Rabbit Antibody to Matriptase-1 (MTSP-1, ST14, SNC19, TADG-15, Epithin) Amino end cleaved MTSP-1

RP4-Matriptase-1 is a polyclonal antibody made to the Type-II serine protease matriptase-1.  The antibody is made to a synthetic peptide based on the amino end of shed human matriptase-1.  RP1-Matriptase-1 reacts with human, mouse and rat matriptase-1, and does not recognize matriptase-2. The antibody has been peptide-affinity purified, concentrated to 1.0 mg/ml, with the addition of 0.05% sodium azide as preservative and 50% glycerol as cryoprotectant.

Matriptase-1 was first identified as a gelatinolytic proteianse in the media and cell lysates of breast tumor cells in culture. Independently described as membrane-type serine proteinase-1 (MT-SP1), Prostamin, TADG15 (Tumor Associated Differentially-expressed Gene-15), ST14 (Supressor of Tumorigenicity 14), SNC19, PRSS14 (Protease, Serine, 14), and epithin (the mouse orthologue), the literature nomenclature is further confused by the addition of MTSP-1 (Mouse Trypsin-Type Serine Protease-1), a different protease with a name that predates MT-SP1. Originally matriptase-1 was thought to be specific for either prostate tumors (prostamin) or breast tumors (MT-SP1), or to be a tumor suppressor (TADG15). More extensive characterizations determined that matriptase is found in many normal and tumor cell lines, and in breast milk, serum and urine. Matriptase-2 has only 37% identity with matriptase-1, mostly in the catalytic domain. Matriptase-1 is a Type-II serine proteinase, meaning it contains a transmembrane motif in the amino end of the protein. The latent protein is membrane attached, and has a cytoplasmic tail. The extracellular domains contain a stem region, followed by two CUB domains and four repeats of LDL-receptor-like homology, and a serine protease domain located in the carboxyterminal end of the protein. Matriptase-1 is a member of the S1A family of the PA clan of serine proteinases, which includes acrosin, kallikreins, trypsin, chymotrypsin, and many other important enzymes. The endogenous inhibitor of matriptase-1 is thought to be HAI-1 (Hepatocyte Activator Inhibitor-1), a serine proteinase inhibitor that was determined to block the activation of HGF. Matriptase-1 is often found complexed with HAI-1, although some cell lines express either HAI-1 or matriptase-1 alone. When expressed alone, matriptase-1 is a single-chain molecule, and when expressed with HAI-1 the dominant form is a two-chain matriptase-1 bound with the HAI-1. Nonreduced SDS-PAGE Western blots yield bands of 110-95 kDa for matriptase-1 complexed with HAI-1, and a 70 kDa band for the single-chain form. The 95 kDa complex resolves to A and B chains of 45 and 25 kDa for matriptase-1, plus a 36 kDa band for the HAI-1. The single-chain form is produced by cleavage in the SEA domain, between the stem and the CUB domains, and the catalytic domain is liberated by cleavage after the LRLR domains.   A recommended starting concentration for Western blots is 1:1,000 when using colorimetric substrates such as BCIP/NBT, and 1:5,000 for chemiluminescent substrates.  Higher concentrations of antibody may be needed for samples from more distantly related species.  EDTA/EGTA treatment of tissues or lysates is required to see latent zymogen.

FOR RESEARCH USE ONLY. NOT FOR USE IN HUMANS.

Triple Point Biologics products are sold exclusively through Abcam. For availability, pricing and buying information please select your country below and press 'Go'. You will be relocated to the relevant datasheet page on Abcam's website.