Recombinant Human Growth/Differentiation Factor 2 (GDF2) Protein (His)

Name: Recombinant Human Growth/Differentiation Factor 2 (GDF2) Protein (His)
Brand: Beta LifeScience
SKU: BLC-04506P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality cytokines for advanced research, High-quality recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Growth/Differentiation Factor 2 (GDF2) Protein (His) is produced by our Yeast expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9UK05
Target Symbol	GDF2
Synonyms	GDF2; BMP9Growth/differentiation factor 2; GDF-2; Bone morphogenetic protein 9; BMP-9
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	HEEDTDGHVAAGSTLARRKRSAGAGSHCQKTSLRVNFEDIGWDSWIIAPKEYEAYECKGGCFFPLADDVTPTKHAIVQTLVHLKFPTKVGKACCVPTKLSPISVLYKDDMGVPTLKYHYEGMSVAECGCR
Expression Range	300-429aa
Protein Length	Partial
Mol. Weight	16.3kDa
Research Area	Cell Biology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	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.
Subcellular Location	Secreted.
Protein Families	TGF-beta family
Database References	HGNC: 4217 OMIM: 605120 KEGG: hsa:2658 STRING: 9606.ENSP00000249598 UniGene: PMID: 29650961 Low BMP9 expression is associated with breast cancer. PMID: 30015950 BMP-9 was found the most effective to induce osteogenic transdifferentiation of fat tissue in vitro PMID: 28054585 Epigenetic Regulation of GDF2 Suppresses Anoikis in Ovarian and Breast Epithelia. PMID: 26678910 BMP9 is highly expressed in bladder cancer cells. BMP9 promotes bladder cancer cell proliferation and migration through up-regulation of lncRNA UCA1. PMID: 29642505 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 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 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 BMP9 is overexpressed in hepatic stellate cells in a cohort of liver fibrosis patients. PMID: 29223735 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 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 this is the first study that accurately identifies BMP9 as a profibrotic factor in fibroblasts. PMID: 27208502 the combination of BMP-9 and MC-GAG stimulates chondrocytic and osteogenic differentiation of hMSCs. PMID: 27275929 The results from this study demonstrate that the use of rhBMP9 significantly and markedly induced osteoblast differentiation when compared to rhBMP2 and PMID: 27699987 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 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 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 circulating levels significantly decreased in type 2 diabetes mellitus patients and associated with glucose homoeostasis and insulin sensitivity PMID: 27940998 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 BMP9 inhibited the proliferation and migration of the A549 cells. PMID: 27177272 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 IGF1 can enhance BMP9-induced osteogenic differentiation in mesenchymal stem cells. PMID: 26645636 In ovarian and breast epithelial cells, epigenetic regulation of GDF2 suppresses anoikis. PMID: 26678910 BMP9 also influenced the expression of PPARgamma. PMID: 26609524 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 DLL4/Notch1 and BMP9 interdependent signaling induces endothelial cell quiescence via P27KIP1/thrombospondin pathway. PMID: 26471266 BMP9 Crosstalk with the Hippo Pathway Regulates Endothelial Cell Matricellular and Chemokine Responses PMID: 25909848 BMP-9 induces vascular smooth muscle cell osteogenic differentiation and calcification via ALK1, Smad and ALP dependent mechanisms. PMID: 25297851 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 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 structural analysis of the bone morphogenetic protein 9 procomplex PMID: 25751889 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 BMP9 is regulated by redox-dependent proteolysis PMID: 25237187 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 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 BMP9 can regulate tumor growth of osteosarcoma cells through the Wnt/beta-catenin pathway. PMID: 24337584 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 the cross-talk between EGF and BMP9 signalling pathways in mesenchymal stem cells may underline their important roles in regulating osteogenic differentiation. PMID: 23844832 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 BMP9 signaling may be relevant during hepatocarcinogenesis in vivo. PMID: 23936038 We demonstrate a cross-talk between BMPs and CRYAB and a major effect of this regulatory interaction on resistance to apoptosis. PMID: 24072698 Mutations in BMP9 (also known as GDF2) were identified in three probands with hereditary hemorrhagic telangiectasia. PMID: 23972370 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 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 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 SNPs in the BMP9 gene appear to contribute to the risk of OPLL in association with certain clinical and demographic characteristics. PMID: 22829878 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 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 Mutual regulation by BMP-9 and CV2 is essential in regulating the development of the vascular endothelium. PMID: 22474252 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

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.