BMP-1/PCP Antibody [D9N3] | Primary Antibodies

Application: Reactivity: Human

Usage Information

Dilution
WB1:500 IP1:40

Application
WB, IP

Reactivity
Human

Source
Rat Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
111 kDa 180 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
BMP-1/PCP Antibody [D9N3] detects endogenous levels of total BMP-1/PCP protein.

Clone
D9N3

Synonym(s)
BMP1, PCP

Background
BMP‑1, also known as procollagen C‑proteinase (PCP), is a secreted zinc‑dependent metalloprotease of the astacin family that serves as the prototypical type I procollagen C‑propeptide protease and a key regulator of extracellular matrix assembly. The protein is synthesized as a multidomain precursor with an N‑terminal signal peptide and pro‑domain followed by an astacin‑like catalytic domain and multiple CUB and EGF‑like modules, and removal of the pro‑domain by a furin‑like proprotein convertase generates the active enzyme that associates with matrix components at the cell surface and within the pericellular space. BMP‑1/PCP cleaves the C‑terminal propeptides of fibrillar procollagens I, II, and III and also processes the C‑terminal domain of procollagen V, generating mature collagen molecules that can assemble into properly structured fibrils, and thereby directly controls the efficiency and quality of collagen fibrillogenesis. In addition to procollagens, BMP‑1 acts on a broader set of extracellular precursor proteins, including biglycan, laminin‑5, dentin matrix protein‑1, and the pro‑forms of lysyl oxidase, which link BMP‑1 activity to the maturation of proteoglycans, basement membrane networks, mineralized matrix components, and collagen cross‑linking enzymes. Through this substrate spectrum, BMP‑1 couples proteolytic processing to the acquisition of full structural and functional properties of the extracellular matrix, influencing matrix stiffness, fibril organization, and the capacity of tissues to withstand mechanical load, support mineral deposition, or provide cell‑adhesive scaffolds. BMP‑1 belongs to a small group of related proteases encoded by the BMP1 locus that generate several isoforms with distinct C‑terminal domain compositions, and these variants display differences in substrate preference, tissue distribution, and cofactor interactions, allowing tissue‑specific tuning of ECM processing. The enzyme interacts functionally with procollagen C‑endopeptidase enhancer proteins (PCPEs), which bind procollagen substrates and increase the efficiency of BMP‑1‑mediated C‑terminal cleavage, providing an additional regulatory layer that adjusts procollagen processing in response to matrix context. BMP‑1 activity contributes to bone and cartilage formation by ensuring proper maturation and assembly of collagenous matrices that support osteoblast and chondrocyte function, and BMP‑1‑dependent processing also influences activation of growth factor pathways that are embedded within ECM, including selected TGF‑β‑related components. Dysregulation of BMP‑1 expression or activity associates with connective tissue abnormalities, fibrotic remodeling, and impaired bone repair, reflecting the central position of this protease in coordinating collagen processing, cross‑linking enzyme activation, and integration of structural and signaling roles of the extracellular matrix.

Background

BMP‑1, also known as procollagen C‑proteinase (PCP), is a secreted zinc‑dependent metalloprotease of the astacin family that serves as the prototypical type I procollagen C‑propeptide protease and a key regulator of extracellular matrix assembly. The protein is synthesized as a multidomain precursor with an N‑terminal signal peptide and pro‑domain followed by an astacin‑like catalytic domain and multiple CUB and EGF‑like modules, and removal of the pro‑domain by a furin‑like proprotein convertase generates the active enzyme that associates with matrix components at the cell surface and within the pericellular space. BMP‑1/PCP cleaves the C‑terminal propeptides of fibrillar procollagens I, II, and III and also processes the C‑terminal domain of procollagen V, generating mature collagen molecules that can assemble into properly structured fibrils, and thereby directly controls the efficiency and quality of collagen fibrillogenesis. In addition to procollagens, BMP‑1 acts on a broader set of extracellular precursor proteins, including biglycan, laminin‑5, dentin matrix protein‑1, and the pro‑forms of lysyl oxidase, which link BMP‑1 activity to the maturation of proteoglycans, basement membrane networks, mineralized matrix components, and collagen cross‑linking enzymes. Through this substrate spectrum, BMP‑1 couples proteolytic processing to the acquisition of full structural and functional properties of the extracellular matrix, influencing matrix stiffness, fibril organization, and the capacity of tissues to withstand mechanical load, support mineral deposition, or provide cell‑adhesive scaffolds. BMP‑1 belongs to a small group of related proteases encoded by the BMP1 locus that generate several isoforms with distinct C‑terminal domain compositions, and these variants display differences in substrate preference, tissue distribution, and cofactor interactions, allowing tissue‑specific tuning of ECM processing. The enzyme interacts functionally with procollagen C‑endopeptidase enhancer proteins (PCPEs), which bind procollagen substrates and increase the efficiency of BMP‑1‑mediated C‑terminal cleavage, providing an additional regulatory layer that adjusts procollagen processing in response to matrix context. BMP‑1 activity contributes to bone and cartilage formation by ensuring proper maturation and assembly of collagenous matrices that support osteoblast and chondrocyte function, and BMP‑1‑dependent processing also influences activation of growth factor pathways that are embedded within ECM, including selected TGF‑β‑related components. Dysregulation of BMP‑1 expression or activity associates with connective tissue abnormalities, fibrotic remodeling, and impaired bone repair, reflecting the central position of this protease in coordinating collagen processing, cross‑linking enzyme activation, and integration of structural and signaling roles of the extracellular matrix.

References
https://pubmed.ncbi.nlm.nih.gov/8553073/ https://pubmed.ncbi.nlm.nih.gov/11358968/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%