Recombinant Human Bone Morphogenetic Protein 1 (BMP1) Protein (His)

Name: Recombinant Human Bone Morphogenetic Protein 1 (BMP1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-04415P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other 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 Bone Morphogenetic Protein 1 (BMP1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P13497
Target Symbol	BMP1
Synonyms	BMP 1; BMP-1; BMP1; BMP1_HUMAN; Bone morphogenetic protein 1; Mammalian tolloid protein; mTld; OI13; PCOLC; PCP; PCP2; Procollagen C endopeptidase; Procollagen C proteinase; Procollagen C-proteinase; TLD; Tolloid; Drosophila; homolog of
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	AATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRGIFLDTIVPKYEVNGVKPPIGQRTRLSKGDIAQARKLYKCPACGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSLDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGSKLPEPIVSTDSRLWVEFRSSSNWVGKGFFAVYEAICGGDVKKDYGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSTLIGRYCGYEKPDDIKSTSSRLWLKFVSDGSINKAGFAVNFFKEVDECSRPNRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRCEAACGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEKPEVITSQYNNMRVEFKSDNTVSKKGFKAHFFSDKDECSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNKHDCKEAGCDHKVTSTSGTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFMEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSKKPEPVLATGSRMFLRFYSDNSVQRKGFQASHATECGGQVRADVKTKDLYSHAQFGDNNYPGGVDCEWVIVAEEGYGVELVFQTFEVEEETDCGYDYMELFDGYDSTAPRLGRYCGSGPPEEVYSAGDSVLVKFHSDDTITKKGFHLRYTSTKFQDTLHSRK
Expression Range	121-986aa
Protein Length	Full Length of Mature Protein
Mol. Weight	102.0kDa
Research Area	Developmental 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.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
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	Metalloprotease that plays key roles in regulating the formation of the extracellular matrix (ECM) via processing of various precursor proteins into mature functional enzymes or structural proteins. Thereby participates in several developmental and physiological processes such as cartilage and bone formation, muscle growth and homeostasis, wound healing and tissue repair. Roles in ECM formation include cleavage of the C-terminal propeptides from procollagens such as procollagen I, II and III or the proteolytic activation of the enzyme lysyl oxidase LOX, necessary to formation of covalent cross-links in collagen and elastic fibers. Additional substrates include matricellular thrombospondin-1/THBS1 whose cleavage leads to cell adhesion disruption and TGF-beta activation.; Plays an important role in bone repair by acting as a coactivator of BMP7.
Subcellular Location	Golgi apparatus, trans-Golgi network. Secreted, extracellular space, extracellular matrix. Secreted.; [Isoform BMP1-3]: Secreted.
Protein Families	Peptidase M12A family
Database References	HGNC: 1067 OMIM: 112264 KEGG: hsa:649 STRING: 9606.ENSP00000305714 UniGene: PMID: 30062502 Mechanical stress affects the osteogenic differentiation of human ligamentum flavum cells via the BMP-Smad1 signaling pathway. PMID: 28944874 For meprin beta a reduction and for BMP-1 an increase in activity was reported under increasing calcium concentrations. PMID: 28365001 BMP1 c.941G>A (p.(R314H)) variant was identified in the family with Chiari malformation type 1. PMID: 28513615 Results indicate the significance of follistatin-like protein 1 (FSTL1) in driving oncogenesis and metastasis in esophageal squamous cell carcinoma (ESCC) by coordinating NF-kappa B (NFkappaB) and bone morphogenetic proteins (BMP) pathway control. PMID: 28883005 Given the association of BMP1-related Osteogenesis Imperfecta (OI) with very high bone material density, concerns remain whether anti-resorptive therapy is indicated in this ultra-rare form of OI PMID: 27576954 Data show that the KKN1 fragment generated by BMP1-cleavage of WFIKKN1 protein contributes most significantly to the observed enhancer activity. PMID: 27782377 a previously unknown O-glycosylation site and Asn-hydroxylation site, indicating a novel feature of BMP-1 in the EGF domain. The study clearly outlines the benefit of in-depth characterization of overexpressed proteins to deduce important protein modifications. PMID: 26944735 BMP-1 accelerates the connective tissue growth factor production dependently on cellular internalization in human dental pulp cells, indicating a novel property of BMP-1 which potentially enhances bone-like reparative dentin formation. PMID: 25944709 Studies indicate crosstalk between Notch receptor and Wnt protein, Hedgehog protein, hypoxia and transforming growth factor beta (TGFbeta)/bone morphogenetic protein (BMP) pathways. PMID: 26592459 study thus highlights the severe and progressive nature of BMP1-associated OI in adults and broadens insights into the functional consequences of BMP1/mTLD-deficiency on ECM organization. PMID: 25656619 Data indicate that BMP-1 can simultaneously trigger matrix assembly and boost the synthesis of matrix proteins via a direct effect on growth factors in the contexts of development, growth and tissue repair. [review] PMID: 25701650 Two novel variants in the BMP1 gene: