Analytical Data
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Gene name
PDGF BB
- Application
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Alternative Names
PDGF BB；PDGF2；SIS；Platelet-derived growth factor subunit B
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P01127
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Expression Region
82-190aa
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AA Sequence
M+SLGSLTIAEPAMIAECKTRTEVFEISRRLIDRTNANFLVWPPCVEVQRCSGCCNNRNVQCRPTQVQLRPVQVRKIEIVRKKPIFKKATVTLEDHLACKCETVAAARPV
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Molecular Weight
12.4 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
Platelet-Derived Growth Factor BB (PDGF-BB) is a crucial protein involved in regulating cellular processes such as proliferation, migration, and survival. It specifically binds to PDGF receptors on the surface of various cell types, playing a significant role in tissue repair, development, and angiogenesis. Research into PDGF-BB has gained traction due to its implications in various pathological conditions, including cancer, atherosclerosis, and fibrotic diseases. Overexpression or aberrant signaling of PDGF-BB can lead to uncontrolled cell growth and contribute to tumorigenesis. Therefore, scientists have focused on developing recombinant PDGF-BB proteins for therapeutic applications, particularly in wound healing and regenerative medicine. Recent studies have explored its efficacy in promoting the healing of chronic wounds and enhancing bone regeneration. By utilizing biotechnological methods to produce recombinant PDGF-BB, researchers aim to deliver this potent growth factor in a controlled manner, optimizing its biological activities while minimizing side effects. The ongoing investigation into PDGF-BB not only seeks to clarify its mechanistic role in various diseases but also to harness its therapeutic potential, making it a significant target for innovation in biomedical research and treatment strategies.
