Recombinant Human BMP1/PCP Protein Standard (His tag)
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Recombinant Human BMP1/PCP Protein Standard (His tag) is a Human Fragment protein, expressed in HEK 293 cells, with >80%, suitable for sELISA, SDS-PAGE.
View Alternative Names
PCOLC, BMP1, Bone morphogenetic protein 1, BMP-1, Mammalian tolloid protein, Procollagen C-proteinase, mTld, PCP
- sELISA
Supplier Data
Sandwich ELISA - Recombinant Human BMP1/PCP Protein Standard (His tag) (AB323019)
Sandwich ELISA with the capture antibody dilution at 2 µg/mL and detector antibody dilution at 0.5 µg/mL.
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human BMP1/PCP Protein Standard (His tag) (AB323019)
SDS-PAGE analysis of ab323019 under reducing conditions for 2ug protein.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Specifications
Form
Liquid
General info
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 (PubMed : 33206546). Thereby participates in several developmental and physiological processes such as cartilage and bone formation, muscle growth and homeostasis, wound healing and tissue repair (PubMed : 32636307, PubMed : 33169406). 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 (PubMed : 31152061, PubMed : 33206546). Additional substrates include matricellular thrombospondin-1/THBS1 whose cleavage leads to cell adhesion disruption and TGF-beta activation (PubMed : 32636307).. Isoform BMP1-3. Plays an important role in bone repair by acting as a coactivator of BMP7.
Post-translational modifications
Proteolytically activated in the trans-Golgi network by furin-like/paired basic proprotein convertases, cleavage is not required for secretion.
Target data
Product promise
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