You Searched For: 4-Hydroxybenzoylacrylic acid


2  results were found

Sort Results

List View Easy View
SearchResultCount:"2"
Description: Matrix Metalloproteinases (MMPs) are a large family of endopeptidases. Collectively, MMPs can degrade all kinds of extracellular matrix proteins, and can also process a number of bioactive molecules. They are known to be involved in the cleavage of cell surface receptors, the release of apoptotic ligands, and chemokine/cytokine inactivation. MMPs are also thought to play a major role in cell behaviors such as cell proliferation, migration (adhesion/dispersion), differentiation, angiogenesis, apoptosis, and host defense.
This peptide is a sensitive substrate for assaying MMP-1, 2, 7, 8, 12, 13 and 14 activities, Abs/Em = 494/521 nm.
Sequence:QXL™ 520 -γ-Abu-PQGL-Dab(5-FAM)-AK-NH2
MW:1647.7 Da
% peak area by HPLC:95
Storage condition:-20° C
Catalog Number: 103005-944
Supplier: Anaspec Inc


Description: TIMP-1 and TIMP-2 are inhibitory enzymes of matrix metalloproteinase family. TIMPs are of great importance in the maintenance of connective tissue integrity. TIMP-2 shows the highest binding affinity to both the latent (pro) and active forms of 72 kD Type IV collagenase (MMP-2) and active form of 92 kD Type IV collagenase (MMP-9). TIMPs inhibit the proteolytic invasiveness of tumor cells and normal placental trophoblast cells.
Catalog Number: 89361-088
Supplier: Genetex


Description: Human MMP13 AccuSignal ELISA Kit
Catalog Number: 76236-754
Supplier: Rockland Immunochemical


Description: Matrix Metalloproteinases (MMPs) are a large family of endopeptidases. Collectively, MMPs can degrade all kinds of extracellular matrix proteins, and can also process a number of bioactive molecules. They are known to be involved in the cleavage of cell surface receptors, the release of apoptotic ligands, and chemokine/cytokine inactivation. MMPs are also thought to play a major role in cell behaviors such as cell proliferation, migration (adhesion/dispersion), differentiation, angiogenesis, apoptosis, and host defense.
This peptide is a sensitive substrate for assaying MMP-1, 2, 7, 8, 12 and 13 activities, Abs/Em = 494/521nm.
Sequence:5-FAM-RPKPYA-Nva-WM-K(QXL™ 520)-NH2
MW:2125.4 Da
% peak area by HPLC:95
Storage condition:-20° C
Catalog Number: 103005-938
Supplier: Anaspec Inc


Description: In this protease substrate, collagen is heavily labeled with a fluorescein derivative, resulting in almost total quenching of the conjugate's fluorescence. Protease-catalyzed hydrolysis relieves this quenching conjugate, yielding brightly green fluorescent dye-labeled peptides. The increase in fluorescence intensity is directly proportional to protease activity. Collagen, Type IV should be particularly useful in the development of HTS assays for screening Gelatinase A (MMP-2) and Gelatinase A inhibitors, as well as for other gelatinases and collagenases that specifically degrade (Type IV) Collagen. Additionally, lightly fluorescein-labeled collagen may be useful for continuous assays monitored by fluorescence polarization.
Catalog Number: 103011-294
Supplier: Anaspec Inc


Description: Matrix Metalloproteinases (MMPs) are a large family of endopeptidases. Collectively, MMPs can degrade all kinds of extracellular matrix proteins, and can also process a number of bioactive molecules. They are known to be involved in the cleavage of cell surface receptors, the release of apoptotic ligands, and chemokine/cytokine inactivation. MMPs are also thought to play a major role in cell behaviors such as cell proliferation, migration (adhesion/dispersion), differentiation, angiogenesis, apoptosis, and host defense.
This peptide is a sensitive substrate for assaying MMP-1, 2, 3, 7, 8, 9, 12, and 13 activities, Abs/Em = 494/521 nm.
Sequence:QXL™ 520 -γ-Abu-P-Cha-Abu-Smc-HA-Dab(5-FAM)-AK-NH2 (Smc=S-Methyl-L-cysteine)
MW:1913.1 Da
% peak area by HPLC:95
Storage condition:-20° C
Catalog Number: 103005-942
Supplier: Anaspec Inc


