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SB-3CT is a potent and competitive matrix metalloproteinase MMP-2 and MMP-9 inhibitor with Ki values of 13.9 and 600 nM, respectively. SB-3CT has high selectivity for gelatinases. SB-3CT shows blood-brain barrier permeability and has neuroprotective effects and anticancer activity .
Siamycin I (BMY-29304), a 21-residue tricyclic peptide, is a secondary metabolite in actinomycetes. Siamycin I is a HIV fusion inhibitor with ED50s of 0.05 to 5.7 μM for acute HIV type 1 (HIV-1) and HIV-2 infections. Siamycin I inhibits the gelatinase and gelatinase biosynthesis-activating pheromone (GBAP) signaling via the FsrC-FsrA two-component regulatory system in a noncompetitive manner. Siamycin I suppresses the expression of both fsrBDC and gelE-sprE transcripts. Siamycin I, a lasso peptide, interacts with lipid II and inhibits cell wall biosynthesis. Siamycin I, an antibiotic, has the potential for enterococcal infections research .
Lysozyme, Human Neutrophil is found to be present in all three types of human neutrophil granules (azurophil-, specific- and gelatinase granules). Lysozyme, Human Neutrophil takes part in antibacterial activity of leukocytes .
Dnp-PLGLWAr-NH2 is a synthetic collagenase/gelatinase substrate. Dnp-PLGLWAR-NH2 can be used to quantify total MMP activity in APMA-activated conditioned medium samples .
MMP2-IN-4 (compound 3h) is a potent MMP2 inhibitor. MMP2-IN-4 inhibits MMP2, MMP9 and MMP12 with IC50s of 266.74, 402.75 and 1237.39 nM, respectively .
LY52 is an MMP-2 and MMP-9 inhibitor. LY52 can significantly block the proteolytic activity of gelatinases, reducing the expression of MMP-2 and MMP-9 in SKOV3 cells, thereby inhibiting cell invasion. LY52 can also suppress the pulmonary metastasis of Lewis lung carcinoma cells in mice. LY52 may be used in cancer research .
Siamycin I (BMY-29304), a 21-residue tricyclic peptide, is a secondary metabolite in actinomycetes. Siamycin I is a HIV fusion inhibitor with ED50s of 0.05 to 5.7 μM for acute HIV type 1 (HIV-1) and HIV-2 infections. Siamycin I inhibits the gelatinase and gelatinase biosynthesis-activating pheromone (GBAP) signaling via the FsrC-FsrA two-component regulatory system in a noncompetitive manner. Siamycin I suppresses the expression of both fsrBDC and gelE-sprE transcripts. Siamycin I, a lasso peptide, interacts with lipid II and inhibits cell wall biosynthesis. Siamycin I, an antibiotic, has the potential for enterococcal infections research .
Dnp-PLGLWAr-NH2 is a synthetic collagenase/gelatinase substrate. Dnp-PLGLWAR-NH2 can be used to quantify total MMP activity in APMA-activated conditioned medium samples .
MMP-9 Protein, a matrix metalloproteinase, plays a crucial role in localized extracellular matrix breakdown, facilitating leukocyte migration. Its potential involvement in bone osteoclastic resorption is suggested. MMP-9 cleaves KiSS1 and NINJ1, generating their secreted forms. It degrades type IV and type V collagen, producing distinct fragments, and fibronectin, while laminin and Pz-peptide remain unaffected. MMP-9 Protein, Human (P. pastoris, His) is the recombinant human-derived MMP-9 protein, expressed by P. pastoris , with N-6*His labeled tag.
The MMP-9 protein is a matrix metalloproteinase that is critical for local extracellular matrix proteolysis and leukocyte migration. It is suggested that it may be involved in bone osteoclastic resorption. MMP-9 Protein, Human (HEK293, His, solution) is the recombinant human-derived MMP-9 protein, expressed by HEK293 , with C-6*His labeled tag.
MMP-9 Protein, a matrix metalloproteinase, plays a crucial role in localized extracellular matrix breakdown, facilitating leukocyte migration. Its potential involvement in bone osteoclastic resorption is suggested. MMP-9 cleaves KiSS1 and NINJ1, generating their secreted forms. It degrades type IV and type V collagen, producing distinct fragments, and fibronectin, while laminin and Pz-peptide remain unaffected. MMP-9 Protein, Human (HEK293, C-His) is the recombinant human-derived MMP-9 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of MMP-9 Protein, Human (HEK293, C-His) is 689 a.a., with molecular weight of ~82.5 kDa.
The MMP-9 protein is a matrix metalloproteinase that is critical for local extracellular matrix proteolysis and leukocyte migration.It is suggested that it may be involved in bone osteoclastic resorption.MMP-9 Protein, Mouse (HEK293, His) is the recombinant mouse-derived MMP-9 protein, expressed by HEK293 , with C-10*His labeled tag.
