimera by the LAL method.
Purity: >95% as determined by SDS-PAGE.
Storage: Avoid repeated freeze-thaw cycles.No activity loss was observed after storage at:In lyophilized state for 1 year (4oC); After reconstitution under sterile conditions for 3 months (-70oC).
Reconstitution: See Certificate of Analysis for reconstitution instructions and specific concentrations.
Gene Name: PDGFRB platelet-derived growth factor receptor, beta polypeptide [ Homo sapiens ]
Official Symbol: PDGFRB
Synonyms: PDGFRB; platelet-derived growth factor receptor, beta polypeptide; PDGFR; platelet-derived growth factor receptor beta; CD140b; JTK12; PDGFR1; PDGFR-beta; PDGF-R-beta; CD140 antigen-like family member B; platelet-derived growth factor receptor 1; beta-type platelet-derived growth factor receptor; CD140B; PDGFR-1;
Gene ID: 5159
mRNA Refseq: NM_002609
Protein Refseq: NP_002600
MIM: 173410
UniProt ID: P09619
Chromosome Location: 5q33.1
Pathway: Calcium signaling pathway, organism-specific biosystem; Calcium signaling pathway, conserved biosystem; Cytokine-cytokine receptor interaction, organism-specific biosystem; Cytokine-cytokine receptor interaction, conserved biosystem; Downstream signal transduction, organism-specific biosystem; Focal Adhesion, organism-specific biosystem; Focal adhesion, organism-specific biosystem;
Function: ATP binding; nucleotide binding; platelet activating factor receptor activity; platelet-derived growth factor beta-receptor activity; platelet-derived growth factor beta-receptor activity; platelet-derived growth factor binding; platelet-derived growth factor binding; platelet-derived growth factor receptor binding; platelet-derived growth factor-activated receptor activity; protein binding; protein tyrosine kinase activity; protein tyrosine kinase activity; receptor activity; receptor binding; signal transducer activity; vascular endothelial growth factor binding;

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