Recombinant Human Growth/differentiation factor 2(GDF2),partial

Code CSB-YP892325HU1
Size US$2010Purchase it in Cusabio online store
(only available for customers from the US)
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names GDF2
Uniprot No. Q9UK05
Research Area Cell Biology
Alternative Names GDF2; BMP9Growth/differentiation factor 2; GDF-2; Bone morphogenetic protein 9; BMP-9
Species Homo sapiens (Human)
Source Yeast
Expression Region 300-429aa
Target Protein Sequence HEEDTDGHVAAGSTLARRKRSAGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECKGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVGKACCVPTKLSPISVLYKDDMGVPTLKYHYEGMSVAECGCR
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 16.3kDa
Protein Length Partial
Tag Info N-terminal 6xHis-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

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 Q&A
Q:

Could you send a price to me for the following below. These will be used on the Biocore so if you can recommend a good purity version, that would be great.
500ug of Human BMP9

A:
Thanks for your inquiry. I checked with our protein center and recommend these products for you.
500ug of Human BMP9
CSB-YP892325HU Recombinant Human Growth/differentiation factor 2(GDF2)
Expression system: Yeast
Expression region: 300-429aa; Full Length
Tag information: N-terminal 6xHis-tagged
Target protein sequence:

HEEDTDGHVAAGSTLARRKRSAGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECKGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVGKACCVPTKLSPISVLYKDDMGVPTLKYHYEGMSVAECGCR


Lead time: .