The MMP-9 protein is a matrix metalloproteinase that is critical for local extracellular matrix proteolysis and leukocyte migration.It is suggested that it may be involved in bone osteoclastic resorption.MMP-9 Protein, Mouse (HEK293, C-His) is the recombinant mouse-derived MMP-9 protein, expressed by HEK293 , with C-10*His labeled tag.
MMP-9 is an important member of the MMP protein family and regulates the extracellular matrix during physiological processes such as development and tissue remodeling. It involves arthritis and metastasis. MMP-9 Protein, Human (HEK293) is the recombinant human-derived MMP-9 protein, expressed by HEK293 , with tag free. The total length of MMP-9 Protein, Human (HEK293) is 688 a.a., with molecular weight of 80-95 kDa.
The MMP-9 protein is a matrix metalloproteinase that is critical for local extracellular matrix proteolysis and leukocyte migration.It is suggested that it may be involved in bone osteoclastic resorption.MMP-9 Protein, Mouse (HEK293) is the recombinant mouse-derived MMP-9 protein, expressed by HEK293 , with tag free.
rHu72 kDa type IV collagenase/MMP-2, His ; 72 kDa Type IV Collagenase; 72 kDa gelatinase; gelatinase A; Matrix Metalloproteinase-2; MMP-2; TBE-1; MMP2; CLG4A
MMP-2 protein is a multifunctional metalloproteinase that actively participates in physiological processes such as vascular remodeling, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. In addition to degrading extracellular matrix proteins, it also acts on non-matrix proteins to promote vasoconstriction. MMP-2 Protein, Human (HEK293, His) is the recombinant human-derived MMP-2 protein, expressed by HEK293 , with C-6*His labeled tag. The total length of MMP-2 Protein, Human (HEK293, His) is 631 a.a., with molecular weight of 68-78 kDa.
rHu72 kDa type IV collagenase/MMP-2, His ; 72 kDa Type IV Collagenase; 72 kDa gelatinase; gelatinase A; Matrix Metalloproteinase-2; MMP-2; TBE-1; MMP2; CLG4A
MMP-2 protein is a multifunctional metalloproteinase that actively participates in physiological processes such as vascular remodeling, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. In addition to degrading extracellular matrix proteins, it also acts on non-matrix proteins to promote vasoconstriction. Animal-Free MMP-2 Protein, Human (His) is the recombinant human-derived animal-FreeMMP-2 protein, expressed by E. coli , with C-His labeled tag. The total length of Animal-Free MMP-2 Protein, Human (His) is 551 a.a., with molecular weight of ~63.00 kDa.
The MMP-9 protein is a matrix metalloproteinase that is critical for local extracellular matrix proteolysis and leukocyte migration. It is suggested that it may be involved in bone osteoclastic resorption. MMP-9 Protein, Cynomolgus (HEK293, His) is the recombinant cynomolgus-derived MMP-9 protein, expressed by HEK293 , with C-His labeled tag. The total length of MMP-9 Protein, Cynomolgus (HEK293, His) is 687 a.a., with molecular weight of 85-100 kDa.
rHu72 kDa type IV collagenase/MMP-2, His ; 72 kDa Type IV Collagenase; 72 kDa gelatinase; gelatinase A; Matrix Metalloproteinase-2; MMP-2; TBE-1; MMP2; CLG4A
MMP-2 is a multifunctional metalloproteinase that plays multiple roles in vasculature remodeling, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. In addition to degrading extracellular matrix proteins, MMP-2 also acts on non-matrix proteins to promote vasoconstriction. MMP-2 Protein, Rat (P. pastoris, His) is the recombinant rat-derived MMP-2 protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of MMP-2 Protein, Rat (P. pastoris, His) is 553 a.a., with molecular weight of 64.1 kDa.
Matrix metalloproteinase-9 (Mmp9) is a member of the matrix metalloproteinase (MMP) family. Mmp9 is secreted as inactive proproteins which are activated when cleaved by extracellular proteinases to generate a mature, zinc-dependent endopeptidase enzyme that degrades collagens of type IV, V and XI, and elastin. Mmp9 is also involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow. MMP-9 Protein, Rat (HEK293, His) is the recombinant rat-derived MMP-9 protein, expressed by HEK293 , with C-10*His labeled tag. The total length of MMP-9 Protein, Rat (HEK293, His) is 689 a.a., with molecular weight of approximately 95 kDa.
MMP-9 Protein, a matrix metalloproteinase, plays a crucial role in localized extracellular matrix breakdown, facilitating leukocyte migration. Its potential involvement in bone osteoclastic resorption is suggested. MMP-9 cleaves KiSS1 and NINJ1, generating their secreted forms. It degrades type IV and type V collagen, producing distinct fragments, and fibronectin, while laminin and Pz-peptide remain unaffected. MMP-9 Protein, Human (HEK293, His-Avi) is the recombinant human-derived MMP-9 protein, expressed by HEK293 , with C-Avi, C-His labeled tag. The total length of MMP-9 Protein, Human (HEK293, His-Avi) is 688 a.a., with molecular weight of 85-100 kDa.
