GDF2 Protein (AA 319-428)
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- Target See all GDF2 Proteins
- GDF2 (Growth Differentiation Factor 2 (GDF2))
- Protein Type
- Recombinant
- Biological Activity
- Active
- Protein Characteristics
- AA 319-428
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Origin
- Mouse
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Source
- CHO Cells
- Application
- Flow Cytometry (FACS)
- Purity
- > 95 % , as determined by Coomassie stained SDS-PAGE.
- Sterility
- 0.22 μm filtered
- Endotoxin Level
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Less than 0.01 ng per μg of cyokine as determine by the LAL method
- Top Product
- Discover our top product GDF2 Protein
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- Application Notes
- Optimal working dilution should be determined by the investigator.
- Comment
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Biological activity: ED50 = 0.5 - 3 ng/ml, corresponding to a specific activity of 0.33 - 2.0 x 106 units/mg, as determined by induction of alkaline phosphatase in ATDC5 cells in a dose dependent manner.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Reconstitution
- For maximum results, quick spin vial prior to opening. Stock solutions should be prepared at no less than 10 μg/mL in sterile buffer (PBS, HPBS, DPBS, and EBSS) containing carrier protein such as 1 % BSA or HSA. After dilution, the cytokine can be stored between 2 °C and 8 °C for one month or from -20 °C to -70 °C for up to 3 months.
- Buffer
- 0.22 μm filtered protein solution is in 0.1 % TFA, <30 % ACN.
- Handling Advice
- Avoid repeated freeze/thaw cycles.
- Storage
- -20 °C
- Storage Comment
- Unopened vial can be stored between 2°C and 8°C for three months, at -20°C for six months, or at -70°C for one year.
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- Target
- GDF2 (Growth Differentiation Factor 2 (GDF2))
- Alternative Name
- BMP-9 (GDF2 Products)
- Synonyms
- bmp9 Protein, BMP-9 Protein, BMP9 Protein, Bmp9 Protein, DSL1 Protein, growth differentiation factor 2 Protein, gdf2 Protein, GDF2 Protein, Gdf2 Protein
- Background
- BMP-9 was initially isolated from fetal mouse liver cDNA libraries. The mouse and human proteins share 84 % identity. They are part of the bone morphogenetic protein (BMP) family of proteins, which are members of the TGF-β superfamily and play a key role in skeletal development, bone formation, and stem cell differentiation. BMP-9 is one of the most osteogenic factors of the family. It is synthetized by hepatocytes and intrahepatic biliary epithelial cells. It circulates in plasma in an unprocessed, inactive form, that can be further activated by furin as well as a mature and fully active complex form bound to its prodomain. BMPs signal through heterotetrameric complex receptors, which include four type I receptors (ALK-1, ALK-2, ALK-3, and ALK-6) and three type II receptors (BMPRII, ActRIIA, and ActRIIB). BMP-9 and BMP-10 bind to ALK-1 (mainly expressed in endothelial cells). BMP-9 inhibits the proliferation of endothelial cells induced by basic FGF and VEGF-stimulated angiogenesis by binding to ALK-1. BMP-9 also binds to ALK-2 in primary myeloma cells, and this binding can be inhibited by membrane-bound or soluble endoglin (an accessory receptor for the TGF-β family). BMP-9 activity is inhibited by crossveinless-2 (CV2), a member of the chordin family and an extracellular regulator. BMP-9 induces CV2 expression in endothelial cells and in a negative feedback loop inhibits its own activity by the binding of CV2 to BMP-9, which consequently inhibits its binding to ALK-1. BMP-9 and -10 possess tumor suppressing activity in breast and prostate cancer, BMP-9 also induces apoptosis in primary myeloma cells. In contrast, autocrine BMP-9 signaling induces proliferation of ovarian and liver cancer cells.
- Molecular Weight
- The 110 amino acid recombinant protein has a predicted molecular mass of approximately 12 kDa. The DTT-reduced and non-reduced protein migrate at approximately 14 kDa and 24 kDa respectively by SDS-PAGE. The predicted N-terminal amino acid is Ser.
- Pathways
- Transition Metal Ion Homeostasis
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