You Searched For: Prolyl+endopeptidase+inhibitor

Catalog Number: (76081-104)

Supplier: Bioss

Description: In association with DPP4 is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers.

Catalog Number: (10422-872)

Supplier: Bioss

Description: In association with DPP4 is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers.

Catalog Number: (10422-866)

Supplier: Bioss

Description: In association with DPP4 is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers.

Catalog Number: (10422-864)

Supplier: Bioss

Description: In association with DPP4 is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers.

Catalog Number: (10422-868)

Supplier: Bioss

Description: In association with DPP4 is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers.

Catalog Number: (76081-102)

Supplier: Bioss

Description: In association with DPP4 is involved in the pericellular proteolysis of the extracellular matrix (ECM), the migration and invasion of endothelial cells into the ECM. May have a role in tissue remodeling during development and wound healing, and may contribute to invasiveness in malignant cancers.

Supplier: Bachem Americas

Description: Specific inhibitor of rat endopeptidase 24.16 (oligopeptidase M, neurolysin).

Supplier: Bachem Americas

Description: MRFA is used as a calibration standard in mass spectrometry (ESI). Miao et al. studied Pt(II) complexes of the tetrapeptide by mass spectrometric methods. MRFA has been shown to be a competitive inhibitor of an enkephalin-generating endopeptidase isolated from rat brain. The peptide is a substrate for dipeptidyl peptidase III from human erythrocytes and for snapalysin.

Catalog Number: (89161-686)

Supplier: Enzo Life Sciences

Description: Apstatin is a potent and selective inhibitor of aminopeptidase P (APP), Ki=2.6 µM for purified rat lung membrane-bound APP. It blocks the APP-mediated degradation of bradykinin. Limits myocardial infarct size alone or with ACE inhibitors.

Catalog Number: (103010-644)

Supplier: Anaspec Inc

Description: Cathepsin L, a lysosomal endopeptidase, is a member of the papain-like family of cysteine proteinases

Catalog Number: (N-1000.0005BA)

Supplier: Bachem Americas

Description: A reversible compeptitive protease inhibitor, which was shown to inhibit cathepsins B, H, L, and S, calpain and trypsin. Ac-LLR-CHO inhibits the trypsin-like activity of the proteasome endopeptidase complex. CAS Number (hemisulfate): 103476-89-7.

Catalog Number: (103010-622)

Supplier: Anaspec Inc

Description: Factor Xa (FXa) is a serine endopeptidase composed of two disulfide-linked subunits

Catalog Number: (103010-624)

Supplier: Anaspec Inc

Description: Factor Xa (FXa) is a serine endopeptidase composed of two disulfide-linked subunits

Catalog Number: (77437-458)

Supplier: Bioss

Description: Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, vibronectin, tenascin, laminin, fibronectin, fibrin or casein. Have also dipeptidyl peptidase activity, exhibiting the ability to hydrolyze the prolyl bond two residues from the N-terminus of synthetic dipeptide substrates provided that the penultimate residue is proline, with a preference for Ala-Pro, Ile-Pro, Gly-Pro, Arg-Pro and Pro-Pro. Natural neuropeptide hormones for dipeptidyl peptidase are the neuropeptide Y (NPY), peptide YY (PYY), substance P (TAC1) and brain natriuretic peptide 32 (NPPB) (PubMed:21314817). The plasma membrane form, in association with either DPP4, PLAUR or integrins, is involved in the pericellular proteolysis of the extracellular matrix (ECM), and hence promotes cell adhesion, migration and invasion through the ECM. Plays a role in tissue remodeling during development and wound healing. Participates in the cell invasiveness towards the ECM in malignant melanoma cancers. Enhances tumor growth progression by increasing angiogenesis, collagen fiber degradation and apoptosis and by reducing antitumor response of the immune system. Promotes glioma cell invasion through the brain parenchyma by degrading the proteoglycan brevican. Acts as a tumor suppressor in melanocytic cells through regulation of cell proliferation and survival in a serine protease activity-independent manner.

Supplier: Enzo Life Sciences

Description: DMOG is a cell permeable prolyl-4-hydroxylase inhibitor which upregulates HIF activity. HIF activation stimulates angiogenesis in several different models. DMOG also inhibits FIH (Factor Inhibiting HIF), an asparaginyl hydroxylase, which enhances the HIF response. It is active in vivo and attenuates myocardial injury in a rabbit ischemia reperfusion model (20mg/kg). Is expected to act pro-angiogenic.

Supplier: Anaspec Inc

Description: Matrix metalloproteinases (MMPs) belong to a family of secreted or membrane-associated zinc endopeptidases capable of digesting extracellular matrix components. MMP-12 (macrophage elastase) is involved in smoke-induced emphysema, tumor and other diseases. MMP-12 is secreted as a 54-kDa zymogen and becomes the mature 45-kDa active form after proteolytic cleavage. MMP-12 has a broad range of substrates, including α-1 proteinase inhibitor, α-2 antiplasmin, plasminogen activator inhibitor-2, collagen IV, laminin, fibronectin, elastin, but not interstitial collagens.

The sequence (Accession # NP_002417) corresponding to the catalytic domain (aa 106-267) of Human MMP-12 was expressed in E. coli. The recombinant human MMP-12 was purified from bacterial lysate and refolded using proprietary technique. The molecular weight of the recombinant Human MMP-12 Catalytic Domain is 18 kDa.