MMP-9 Protein, a matrix metalloproteinase, plays a crucial role in localized extracellular matrix breakdown, facilitating leukocyte migration. Its potential involvement in bone osteoclastic resorption is suggested. MMP-9 cleaves KiSS1 and NINJ1, generating their secreted forms. It degrades type IV and type V collagen, producing distinct fragments, and fibronectin, while laminin and Pz-peptide remain unaffected. MMP-9 Protein, Human (Biotinylated, HEK293, His-Avi) is the recombinant human-derived MMP-9 protein, expressed by HEK293 , with C-Avi, C-His labeled tag. The total length of MMP-9 Protein, Human (Biotinylated, HEK293, His-Avi) is 688 a.a., with molecular weight of 95-105 kDa.
MMP-2 protein is a multifunctional metalloproteinase that actively participates in physiological processes such as vascular remodeling, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. In addition to degrading extracellular matrix proteins, it also acts on non-matrix proteins to promote vasoconstriction. MMP-2 Protein, Human (HEK293) is the recombinant human-derived MMP-2 protein, expressed by HEK293 , with tag free.
Lipocalin-2/NGAL is a multifaceted iron transporter involved in multiple biological processes, including apoptosis, innate immunity, and kidney development. Lipocalin-2 dynamically affects cellular iron concentration through binding to the siderophore 2,3-dihydroxybenzoate. Lipocalin-2/NGAL Protein, Cynomolgus (CHO, His) is the recombinant cynomolgus-derived Lipocalin-2/NGAL protein, expressed by CHO , with C-His labeled tag.
MMP-2 protein is a ubiquitous metalloprotease that contributes to vasculature remodeling, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. In addition to extracellular matrix degradation, it also targets non-matrix proteins and promotes vasoconstriction. MMP-2 Protein, Mouse (HEK293, His) is the recombinant mouse-derived MMP-2 protein, expressed by HEK293 , with N-His labeled tag.
Lipocalin-2/NGAL is a multifaceted iron transporter involved in multiple biological processes, including apoptosis, innate immunity, and kidney development. Lipocalin-2 dynamically affects cellular iron concentration through binding to the siderophore 2,3-dihydroxybenzoate. Lipocalin-2/NGAL Protein, Rat (sf9, His) is the recombinant rat-derived Lipocalin-2/NGAL protein, expressed by Sf9 insect cells , with C-His labeled tag.
Lipocalin-2/NGAL Protein, Mouse (HEK293, His) is an 20-28 kDa NGAL protein with a His-flag, which is expressed in HEK293 cells. NGAL is an antibacterial factor of natural immunity, and an acute-phase protein.
Lipocalin-2/NGAL Protein, Mouse (HEK293, His) is an 20-28 kDa NGAL protein with a His-flag, which is expressed in HEK293 cells. NGAL is an antibacterial factor of natural immunity, and an acute-phase protein.
Lipocalin-2/NGAL is an iron transporter that plays a crucial role in various cellular processes. It interacts with the siderophore 2,3-DHBA to transport iron into or out of cells depending on cellular needs. Lipocalin-2/NGAL Protein, Human (HEK293, His) is the recombinant human-derived Lipocalin-2/NGAL protein, expressed by HEK293 , with C-6*His labeled tag.
MMP9; CLG4B; Matrix metalloproteinase-9; MMP-9; 92 kDa gelatinase; 92 kDa type IV collagenase; gelatinase B; GELB
WB, IHC-P, ICC/IF
Human, Mouse, Rat
MMP9 Antibody is a non-conjugated and Rabbit origined polyclonal antibody about 78 kDa, targeting to MMP9. It can be used for WB,IHC-P,ICC/IF assays with tag free, in the background of Human, Mouse, Rat.
FAP; Seprase; 170 kDa melanoma membrane-bound gelatinase; Fibroblast activation protein alpha; Integral membrane serine protease
WB, IHC-P
Human
FAP Antibody (YA1090) is a rabbit-derived non-conjugated IgG antibody (Clone NO.: YA1090), targeting FAP, with a predicted molecular weight of Calculated band size: 88 kDa (observed band size: 95 kDa). FAP Antibody (YA1090) can be used for WB, IHC-P experiment in human background.
FAP; Seprase; 170 kDa melanoma membrane-bound gelatinase; Fibroblast activation protein alpha; Integral membrane serine protease
IHC-P, FC, ELISA
Human
FAP Antibody (YA1442) is a mouse-derived non-conjugated IgG1 antibody (Clone NO.: YA1442), targeting FAP. FAP Antibody (YA1442) can be used for IHC-P, FC, ELISA experiment in human background.
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