PDGF-BB Protein, Human

PDGF-BB Protein, Human is the most active PDGF isoform, binds to PDGF receptor, promotes diverse cell types proliferation and osteogenesis, and further stimulates bone formation in fracture or defect. PDGF-BB Protein, Human improves collagenase-induced Achilles tendinopathy in rats.

Recombinant Human Platelet-derived Growth Factor-BB is the most active PDGF isoform, binds to PDGF receptor, promotes diverse cell types proliferation and osteogenesis, and further stimulates bone formation in fracture or defect. Platelet-derived growth factor-BB (PDGF-BB) is primarily secreted from platelet α-granules and is the most active PDGF isoform in bone and other connective tissue as it can bind to all known PDGF receptors. PDGF-BB plays an important role in bone regeneration by inducing mitogenesis, chemotaxis, extracellular matrix formation, and vascularization^[1]. Recombinant Human Platelet-derived Growth Factor-BB (rhPDGF-BB) accelerates tendon healing by improving matrix remodeling, increased collagen synthesis, and increased cell proliferation. Recombinant Human Platelet-derived Growth Factor-BB is also efficacious in a non-ruptured, degenerated, tendinopathy model. Furthermore, Recombinant Human Platelet-derived Growth Factor-BB addresses chronic tendinopathies by inducing proliferation and migration of progenitor cells and tenocytes, which stimulate structural repair of the degenerated tendon^[2].

PDGF-BB Protein, Human (7.5 ng/mL-7.5 µg/mL) significantly enhances the proliferation of human foreskin fibroblasts^[4].
PDGF-BB Protein, Human (10 ng/mL; 0-24 h) promotes the migration of rat bone marrow mesenchymal stem cells (rBM MSC)^[5].
PDGF-BB Protein, Human (50 ng/mL; 2-4 h) upregulates the gene expression of CCL2 and CCL7 in mouse 10T1/2 cells^[6].

PDGF-BB Protein, Human (3-10 μg; intra-tendon injection) improves maximum load-to-rupture and stiffness in a rat Achilles tendinopathy model induced by collagenase^[2].
PDGF-BB Protein, Human (3 mg/wound; topical application; once daily; 10 d) does not accelerate wound closure, re-epithelialization, or collagen deposition in a splinted full-thickness skin wound model in db/db diabetic mice^[4].

The ED₅₀ is ≤11 ng/mL as measured by murine Balb/c 3T3 cells.

• 
  Measured in a cell proliferation assay using Balb/c 3T3 cells. The ED₅₀ for this effect is 1.81 ng/mL, corresponding to a specific activity is 5.54×10⁵ units/mg.

Human

E. coli

Tag Free

P01127-1 (S82-T190)

5155  [NCBI]

Full Length of PDGFB

SLGSLTIAEPAMIAECKTRTEVFEISRRLIDRTNANFLVWPPCVEVQRCSGCCNNRNVQCRPTQVQLRPVQVRKIEIVRKKPIFKKATVTLEDHLACKCETVAAARPVT

Approximately 14 kDa, based on SDS-PAGE under reducing conditions.

• 
  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder

1.Lyophilized from a 0.22 μm filtered solution of 20 mM NaAC-HAC, 4% mannitol, pH 4.5.
2.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.
3.Lyophilized from a 0.22 μm filtered solution of 50 mM Tris-HCl, 200 mM NaCl, 500 mM arginine, pH 8.0.
Please refer to the lot-specific COA for specific buffer information.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. Sun H, et al. Recombinant human platelet-derived growth factor-BB versus autologous bone graft in foot and ankle fusion: A systematic review and meta-analysis. Foot Ankle Surg. 2017 Mar;23(1):32-39.  [Content Brief]

  [2]. Solchaga LA, et al. Comparison of the effect of intra-tendon applications of recombinant human platelet-derived growth factor-BB, platelet-rich plasma, steroids in a rat achilles tendon collagenase model. J Orthop Res. 2014 Jan;32(1):145-50.  [Content Brief]

  [3]. Chen L, et al. Inhibition of PDGF-BB reduces alkali-induced corneal neovascularization in mice. Mol Med Rep. 2021 Apr;23(4):238.  [Content Brief]

  [4]. Park SA, et al. PDGF-BB does not accelerate healing in diabetic mice with splinted skin wounds. PLoS One. 2014 Aug 14;9(8):e104447.  [Content Brief]

  [5]. Chung R, et al. Potential roles of growth factor PDGF-BB in the bony repair of injured growth plate. Bone. 2009 May;44(5):878-85.  [Content Brief]

  [6]. Au P, et al. Paradoxical effects of PDGF-BB overexpression in endothelial cells on engineered blood vessels in vivo. Am J Pathol. 2009 Jul;175(1):294-302.  [Content Brief]

  [7]. Cao H, et al. PDGF-BB prevents destructive repair and promotes reparative osteogenesis of steroid-associated osteonecrosis of the femoral head in rabbits. Bone. 2023 Feb;167:116645.  [Content Brief]