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  • 产品名称：Platelet-DerivedGrowthFactorReceptor,betaPolypeptide(PDGFRB)(AA33-530)(Active)p

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  • 产品厂商：ACROBiosystems
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简单介绍：
Platelet-DerivedGrowthFactorReceptor,betaPolypeptide(PDGFRB)(AA33-530)(Active)protein(Histag)
详情介绍：
Characteristics This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 57 kDa. The protein migrates as 95-100 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Purity >95 % as determined by SDS-PAGE.
Sterility 0.22 μm filtered
Endotoxin Level Less than 1.0 EU per μg by the LAL method.
ProductDetails: Biological Activity Comment Biological Activity: Measured by its ability to inhibit the biological activity of PDGFBB using NR6R-3T3 mouse fibroblast cells. The ED50 for this effect is typically 3-8 μg/mL in the presence of 4 ng/mL rhPDGFBB.
Background 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.
Molecular Weight 57 kDa
NCBI Accession NP_002600
UniProt P09619
Pathways Fc-epsilon Receptor Signaling Pathway, EGFR Signaling Pathway, Neurotrophin Signaling Pathway, Inositol Metabolic Process, Glycosaminoglycan Metabolic Process, Smooth Muscle Cell Migration, Platelet-derived growth Factor Receptor Signaling
Restrictions For Research Use only
Format Lyophilized
Reconstitution Please see Certificate of Analysis for specific instructions. For best performance, we strongly recommend you to follow the reconstitution protocol provided in the CoA.
Buffer PBS, pH 7.4
Handling Advice Avoid repeated freeze-thaw cycles.
Storage -20 °C
Storage Comment No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C-8 °C), After reconstitution under sterile conditions for 1 month (4 °C-8 °C) or 3 months (-20 °C to -70 °C).
Supplier Images
SDS-PAGE (SDS) image for Platelet-Derived Growth Factor Receptor, beta Polypeptide (PDGFRB) (AA 33-530) (Active) protein (His tag) (ABIN2181629) Human PDGF R beta, His Tag on SDS-PAGE under reducing (R) condition. The gel was stai...
Background publications Morerio, Acquila, Rosanda, Rapella, Dufour, Locatelli, Maserati, Pasquali, Panarello: "HCMOGT-1 is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with t(5;17)(q33;p11.2)." in: Cancer research, Vol. 64, Issue 8, pp. 2649-51, 2004 (PubMed).

Chi, McPhee, Wagner, Dietz, Pantazis, Goustin: "Integration of proviral DNA into the PDGF beta-receptor gene in HTLV-I-infected T-cells results in a novel tyrosine kinase product with transforming activity." in: Oncogene, Vol. 15, Issue 9, pp. 1051-7, 1997 (PubMed).

Golub, Barker, Lovett, Gilliland: "Fusion of PDGF receptor beta to a novel ets-like gene, tel, in chronic myelomonocytic leukemia with t(5;12) chromosomal translocation." in: Cell, Vol. 77, Issue 2, pp. 307-16, 1994 (PubMed).