Description: Matrix Metalloproteinases (MMPs) are a large family of endopeptidases. Collectively, MMPs can degrade all kinds of extracellular matrix proteins, and can also process a number of bioactive molecules. They are known to be involved in the cleavage of cell surface receptors, the release of apoptotic ligands, and chemokine/cytokine inactivation. MMPs are also thought to play a major role in cell behaviors such as cell proliferation, migration (adhesion/dispersion), differentiation, angiogenesis, apoptosis, and host defense.
This peptide is a fluorogenic substrate that is best cleaved by MMP-7, 8, 9 and 13. The highly fluorescent Mca moiety is efficiently quenched by energy transfer to the Dnp group. The punctuated metallo proteinase (PUMP, EC 3.4.24.23) cleaves the substrate at the Gly-Leu bond with a 190-fold increase in fluorescence (Abs/Em = 325/393 nm). In human MMP assays, this substrate is about 50 to 100 times more sensitive than the generic MMP substrate, Dnp-PLGLWAr-NH2.
Sequence:Mca-PLGL-Dap(Dnp)-AR-NH2
MW:1093.2 Da
% peak area by HPLC:95
Storage condition:-20° C
Catalog Number: 102996-762
Supplier: Anaspec Inc


Description: NBD-Arg-Pro-Lys-Pro-Leu-Ala-Nva-Trp-Lys(DMC)-NH₂ (NBD-RPKPLA-Nva-WK(DMC) amide) is an excellent fluorogenic substrate for hydrolysis of the matrix metalloproteinase stromelysin (MMP-3). This FRET substrate exhibits high sensitivity and improves accuracy at lower substrate turnover. It has a kcat/Km value of 2.14 x 10⁴ M⁻¹s⁻¹ and can be easily detected at 350 nm (excitation) and 465 nm (emission). Therefore this compound is a suitable tool for high-throughput inhibitor screening.
Catalog Number: M-2300.0001BA
Supplier: Bachem Americas


Description: Matrix Metalloproteinases (MMPs) are a large family of endopeptidases. Collectively, MMPs can degrade all kinds of extracellular matrix proteins, and can also process a number of bioactive molecules. They are known to be involved in the cleavage of cell surface receptors, the release of apoptotic ligands, and chemokine/cytokine inactivation. MMPs are also thought to play a major role in cell behaviors such as cell proliferation, migration (adhesion/dispersion), differentiation, angiogenesis, apoptosis, and host defense.
This peptides is a highly soluble fluorogenic MMP substrate for MMP-2, 8, 12, 13 and 14, containing the MMP cleavable Gly-Leu bond and EDANS/DABCYL. Fluorogenic assays using TNO211 are sensitive and can detect MMP activity in culture medium from endothelial cells and untreated synovial fluid from patients. Abs/Em = 340/490 nm.
Sequence:DABCYL-(γ-Abu)-PQGL-E(EDANS)AK-NH2
MW:1326.5 Da
% peak area by HPLC:95
Storage condition:-20° C
Catalog Number: 102996-712
Supplier: Anaspec Inc


Description: Matrix Metalloproteinases (MMPs) are a large family of endopeptidases. Collectively, MMPs can degrade all kinds of extracellular matrix proteins, and can also process a number of bioactive molecules. They are known to be involved in the cleavage of cell surface receptors, the release of apoptotic ligands, and chemokine/cytokine inactivation. MMPs are also thought to play a major role in cell behaviors such as cell proliferation, migration (adhesion/dispersion), differentiation, angiogenesis, apoptosis, and host defense.
This peptide is a sensitive substrate for assaying MMP-7, 12 and 13 activities, Abs/Em = 494/521 nm.
Sequence:QXL™ 520-PYAYWMRK(5-FAM)-NH2
MW:1963.1 Da
% peak area by HPLC:95
Storage condition:-20° C
Catalog Number: 103003-250
Supplier: Anaspec Inc


Description: ADAMTS proteases are secreted enzymes containing a prometalloprotease domain of the reprolysin type. The ADAMTS proteases function in processing of procollagens and von Willebrand factor as well as catabolism of aggrecan, versican and brevican. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration.A member of the metalloproteinase family containing disintegrin like domains (ADAMs), the function of ADAMTS8 is still poorly understood. ADAMTS8 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active on a range of substrates. ADAMTS8 is inhibited by the endogenous MMP inhibitors, TIMP1, 2, 3 and 4, but most efficiently by TIMP3. In addition to the metalloprotease domain, ADAMTS8 has a propeptide domain, a Prohormone Convertase (PC, furin) cleavage site, a cysteine rich domain and thrombospondin 1 like domains.
Catalog Number: 10425-276
Supplier: Bioss


