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| Alternative Names | Human PDGF-BB protein、PDGF-BB |
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| Expression System | |
| Formulation | |
| Gene ID | |
| Molecular Weight | |
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| Purity | |
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| Target |
Background
PDGF-BB is supplied as a recombinant protein reagent for research use only. In RUO settings, recombinant proteins provide defined inputs for biochemical assays, interaction mapping, and assay development where control over protein identity and concentration supports reproducibility.
Also known as: Human PDGF-BB protein、PDGF-BB.
Species origin: Human.
Platelet derived growth factor (PDGF) is a potent mitogen and chemoattractant for mesenchymal and osteogenic cells and stimulates angiogenic molecules which play an essential role in bone regeneration. PDGF-BB is a member of PDGF family, which promotes cell proliferation, survival and migration, through binding to the tyrosine kinase
Endotoxin: <1 EU per μg of the protein by the LAL method
Biological significance and function
Functionally, PDGF-BB mediates intercellular communication in immune and stress-response settings through receptor engagement and downstream transcriptional programs. Experimental systems often use defined protein inputs to disentangle receptor proximal signaling from later transcriptional responses. This target is frequently investigated in research themes such as Oncology & Angiogenesis.
Molecular characteristics
Molecular characteristics: Protein domains, oligomeric state, and modification-sensitive surfaces can influence binding behavior and functional readouts in vitro. Where relevant, isoforms and PTMs may alter activity, stability, or interaction specificity.
- Source species: Human
- Molecular weight: 12.3 kDa
- Protein length: The recombinant Human PDGF-BB Protein consists of 109amino acids and predicts a molecular mass of 12.3 kDa.
- Expression region: Amino acid sequence derived from Human PDGF-BB (Ser82-Thr190) (P01127) was expressed.
- Purity: > 98 % as determined by SDS-PAGE
- Biological activity: Measured in a cell proliferation assay using BaIb/c 3T3. The ED50 for this effect is typically 2.588 ng/mL. The specific activity of recombinant Human PDGF-BB is approximately >3.86 x 105 IU/mg.
Post-translational considerations: E. coli expression typically yields a non-glycosylated recombinant form. This is often suitable for many intracellular enzymes and binding studies, while PTM-dependent targets may show differences when glycosylation or specific disulfide-bond patterns are required. For many extracellular signaling proteins and proteases, disulfide bonding and glycosylation can be important for stability and activity.
Expression and purification strategy
Expression system: E.coli. Expression system selection can influence folding state and PTM profile, which may affect binding or activity for PTM-sensitive targets.
Tagging: No tag tags are commonly used to streamline purification and enable capture/immobilization in interaction assays. Tag presence or removal can influence some binding measurements depending on assay design.
Formulation: Lyophilized from sterile PBS, pH 7.4.. Formulation and buffer composition can influence stability, aggregation propensity, and assay background in downstream biochemical experiments.
Research interpretation
Research interpretation: Cytokine-driven outcomes depend on receptor availability, timing, and crosstalk with stress and metabolic pathways. Defined protein inputs help disentangle receptor-proximal signaling from downstream transcriptional and phenotypic responses.