Cat.No. : AD00128Z
Titer: ≥1x10^10 IFU/mL / ≥1x10^11 IFU/mL / ≥1x10^11 VP/mL / ≥1x10^12 VP/mL Size: 100 ul/500 ul/1 mL
Storage: -80℃ Shipping: Frozen on dry ice
| Cat. No. | AD00128Z |
| Target Gene | BMP7 |
| Product Type | Adenoviral particle |
| Insert | BMP7 |
| Titer | Varies lot by lot, for example, ≥1x10^10 IFU/mL, ≥1x10^11 IFU/mL, ≥1x10^11 VP/mL etc. |
| Size | Varies lot by lot, for example, 250 ul, 500 ul, 1 mL etc. |
| Storage | Store at -80℃. Avoid multiple freeze/thaw cycles. |
| Shipping | Frozen on dry ice |
| Creative Biogene ensures high-quality adenovirus particles by optimizing and standardizing production protocols and performing stringent quality control (QC). The specific QC experiments performed vary between adenovirus particle lots. | |
| Endotoxin | Endotoxins, primarily derived from Gram-negative bacteria, can trigger adverse immune responses. Endotoxin contamination is a significant concern in adenovirus production, especially for applications in animal studies and gene therapy. Creative Biogene utilizes rigorous endotoxin detection methods to monitor the endotoxin level in our produced adenovirus particles to ensure regulatory compliance. |
| Sterility | Creative Biogene ensures that adenovirus products are free of any bacterial, fungal and other microbial contamination. |
| Ad5 E1 Detection | All Creative Biogene adenoviruses are PCR tested to ensure that there are no detectable E1 sequences in the particles, which could be from revertants or external E1 contamination. |
| RCA Assays | Adenovirus products originating at Creative Biogene are guaranteed to have undetectable replication-competent adenovirus (RCA). This quality control measure is important because there is always the possibility of wild-type contamination due to revertants or environmental sources. |
| PFU Titering | All purified adenovirus preparations are tested for infectious titer. Creative Biogene's PFU test takes a few days longer but counts true plaques in HEK cells rather than estimating PFU titers via IHC staining or TCI50 of infected cells. |
| Gene Name | BMP7 bone morphogenetic protein 7 [ Homo sapiens ] |
| Gene Symbol | BMP7 |
| Synonyms | BMP7; bone morphogenetic protein 7; OP 1; osteogenic protein 1; BMP-7; OP-1; |
| Gene ID | 655 |
| UniProt ID | P18075 |
| mRNA Refseq | BC004248 |
| Chromosome Location | 20q13 |
| Function | cytokine activity; growth factor activity; protein binding; contributes_to protein binding; |
| Pathway | ALK2 signaling events, organism-specific biosystem; BMP receptor signaling, organism-specific biosystem; Cytokine-cytokine receptor interaction, organism-specific biosystem; Cytokine-cytokine receptor interaction, conserved biosystem; Endochondral Ossification, organism-specific biosystem; Hedgehog signaling pathway, organism-specific biosystem; Hedgehog signaling pathway, conserved biosystem; |
| MIM | 112267 |
Bone morphogenetic protein 7 (BMP7) is a member of the transforming growth factor-β (TGF-β) family and plays a key role in energy expenditure. However, whether and how BMP7 regulates hepatic insulin sensitivity remains poorly understood. Here, researchers show that hepatic BMP7 expression is reduced in high-fat diet (HFD)-induced diabetic mice and in palmitic acid (PA)-induced insulin-resistant HepG2 and AML12 cells. BMP7 improved the insulin signaling pathway in insulin-resistant hepatocytes. Conversely, knockdown of BMP7 further impaired insulin signaling in PA-treated cells. Increased expression of BMP7 by adenovirus expressing BMP7 improved hyperglycemia, insulin sensitivity, and insulin signaling. Furthermore, BMP7 inhibited mitogen-activated protein kinase (MAPK) in obese mouse livers and PA-treated cells. Moreover, inhibition of MAPK recapitulated the effects of BMP7 on insulin signaling in cultured hepatocytes treated with PA. Activation of p38 MAPK abolished BMP7-mediated upregulation of insulin signaling both in vitro and in vivo. Taken together, these results suggest that hepatic BMP7 regulates insulin sensitivity by inhibiting MAPK, providing new insights into the treatment of insulin resistance-related diseases such as type 2 diabetes.
In cultured hepatocytes, the researchers observed that BMP7 appeared to prevent lipid accumulation. To confirm this finding, lipid deposition in the liver was analyzed in the following experiments. First, the researchers quantified the expression level of BMP7 in the liver by immunohistochemical analysis. As shown in Figure 1A, the signal corresponding to BMP7 was significantly reduced in the liver of obese mice. Tail vein injection of adenoviruses expressing BMP7 (Ad-BMP7) successfully increased the expression of BMP7 in the liver. H&E staining and oil red analysis showed that lipid deposition in the liver of obese mice was greatly upregulated. However, increased BMP7 expression in the liver attenuated lipid accumulation (Figure 1B). Consistent with these morphological changes, increased BMP7 expression in the liver reduced the levels of triglycerides and free cholesterol (Figures 1C and D).
Figure 1. Increased expression of BMP7 ameliorates lipid deposition in the liver of obese mice. (Ma H, et al., 2019)
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Used the Human BMP7 adenoviral particles in renal cells, and the anti-fibrotic effects were clearly evident. The product was stable, and Creative Biogene provided detailed protocols. Excellent for translational research!
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