Description: JBS True Blue

Description: A competitive ELISA for quantitative measurement of Canine True insulin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: A competitive ELISA for quantitative measurement of Canine True insulin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: A competitive ELISA for quantitative measurement of Canine True insulin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: A competitive ELISA for quantitative measurement of Rabbit True insulin in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. This is a high quality ELISA kit developped for optimal performance with samples from the particular species.

Description: Description of target: Type IV collagenase, 72-kD, is officially designated matrix metalloproteinase-2 (MMP2). It is also known as gelatinase, 72-kD. MMP-2 plays an essential role in angiogenesis and arteriogenesis, two processes critical to restoration of tissue perfusion after ischemia. MMP-2 expression is increased in tissue ischemia, but the responsible mechanisms remain unknown.1 Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability.2 The gene is localized to 16q21 using somatic cell hybrids and in situ hybridization.3 The standard product used in this kit is recombinant rat MMP-2, consisting of 662 amino acids with the molecular mass of 72KDa. The detected MMP-2 includes zymogen and active enzyme.;Species reactivity: Rat;Application: ELISA;Assay info: ;Sensitivity: < 10 pg/ml

Description: Description of target: Type IV collagenase, 72-kD, is officially designated matrix metalloproteinase-2 (MMP2). It is also known as gelatinase, 72-kD. MMP-2 plays an essential role in angiogenesis and arteriogenesis, two processes critical to restoration of tissue perfusion after ischemia. MMP-2 expression is increased in tissue ischemia, but the responsible mechanisms remain unknown.1 Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability.2 The gene is localized to 16q21 using somatic cell hybrids and in situ hybridization.3 The standard product used in this kit is recombinant human MMP-2, consisting of 631 amino acids with the molecular mass of 71KDa. The detected MMP-2 includes zymogen and active enzyme.;Species reactivity: Human;Application: ELISA;Assay info: ;Sensitivity: < 10 pg/mL

Description: Description of target: Type IV collagenase, 72-kD, is officially designated matrix metalloproteinase-2 (MMP2). It is also known as gelatinase, 72-kD. MMP-2 plays an essential role in angiogenesis and arteriogenesis, two processes critical to restoration of tissue perfusion after ischemia. MMP-2 expression is increased in tissue ischemia, but the responsible mechanisms remain unknown.1 Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability.2 The gene is localized to 16q21 using somatic cell hybrids and in situ hybridization.3 The standard product used in this kit is recombinant mouse MMP-2, consisting of 662 amino acids with the molecular mass of 72KDa. The detected MMP-2 includes zymogen and active enzyme.;Species reactivity: Mouse;Application: ELISA;Assay info: ;Sensitivity: < 10 pg/mL

Description: Description of target: ;Species reactivity: Canine;Application: ;Assay info: Assay Type: Quantitative Sandwich ELISA;Sensitivity: 18.75 pg/mL

Description: Enzyme-linked immunosorbent assay kit for quantification of Rat MMP-2 in samples from serum, plasma, tissue homogenates and other biological fluids.

Description: Enzyme-linked immunosorbent assay kit for quantification of Human MMP-2 in samples from serum, plasma, tissue homogenates and other biological fluids.

Description: Enzyme-linked immunosorbent assay kit for quantification of Mouse MMP-2 in samples from serum, plasma, tissue homogenates and other biological fluids.

Description: For quantitative detection of rat MMP-2 in cell culture supernates, serum and plasma(heparin).