Rabbit MMP9(Matrix Metalloproteinase 9) ELISA Kit

Description: A sandwich quantitative ELISA assay kit for detection of Equine Matrix Metalloproteinase 9 (MMP9) in samples from serum, plasma, tissue homogenates or other biological fluids.

Description: A sandwich quantitative ELISA assay kit for detection of Equine Matrix Metalloproteinase 9 (MMP9) in samples from serum, plasma, tissue homogenates or other biological fluids.

Description: A sandwich quantitative ELISA assay kit for detection of Human Matrix Metalloproteinase 9 (MMP9) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

Description: A sandwich quantitative ELISA assay kit for detection of Human Matrix Metalloproteinase 9 (MMP9) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

Description: A sandwich quantitative ELISA assay kit for detection of Mouse Matrix Metalloproteinase 9 (MMP9) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

Description: A sandwich quantitative ELISA assay kit for detection of Mouse Matrix Metalloproteinase 9 (MMP9) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

Description: A sandwich quantitative ELISA assay kit for detection of Porcine Matrix Metalloproteinase 9 (MMP9) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

Description: A sandwich quantitative ELISA assay kit for detection of Porcine Matrix Metalloproteinase 9 (MMP9) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

Description: A sandwich quantitative ELISA assay kit for detection of Rat Matrix Metalloproteinase 9 (MMP9) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

Description: A sandwich quantitative ELISA assay kit for detection of Rat Matrix Metalloproteinase 9 (MMP9) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates or other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rabbit Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rabbit Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rabbit Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Rabbit Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Rabbit Matrix Metalloproteinase 9 (MMP9) in samples from Serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids with no significant corss-reactivity with analogues from other species.

Description: A sandwich ELISA kit for detection of Matrix Metalloproteinase 9 from Rabbit in samples from blood, serum, plasma, cell culture fluid and other biological fluids.

Description: Quantitative sandwich ELISA for measuring Rabbit Matrix metalloproteinase 9 (MMP9) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.

Description: Quantitative sandwich ELISA for measuring Rabbit Matrix metalloproteinase 9 (MMP9) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.

Description: Quantitative sandwich ELISA for measuring Rabbit Matrix metalloproteinase 9 (MMP9) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.

Description: Recombinant Dog Matrix metalloproteinase-9(MMP9) expressed in Yeast

Description: Recombinant Human Matrix metalloproteinase-9(MMP9) ,partial expressed in Yeast

Description: Recombinant Human Matrix Metalloproteinase 9 expressed in: Yeast(Pichia pastor)

Description: Recombinant Mouse Matrix Metalloproteinase 9 expressed in: Yeast

Description: Recombinant Rat Matrix Metalloproteinase 9 expressed in: Yeast

Description: Recombinant Human Matrix Metalloproteinase 9 expressed in: Available from E.coli, Yeast, Baculovirus and Mammalian cells

Description: Recombinant Pig Matrix Metalloproteinase 9 expressed in: Available from E.coli, Yeast, Baculovirus and Mammalian cells

Description: Recombinant Bovine Matrix Metalloproteinase 9 expressed in: E.coli

Description: Recombinant Human Matrix Metalloproteinase 9 expressed in: E.coli

Description: Recombinant Mouse Matrix Metalloproteinase 9 expressed in: E.coli

Description: Recombinant Rat Matrix Metalloproteinase 9 expressed in: E.coli

Description: Recombinant Rabbit Matrix Metalloproteinase 9 expressed in: E.coli

Description: The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.

Description: The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.

Description: The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.

Description: The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.

Description: The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.

Description: The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.

Description: The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.

Description: The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.

Description: The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP-1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.

Description: The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP1 expression.

Description: The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP1 expression.

Description: The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP1 expression.

Description: The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP9 (also designated 92 kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption. MMP1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP1 expression.

Description: May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.;;In the arthritis patient this enzyme might contribute to the pathogenesis of joint destruction and might constitute a useful marker of disease status. [UniProt]

Description: May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.;;In the arthritis patient this enzyme might contribute to the pathogenesis of joint destruction and might constitute a useful marker of disease status. [UniProt]

Description: May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.;;In the arthritis patient this enzyme might contribute to the pathogenesis of joint destruction and might constitute a useful marker of disease status. [UniProt]

Description: May play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.;;In the arthritis patient this enzyme might contribute to the pathogenesis of joint destruction and might constitute a useful marker of disease status. [UniProt]

Description: Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, angiogenesis, bone development, wound healing, cell migration, learning and memory, as well as in pathological processes, such as arthritis, intracerebral hemorrhage, and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens and other extracellular matrix proteins. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. [Wiki]

Description: Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, angiogenesis, bone development, wound healing, cell migration, learning and memory, as well as in pathological processes, such as arthritis, intracerebral hemorrhage, and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens and other extracellular matrix proteins. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. [Wiki]

Description: Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, angiogenesis, bone development, wound healing, cell migration, learning and memory, as well as in pathological processes, such as arthritis, intracerebral hemorrhage, and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens and other extracellular matrix proteins. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. [Wiki]

Description: Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, angiogenesis, bone development, wound healing, cell migration, learning and memory, as well as in pathological processes, such as arthritis, intracerebral hemorrhage, and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens and other extracellular matrix proteins. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. [Wiki]

Description: Quantitativesandwich ELISA kit for measuring Bovine Matrix metalloproteinase-9 (MMP9) in samples from serum, plasma, tissue homogenates. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price.

Description: Quantitativesandwich ELISA kit for measuring Bovine Matrix metalloproteinase-9(MMP9) in samples from serum, plasma, tissue homogenates. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Cattle Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Cattle Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Cattle Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Cattle Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates and other biological fluids.

Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Cattle Matrix Metalloproteinase 9 (MMP9) in samples from serum, plasma, tissue homogenates and other biological fluids with no significant corss-reactivity with analogues from other species.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Dog Matrix Metalloproteinase 9 (MMP9) in serum, plasma and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Dog Matrix Metalloproteinase 9 (MMP9) in serum, plasma and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Dog Matrix Metalloproteinase 9 (MMP9) in serum, plasma and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Dog Matrix Metalloproteinase 9 (MMP9) in serum, plasma and other biological fluids.

Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Dog Matrix Metalloproteinase 9 (MMP9) in samples from Serum, plasma and other biological fluids with no significant corss-reactivity with analogues from other species.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Horse Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Horse Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Horse Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Horse Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates and other biological fluids.

Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Horse Matrix Metalloproteinase 9 (MMP9) in samples from serum, plasma, tissue homogenates and other biological fluids with no significant corss-reactivity with analogues from other species.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Matrix Metalloproteinase 9 (MMP9) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids with no significant corss-reactivity with analogues from other species.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Mouse Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Mouse Matrix Metalloproteinase 9 (MMP9) in samples from serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids with no significant corss-reactivity with analogues from other species.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Pig Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Pig Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Pig Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Pig Matrix Metalloproteinase 9 (MMP9) in serum, plasma, tissue homogenates, cell lysates, cell culture supernates and other biological fluids.