c.808A>G and c.1297G>T care associated with osteogenesis imperfecta. PMID: 25402547 Frequent bone fracture in children is cause by BMP1-1 deficiency. PMID: 25214535 mutations of the DSP-PP P4 to P4' cleavage site can block, impair or accelerate dentin sialoprotein phosphophoryn cleavage, and suggest that its Bone morphogenic protein 1 cleavage site is conserved in order to regulate its cleavage efficiency PMID: 25158199 High BMP1 expression is associated with type-1 diabetes. PMID: 24984282 Loss of bone morphogenetic protein is associated with prostate cancer. PMID: 24042462 miR-194 suppresses metastasis of non-small cell lung cancer through regulating expression of BMP1 and p27kip1 PMID: 23584484 Sequence analysis of BMP1 genes did not reveal any putative mutations for hyperostosis cranialis interna to chromosome 8p21 PMID: 23640157 Controlling inhibition of bone morphogenetic protein (BMP1) modulates the number of SOX1 expressing cells, whereas PAX6, another neural precursor marker, remains the same. PMID: 22860217 Excluding anterior cervical fusions, there are no significant differences between spinal fusion procedures with and without BMP-associated overall complications. PMID: 21897187 The molecular and cellular bases of BMP1-dependent osteogenesis were defined. The importance of BMP1 for bone formation and stability were shown in humans and zebrafish. PMID: 22482805 We conclude that BMP1 is an additional gene mutated in autosomal recessive osteogenesis imperfecta (AR-OI). PMID: 22052668 High expression of BMP pathway genes are associated with atypical teratoid/rhabdoid tumors. PMID: 21946044 Disruption of BMPR1A-mediated BMP1 signalling during the narrow window of early embryogenesis may interfere with normal VBW formation, causing omphalocele phenotype in the Cd chick model. PMID: 21258932 Bone morphogenetic protein-1 processes insulin-like growth factor-binding protein 3. PMID: 21697095 BMP1-3 is a novel systemic regulator of bone repair. PMID: 21453682 Circulating bone morphogenetic protein 1-3 isoform increases renal fibrosis. PMID: 21415150 Three isoforms of BMP1 ranging from the shortest BMP1-5 to the longest (mTLD, inefficient at processing procollagen in vitro) were all shown to be capable of removing the highly conserved propeptides from both proDCN. PMID: 20026052 Data show that only those containing both PCPE1 CUB1 and CUB2 were capable of enhancing BMP-1 activity and binding to a mini-procollagen substrate with nanomolar affinity. PMID: 19801683 bone morphogenetic protein-1 (BMP-1), which exhibits procollagen C-proteinase activity, cleaves the C-terminal propeptide from human procollagen VII PMID: 11986329 Post-translational modification is required for secretion and stability of the protein. PMID: 12218058 the minimal domain structure for PCP activity is considerably shorter than expected and comprises the metalloproteinase domain and the CUB1 and CUB2 domains of BMP-1 PMID: 12637537 Pro-BMP-1 is cleaved in the trans-Golgi network PMID: 12637569 Dermal wound healing in red Duroc pigs show unique mRNA expression of HSP47,BMP-1,TIMP1-3 and hypercontracted,hyperpigmented scars. PMID: 15225209 cleaves LG3 from recombinant endorepellin at the physiologically relevant site and cleaves LG3 from endogenous perlecan in cultured mouse and human cells PMID: 15591058 chordinase activity of BMP1 is not enhanced by PCPE-1 PMID: 15817489 tolloid-like 1 binds procollagen C-proteinase enhancer protein 1 and differs from bone morphogenetic protein 1 in the functional roles of homologous protein domains PMID: 16507574 bone morphogenetic protein 1 is inhibited by native and altered forms of alpha2-macroglobulin PMID: 17071617 the BMP1 prodomain specifically binds and regulates signaling by BMP2 and BMP4 PMID: 17255107 By mutating residues flanking the cleavage site of collagen type V alpha 1, we showed that the aspartate residue at position P2' is essential for BMP-1 activity. PMID: 17407447 data support the concept that the C-terminal domains of BMP1 are important for substrate recognition and for controlling and restricting its proteolytic activity via exosite binding PMID: 17516847 BMP1 processes PRL to a 17-kDa anti-angiogenic factor. PMID: 17548836 vascular Bmp Msx2 Wnt signaling and oxidative stress have roles in arterial calcification [review] PMID: 18056036 Expression of BMP1, BMP6, BMP7, and BMP-receptor 2 was significantly increased in advanced stages of myelofibrosis compared and enhanced levels of BMP6 expression were already evident in prefibrotic stages of primary myelofibrosis. PMID: 18349123 The crystal structures of the protease domains of human BMP-1 and the closely related Tolloid-like protease 1 (TLL-1), are reported. PMID: 18824173 BMP-1 expression was significantly higher in thyroid tumors with psammoma bodies or with stromal calcification. PMID: 19305382 Regulation of alternative splicing of mRNA for procollagen C-endopeptidase in leiomyomas and myometrium depends mainly on the hormonal status of women PMID: 19323056 FN binds BMP1-like proteinases in vivo and that FN is an important determinant of the in vivo activity levels of BMP1-like proteinases. PMID: 19617627

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.