Recombinant Human BMP2 protein(Gln283~Arg396), His-tagged
Cat.No. : | BMP2-867H |
Product Overview : | Recombinant Human BMP2 protein(Gln283~Arg396) was expressed in E. coli, with a polyhistidine tag at the N-terminus. |
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Species : | Human |
Source : | E.coli |
Tag : | His |
Protein Length : | Gln283~Arg396 |
Form : | PBS, pH7.4. |
Molecular Mass : | 14.2kDa |
Endotoxin : | <1.0EU per 1μg (determined by the LAL method) |
Purity : | > 95% |
Storage : | Avoid repeated freeze/thaw cycles. Store at 2-8°C for one month. Aliquot and store at -80°C for 12 months. |
Reconstitution : | Reconstitute in 10mM PBS (pH7.4) to a concentration of 0.1-1.0 mg/mL. Do not vortex. |
Gene Name | BMP2 bone morphogenetic protein 2 [ Homo sapiens ] |
Official Symbol | BMP2 |
Synonyms | BMP2; bone morphogenetic protein 2; BMP2A; BMP-2A; bone morphogenetic protein 2A; BDA2; |
Gene ID | 650 |
mRNA Refseq | NM_001200 |
Protein Refseq | NP_001191 |
MIM | 112261 |
UniProt ID | P12643 |
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Case 1: Lin YC, et al. Am J Hum Genet. 2021
SCUBE3 is a crucial glycoprotein that acts as a co-receptor for various growth factors. We've identified that inactivating variants of SCUBE3 can cause a range of developmental issues, leading to a new syndromic disorder. This disorder, observed in 18 individuals from different families, manifests through growth reduction, skeletal and dental features, and unique facial characteristics. Our lab studies revealed these genetic variants disrupt SCUBE3's function, affecting BMP signaling by altering transcript processing and protein secretion. SCUBE3 supports BMP2/BMP4 interactions, enhancing signaling via BMP receptor complexes. Mouse models lacking SCUBE3 mirrored human symptoms, displaying facial and bone growth defects due to impaired BMP-driven processes.
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Fig1. SCUBE3 specifically interacts with BMP proteins but not TGF-β1.
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Fig2. SCUBE3 overexpression enhances BMP2 downstream signaling in C3H10T1/2 cells.
Case 2: Meira M, et al. MAbs. 2024
Some antibody drugs that block immune checkpoints, such as PD-1, PD-L1, and CTLA-4, have limited effectiveness. Aiming at several pathways at once could improve cancer treatment. RGMb is a recently found pathway affected by gut bacteria and connects with PD-L2. We created human antibodies 2C11 and 5C10 that bind strongly to RGMb. We developed human antibodies, 2C11 and 5C10, which have strong affinities for RGMb. These antibodies block RGMb's interaction with PD-L2. Specifically, 2C11 affects RGMb's interaction with BMP2-4, while 5C10 targets Neo1. The 2C11 epitope aligns with PD-L2 and BMP2-4 sites on RGMb. Combining mAb 2C11 with anti-PD-1 or anti-PD-L1 in cancer models significantly boosts anti-tumor responses.
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Fig1. Inhibition of the huRGMb/huBMP2 interactions by RGMb antibodies.
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Fig2. Anticipated epitopes of RGMb mAbs 2C11 and 5C10 and PD-L2-binding interface in relation to BMP2-, BMP4-, Neo1-, and PD-L2-binding regions of RGMb.
Human BMP2 is vital for bone and cartilage development, playing a big role in both scientific research and industrial applications through the use of recombinant BMP2 (rhBMP2). In the lab, rhBMP2's ability to promote bone growth is a major focus. Researchers use it to trigger certain changes in mouse chondrogenic cells, which helps them study bone-building processes. It's also a popular tool in various lab techniques like ELISA and Western Blotting to explore how proteins interact, their expression, and where they're located in tissues. This is especially important in understanding embryonic growth, organ development, and how bones form and mend.
In the industrial realm, rhBMP2 is a cornerstone in regenerative medicine, especially for healing bones and crafting new tissues. It's highly valued in developing treatments for bone and dental issues due to its strong bone-growing capabilities. RhBMP2's purity and effectiveness are carefully measured, making it a reliable choice in cell studies and standardized research tools. The production of rhBMP2 also drives the creation of biomaterials that aid in bone repair and regeneration by encouraging bone marrow stem cells to migrate and turn into bone tissue.
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Fig1. Schematic illustrations of the dual effects of BMP2pp in Ti particles induced osteolysis. (Jiaqian Wang, 2023)
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Fig2. Nanoclay gels attenuate BMP2-associated inflammation and promote chondrogenesis to enhance BMP2-spinal fusion. (Takuya Furuichi, 2024)
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