Target Background

Function
(From Uniprot)
Potent circulating inhibitor of angiogenesis. Signals through the type I activin receptor ACVRL1 but not other Alks. Signaling through SMAD1 in endothelial cells requires TGF-beta coreceptor endoglin/ENG.
Gene References into Functions
  1. Case-control analyses reveal significant overrepresentation of rare variants in ATP13A3, AQP1 and SOX17, and provide independent validation of a critical role for GDF2 in heritable pulmonary arterial hypertension. PMID: 29650961
  2. Low BMP9 expression is associated with breast cancer. PMID: 30015950
  3. BMP-9 was found the most effective to induce osteogenic transdifferentiation of fat tissue in vitro PMID: 28054585
  4. Epigenetic Regulation of GDF2 Suppresses Anoikis in Ovarian and Breast Epithelia. PMID: 26678910
  5. BMP9 is highly expressed in bladder cancer cells. BMP9 promotes bladder cancer cell proliferation and migration through up-regulation of lncRNA UCA1. PMID: 29642505
  6. Bone morphogenetic protein 9 (BMP9) was identified as a target of miR-149 in MG63 cells, and BMP9 expression was negatively correlated with miR149 level in osteosarcoma clinical samples. miR-149 promotes osteosarcoma progression via targeting BMP9. PMID: 28956179
  7. The binding free energies indicate that ALK-3 preferably binds to BMP-2 instead of BMP-9. The structural analysis shows that ALK-3 binding with BMP-2 occurs in a perfectly symmetry pathway, whereas this symmetry is lost for possible ALK-3 interactions with BMP-9 PMID: 28869862
  8. The BMP9-induced phosphorylation of Smad1/5/8 was increased with the overexpression of RUNX3, and yet was decreased with the knockdown of RUNX3. Collectively, our findings suggest that RUNX3 is an essential modulator of the BMP9-induced osteoblast lineage differentiation of mesenchymal stem cells (MSCs). PMID: 29039519
  9. BMP9 is overexpressed in hepatic stellate cells in a cohort of liver fibrosis patients. PMID: 29223735
  10. our study indicates that BMP9 can inhibit the growth and metastasis of breast cancer cells, which may be related to interaction between pre-adipocytes/adipocytes and MDA-MB-231 cells via leptin signaling pathway. PMID: 28415788
  11. BMP9 interacts with a hydrophobic surface of the N-terminal orphan domain of ENG, which adopts a new duplicated fold generated by circular permutation. PMID: 28564608
  12. this is the first study that accurately identifies BMP9 as a profibrotic factor in fibroblasts. PMID: 27208502
  13. the combination of BMP-9 and MC-GAG stimulates chondrocytic and osteogenic differentiation of hMSCs. PMID: 27275929
  14. The results from this study demonstrate that the use of rhBMP9 significantly and markedly induced osteoblast differentiation when compared to rhBMP2 and PMID: 27699987
  15. The results demonstrate that although BMP9 alone does not influence leukocyte recruitment, it primes the vascular endothelium to mount a more intense response when challenged with LPS through an increase in TLR4, E-selectin, and VCAM-1 and ultimately through enhanced leukocyte recruitment. PMID: 27647829
  16. Data suggest BMP9/GDF2 and BMP10 synergize with TNFA to increase monocyte recruitment to vascular endothelial cells; process appears to be mediated mainly via ALK2/ACVR1 (which exhibits protein kinase activity). These studies used in vitro flow monocyte adhesion assay. (BMP9 = growth differentiation factor 2; BMP10 = bone morphogenetic protein 10; TNFA = tumor necrosis factor alpha; ALK2/ACVR1 = activin A receptor type 1) PMID: 28646109
  17. These results suggest that BMP9-transduced calvarial mesenchymal progenitor cells seeded in a PPCN-g thermoresponsive scaffold is capable of inducing bone formation in vivo and is an effective means of creating tissue engineered bone for critical sized defects. PMID: 28249039
  18. circulating levels significantly decreased in type 2 diabetes mellitus patients and associated with glucose homoeostasis and insulin sensitivity PMID: 27940998
  19. the data identify MxA as a novel stimulator of BMP4 and BMP9 transcriptional signaling, and suggest it to be a candidate IFN-alpha-inducible mechanism that might have a protective role against development of pulmonary arterial hypertension and other vascular diseases. PMID: 27875556
  20. BMP9 inhibited the proliferation and migration of the A549 cells. PMID: 27177272
  21. his study shows that BMP9 inhibition is associated with Osteosarcoma (OS) development and that enhanced expression of BMP9 may be a potential treatment method for OS PMID: 27706722
  22. IGF1 can enhance BMP9-induced osteogenic differentiation in mesenchymal stem cells. PMID: 26645636
  23. In ovarian and breast epithelial cells, epigenetic regulation of GDF2 suppresses anoikis. PMID: 26678910
  24. BMP9 also influenced the expression of PPARgamma. PMID: 26609524
  25. Data suggest ALK1 and ACVR2A/ACVR2B, acting as BMP9 co-receptors, rearrange pro-domains of BMP9--pro-domain dimer complex leading to displacement of pro-domains after receptor binding, release of mature non-dimer BPM9, and activation of signaling. PMID: 26677222
  26. DLL4/Notch1 and BMP9 interdependent signaling induces endothelial cell quiescence via P27KIP1/thrombospondin pathway. PMID: 26471266
  27. BMP9 Crosstalk with the Hippo Pathway Regulates Endothelial Cell Matricellular and Chemokine Responses PMID: 25909848
  28. BMP-9 induces vascular smooth muscle cell osteogenic differentiation and calcification via ALK1, Smad and ALP dependent mechanisms. PMID: 25297851
  29. This review summarizes the indirect connection between BMP9 and liver fibrosis, with a focus on the BMP9 signaling pathway members ALK1, endoglin, Id1, hepcidin and Snail. [review] PMID: 25393508
  30. Data show that bone morphogenetic protein 9 (BMP9) can inhibit the migration and invasion of MDA-MB-231 breast cancer cells and promote osteogenesis and proliferation of HS-5 bone marrow-derived mesenchymal stem cells in the co-culture system. PMID: 25209393
  31. structural analysis of the bone morphogenetic protein 9 procomplex PMID: 25751889
  32. These findings suggest that BMP9 can inhibit the proliferation and metastasis of SK-BR-3 cells via inactivating ERK1/2 and PI3K/AKT signaling pathways PMID: 24805814
  33. BMP9 is regulated by redox-dependent proteolysis PMID: 25237187
  34. in primary, non-malignant cells BMP-9 stabilizes the epithelial phenotype and inhibits proliferation, in hepatocellular carcinoma cells it induces cell growth and the acquisition of a migratory phenotype. PMID: 24670474
  35. these observations indicate that BMP9 is an important mediator of breast cancer bone metastasis and a potential therapeutic target for treating this deadly disease. PMID: 24413988
  36. BMP9 can regulate tumor growth of osteosarcoma cells through the Wnt/beta-catenin pathway. PMID: 24337584
  37. results strongly suggest that Creld2 may be directly regulated by BMP9 and ER stress response may play an important role in regulating osteogenic differentiation PMID: 24019898
  38. the cross-talk between EGF and BMP9 signalling pathways in mesenchymal stem cells may underline their important roles in regulating osteogenic differentiation. PMID: 23844832
  39. ResultS suggest that BMP9 may inhibit the migration and invasiveness of Osteosarcoma cells through a Smad-dependent pathway by downregulating the expression and activity of MMP9. PMID: 23807047
  40. BMP9 signaling may be relevant during hepatocarcinogenesis in vivo. PMID: 23936038
  41. We demonstrate a cross-talk between BMPs and CRYAB and a major effect of this regulatory interaction on resistance to apoptosis. PMID: 24072698
  42. Mutations in BMP9 (also known as GDF2) were identified in three probands with hereditary hemorrhagic telangiectasia. PMID: 23972370
  43. BMP-9 was able to induce the phosphorylation of Smad-1/5/8 and ERK 1/2 proteins, but did not induce p38 phosphorylation. PMID: 23313128
  44. the enhanced expression of BMP-9 in osteosarcoma cells by adBMP-9 exerted inhibitory effects on growth and migration of osteosarcoma cells possibly via blockade of the PI3K/AKT signaling pathway. PMID: 22948234
  45. BMP9 regulates the SDF1/CXCR4 axis in endothelial cells. BMP9 signaling via endoglin switches cells from an SDF1-responsive autocrine state to an SDF1-nonresponsive paracrine state repressing endothelial cell migration & promoting vessel maturation. PMID: 23018639
  46. SNPs in the BMP9 gene appear to contribute to the risk of OPLL in association with certain clinical and demographic characteristics. PMID: 22829878
  47. platelets regulate blood/lymphatic vessel separation by inhibiting the proliferation, migration, and tube formation of LECs, mainly because of the release of BMP-9 upon activation by CLEC-2/podoplanin in PMID: 22556408
  48. data suggest that both the VEGF/VEGF receptor and the BMP9/ALK1 pathways are essential for stimulating angiogenesis, and targeting both pathways simultaneously may be an attractive strategy to overcome resistance to antiangiogenesis therapy PMID: 22493445
  49. Mutual regulation by BMP-9 and CV2 is essential in regulating the development of the vascular endothelium. PMID: 22474252
  50. Increased ET-1 production by endothelial cells as a consequence of BMPR II dysfunction may be clinically relevant in the pathogenesis of pulmonary arterial hypertension. PMID: 22299030

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Involvement in disease Telangiectasia, hereditary hemorrhagic, 5 (HHT5)
Subcellular Location Secreted
Protein Families TGF-beta family
Tissue Specificity Detected in blood plasma (at protein level).
Database Links

HGNC: 4217

OMIM: 605120

KEGG: hsa:2658

STRING: 9606.ENSP00000249598

UniGene: Hs.279463

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