Description: ADAMTS proteases are secreted enzymes containing a prometalloprotease domain of the reprolysin type. The ADAMTS proteases function in processing of procollagens and von Willebrand factor as well as catabolism of aggrecan, versican and brevican. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration.A member of the metalloproteinase family containing disintegrin like domains (ADAMs), the function of ADAMTS8 is still poorly understood. ADAMTS8 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active on a range of substrates. ADAMTS8 is inhibited by the endogenous MMP inhibitors, TIMP1, 2, 3 and 4, but most efficiently by TIMP3. In addition to the metalloprotease domain, ADAMTS8 has a propeptide domain, a Prohormone Convertase (PC, furin) cleavage site, a cysteine rich domain and thrombospondin 1 like domains.
Catalog Number: 10425-274
Supplier: Bioss


Description: ADAMTS proteases are secreted enzymes containing a prometalloprotease domain of the reprolysin type. The ADAMTS proteases function in processing of procollagens and von Willebrand factor as well as catabolism of aggrecan, versican and brevican. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration.A member of the metalloproteinase family containing disintegrin like domains (ADAMs), the function of ADAMTS8 is still poorly understood. ADAMTS8 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active on a range of substrates. ADAMTS8 is inhibited by the endogenous MMP inhibitors, TIMP1, 2, 3 and 4, but most efficiently by TIMP3. In addition to the metalloprotease domain, ADAMTS8 has a propeptide domain, a Prohormone Convertase (PC, furin) cleavage site, a cysteine rich domain and thrombospondin 1 like domains.
Catalog Number: 76078-622
Supplier: Bioss


Description: ADAMTS proteases are secreted enzymes containing a prometalloprotease domain of the reprolysin type. The ADAMTS proteases function in processing of procollagens and von Willebrand factor as well as catabolism of aggrecan, versican and brevican. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration.A member of the metalloproteinase family containing disintegrin like domains (ADAMs), the function of ADAMTS8 is still poorly understood. ADAMTS8 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active on a range of substrates. ADAMTS8 is inhibited by the endogenous MMP inhibitors, TIMP1, 2, 3 and 4, but most efficiently by TIMP3. In addition to the metalloprotease domain, ADAMTS8 has a propeptide domain, a Prohormone Convertase (PC, furin) cleavage site, a cysteine rich domain and thrombospondin 1 like domains.
Catalog Number: 10425-278
Supplier: Bioss


Description: ADAMTS proteases are secreted enzymes containing a prometalloprotease domain of the reprolysin type. The ADAMTS proteases function in processing of procollagens and von Willebrand factor as well as catabolism of aggrecan, versican and brevican. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration.A member of the metalloproteinase family containing disintegrin like domains (ADAMs), the function of ADAMTS8 is still poorly understood. ADAMTS8 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active on a range of substrates. ADAMTS8 is inhibited by the endogenous MMP inhibitors, TIMP1, 2, 3 and 4, but most efficiently by TIMP3. In addition to the metalloprotease domain, ADAMTS8 has a propeptide domain, a Prohormone Convertase (PC, furin) cleavage site, a cysteine rich domain and thrombospondin 1 like domains.
Catalog Number: 10425-284
Supplier: Bioss


Description: ADAMTS proteases are secreted enzymes containing a prometalloprotease domain of the reprolysin type. The ADAMTS proteases function in processing of procollagens and von Willebrand factor as well as catabolism of aggrecan, versican and brevican. They have been demonstrated to have important roles in connective tissue organization, coagulation, inflammation, arthritis, angiogenesis and cell migration.A member of the metalloproteinase family containing disintegrin like domains (ADAMs), the function of ADAMTS8 is still poorly understood. ADAMTS8 contains the canonical HExxHxxxxxH zinc metalloproteinase motif, and has been shown to be proteolytically active on a range of substrates. ADAMTS8 is inhibited by the endogenous MMP inhibitors, TIMP1, 2, 3 and 4, but most efficiently by TIMP3. In addition to the metalloprotease domain, ADAMTS8 has a propeptide domain, a Prohormone Convertase (PC, furin) cleavage site, a cysteine rich domain and thrombospondin 1 like domains.
Catalog Number: 10425-280
Supplier: Bioss


1 - 2 of 2