anti-human BMP-1 monoclonal antibody Anti-Human 100 µg,Reliatech,101-M231

This antibody was produced from a hybridoma (Rat myeloma fused with spleen cells from a Rat immunized with human recombinant protein of bone morphogenetic Protein 1 (BMP-1), also known as Procollagen C Proteinase (PCP).

Host

Rat

Reactivity

Human

Application

WB, IHC

Platform ID

BAB120710291

Reliatech

Headquarters

Lindener Straße 15 38300 Wolfenbüttel Germany

Contact

Tel: +49 (0) 5331 - 8586987
Fax: +49 (0) 5331- 8586989

Product Specifications
Scientific Background
Synonyms

Specifications

Nameanti-human BMP-1 monoclonal antibody Anti-Human 100 µg
Cat. No.101-M231
Accession NumberP13497
HostRat
IsotypeIgG2
ReactivityHuman
ApplicationWB, IHC
Working DilutionsWB: 1:200-1000, IHC: 1:50-100
Clone Number(#11B23)
Appearance/Formlyophilized
FormulationPBS
ReconstitutionCentrifuge vial prior to opening. Reconstitute the antibody with 500 µl sterile PBS and the final concentration is 200 µg/ml.
StorageLyophilized samples are stable for 2 years from date of receipt when stored at -70°C. Reconstituted antibody can be aliquoted and stored frozen at < -20°C for at least six months without detectable loss of activity.
Regulatory StatusFor research use only

Scientific Background

Bone morphogenetic protein 1 (BMP1), also known as procollagen Cproteinase (PCP), is a zinc protease of the astacin family. BMP1/ PCP plays a key role in formation of extracellular matrix (ECM) by converting precursor proteins into their mature and functional forms. The precursor proteins identified as substrates for BMP1/ PCP include collagens, biglycan, laminin 5, dentin matrix protein1, and lysyl oxidase. There are six alternatively spliced forms known to be derived from the BMP 1 gene, and isoform 1 consisting of residues 1 to 730 was expressed. The secreted and purified protein does not contain the signal peptide (amino acid residues 122) and pro domain (residues 23-120), but contain protease (residues 121-321), CUB I (residues 322-434), CUB II (residues 435-546), EGFlike (residues 547-588) and CUB III (residues 591-703) domains. The pro domain is apparently cleaved by a furinlike proprotein convertase. The purified BMP1/ PCP is an active protease and its peptidase activity can be determined as described above. The purified BMP1/ PCP is predicted to possess procollagen C proteinase activity because it contains the minimal domain structure required.

Synonyms

BMP1; PCP; TLD; PCP2; PCOLC

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