BMP-1 蛋白, Human (His)

Bone morphogenetic protein 1 (BMP-1), also known as metalloproteinases, belongs to the BMP-1/tolloidlike proteinases (BTP) family^[1][2]. BMP-1 is also a signature extracellular matrix (ECM) protein associated with high metastatic potential in breast tumors^[3]. BMP-1 processes growth factors, including TGF-β, BMP-2, BMP-4, and GFD8, regulates morphogenesis^[4], and mediates the cleavage of COOH-terminal propeptide of type I procollagen (CICP) in the extracellular space^[1]. The total length of human BMP-1 protein is 986 amino acids (M1-K986), with 4 glycosylation domains. BMP-1 Protein, Human (His) has a total length of 866 amino acids (A121-K986), is expressed in E. coli cells with a N-terminal *His-tag.

骨形态发生蛋白 1 (BMP-1) 也称为金属蛋白酶，属于 BMP-1/tolloidlike 蛋白酶 (BTP) 家族^[1][2]。已知 BTP 参与肌肉生长和体内平衡的控制以及伤口愈合和组织修复，而 BMP-1 是一种标志性细胞外基质 (ECM) 蛋白，与乳腺肿瘤的高转移潜力相关^[3] 。BMP-1 通过加工成熟功能性细胞外基质 (ECM) 蛋白和多种生长因子（包括 TGFβ、BMP2、BMP4 和 GFD8）的前体来调节形态发生[4]。
BMP1 是主要的 C-出生后肺成纤维细胞中的蛋白酶，介导 I 型前胶原 COOH 末端前肽 (CICP) 的裂解，主要作用位点为细胞外空间^[1]。
BMP1 维持适当的 I 型前胶原水平及其活化产物，是维持牙周稳态和正常牙骨质形成的重要组成部分^[2]。
血小板反应蛋白-1 (TSP-1) 是一种 ECM 蛋白，分类为“基质细胞”因其调节细胞-基质相互作用的能力而被称为“基质细胞”，导致 BMP-1 过度表达。然而，BMP-1 既可以触发细胞粘附破坏，又可以在富含 TSP-1 的微环境中刺激 TGF-β 信号传导，从而促进原代人角膜细胞分化为肌成纤维细胞^[3]。
因此，BMP1 参与多种发育和生理过程，例如软骨和骨骼形成、肌肉生长和稳态^[2][3]。
BMP1 突变该基因会导致人类成骨不全症，这是一种以易骨折的脆骨为特征的骨骼疾病，或导致小鼠牙周病和皮肤脆性的表型^[3]。
BMP1-3 是一种骨修复的新型系统调节剂。BMP-1 基因的 BMP1-3 亚型在人血浆中循环并增强骨愈合。体外 BMP1-3 会增加 MC3T3-E(1) 成骨细胞样细胞中 I 型胶原蛋白和骨钙素的表达，并增强骨髓间充质干细胞形成矿化骨结节^[4]。
BMP-1广泛存在于不同的动物中，而人类的序列与大鼠(96.54%)、小鼠(96.34)高度相似。

BMP-1 produced by human keratocytes (185 nM; 4 hr; 37 ℃) cleaves TSP-1 whether soluble and insoluble isoform, and results in abnormal adhesion of HT1080 cells on cleaved TSP-1^[4].
BMP1-3, isoform of the Bmp-1, circulates in the human plasma and is significantly increased in patients with acute bone fracture^[5].
BMP1-3 (50 ng/mL; once every two days for three times) increases the expression of collagen type I and osteocalcin in MC3T3-E(1) osteoblast like cells, and enhances the formation of mineralized bone nodules from bone marrow mesenchymal stem cells^[5].

BMP1-3 (human; 3 μg/rats and 20 μg/rabbits; i.v.; 3 times per week for 6 weeks) enhances bone healing when treated systemically to rats (250-300 g) with a long bone fracture and locally to rabbits with a critical size defect of the ulna^[5].

Measured by its ability to cleave a fluorogenic peptide substrate Mca-YVADAPK(Dnp)-OH. The specific activity is 4.879 pmol/min/µg.

Human

E. coli

N-6*His

P13497 (A121-K986)

649  [NCBI]

AATSRPERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVVGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEPQEVESLGETYDFDSIMHYARNTFSRGIFLDTIVPKYEVNGVKPPIGQRTRLSKGDIAQARKLYKCPACGETLQDSTGNFSSPEYPNGYSAHMHCVWRISVTPGEKIILNFTSLDLYRSRLCWYDYVEVRDGFWRKAPLRGRFCGSKLPEPIVSTDSRLWVEFRSSSNWVGKGFFAVYEAICGGDVKKDYGHIQSPNYPDDYRPSKVCIWRIQVSEGFHVGLTFQSFEIERHDSCAYDYLEVRDGHSESSTLIGRYCGYEKPDDIKSTSSRLWLKFVSDGSINKAGFAVNFFKEVDECSRPNRGGCEQRCLNTLGSYKCSCDPGYELAPDKRRCEAACGGFLTKLNGSITSPGWPKEYPPNKNCIWQLVAPTQYRISLQFDFFETEGNDVCKYDFVEVRSGLTADSKLHGKFCGSEKPEVITSQYNNMRVEFKSDNTVSKKGFKAHFFSDKDECSKDNGGCQQDCVNTFGSYECQCRSGFVLHDNKHDCKEAGCDHKVTSTSGTITSPNWPDKYPSKKECTWAISSTPGHRVKLTFMEMDIESQPECAYDHLEVFDGRDAKAPVLGRFCGSKKPEPVLATGSRMFLRFYSDNSVQRKGFQASHATECGGQVRADVKTKDLYSHAQFGDNNYPGGVDCEWVIVAEEGYGVELVFQTFEVEEETDCGYDYMELFDGYDSTAPRLGRYCGSGPPEEVYSAGDSVLVKFHSDDTITKKGFHLRYTSTKFQDTLHSRK

Approximately 102 kDa

Greater than 90% as determined by reducing SDS-PAGE.

无菌粉末

Lyophilized from a 0.2 μm solution of Tris-based buffer, 50% Glycerol or 10 mM Tris-HCl, 1 mM EDTA, 6% Trehalose, pH 8.0 or PBS, 6% Trehalose, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.

• [1]. N'Diaye EN, et al. Extracellular BMP-1 is the major proteinase for COOH-terminal proteolysis of type I procollagen in lung fibroblasts. Am J Physiol Cell Physiol. 2021 Feb 1;320(2):C162-C174.  [Content Brief]

  [2]. Wang J, et al. Proteinase bone morphogenetic protein 1, but not tolloid-like 1, plays a dominant role in maintaining periodontal homeostasis. J Periodontol. 2021 Jul;92(7):1018-1029.  [Content Brief]

  [3]. Anastasi C, et al. BMP-1 disrupts cell adhesion and enhances TGF-β activation through cleavage of the matricellular protein thrombospondin-1. Sci Signal. 2020 Jul 7;13(639):eaba3880.  [Content Brief]

  [4]. Grgurevic L, et al. Bone morphogenetic protein (BMP)1-3 enhances bone repair. Biochem Biophys Res Commun. 2011 Apr 29;408(1):25-31.  [Content Brief]