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方案
≥90% (SDS-PAGE)
质量水平
表单
liquid
比活
≥15 mU/mg protein
制造商/商品名称
Calbiochem®
储存条件
OK to freeze
avoid repeated freeze/thaw cycles
异质活性
other MMP activity, none detected
运输
wet ice
储存温度
−70°C
一般描述
M.W. 56,000/52,000. Note: 1 mU = 1 milliunit.
Native proMMP-1 from cultured, human rheumatoid synovial fibroblast. Corresponds to the 56 kDa/52 kDa enzyme. May contain some activated enzyme but requires activation by APMA (Cat. No. 164610) for 30 - 60 min. at 30°C just prior to use to obtain fully activated enzyme (46 kDa/42 kDa). May also undergo autocatalysis to yield a 27 kDa/22 kDa active enzyme. Expressed by a large number of cell types. Cleaves fibrillar type I collagen.
包装
Please refer to vial label for lot-specific concentration.
警告
Toxicity: Standard Handling (A)
单位定义
One unit is defined as the amount of enzyme that will hydrolyze 1.0 µmol 2,4-DNP-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min at 37°C pH 7.0.
外形
In 300 mM NaCl, 50 mM Tris-HCl, 5 mM CaCl₂, 1 µM ZnCl₂, 0.05% Brij® 35 Detergent, 0.05% NaN₃, pH 7.0.
制备说明
Prepared from culture medium of human rheumatoid synovial fibroblasts that has been shown by certified tests to be negative for HBsAg and for antibodies to HIV and HCV.
重悬
Following initial thaw, aliquot and freeze (-70°C).
其他说明
Liepinsh, E., et al. 2003. J. Biol. Chem.278, 25982.
Pilcher, B.K., et al. 1997. J. Cell Biol. 137, 1445.
Vallon, R., et al. 1997. Eur. J. Biochem. 244, 81.
Marcy, A.I., et al. 1991. Biochemistry30, 6476.
Stricklin, et al. 1983. Biochemistry22, 61.
Pilcher, B.K., et al. 1997. J. Cell Biol. 137, 1445.
Vallon, R., et al. 1997. Eur. J. Biochem. 244, 81.
Marcy, A.I., et al. 1991. Biochemistry30, 6476.
Stricklin, et al. 1983. Biochemistry22, 61.
法律信息
Brij is a registered trademark of Croda International PLC
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
储存分类代码
10 - Combustible liquids
WGK
WGK 1
闪点(°F)
Not applicable
闪点(°C)
Not applicable
Yejiao Shi et al.
Biomaterials science, 7(12), 5132-5142 (2019-10-03)
Matrix metalloproteinases (MMPs) are a family of endopeptidases capable of degrading extracellular matrix (ECM) components. They are known to play crucial roles during the ECM turnover in both physiological and pathological processes. As such, their activities are utilized as biological
Tatiana N Demidova-Rice et al.
Wound repair and regeneration : official publication of the Wound Healing Society [and] the European Tissue Repair Society, 19(1), 59-70 (2010-12-08)
Studies in our laboratory indicate that collagenase from Clostridium histolyticum promotes endothelial cell and keratinocyte responses to injury in vitro and wound healing in vivo. We postulate that matrix degradation by Clostridial collagenase creates bioactive fragments that can stimulate cellular
Takwi Nkyimbeng et al.
PloS one, 8(9), e73279-e73279 (2013-09-12)
Idiopathic pulmonary fibrosis (IPF) is a fatal disease characterized by excessive deposition of extracellular matrix (ECM). We investigated the regulation of matrix metalloproteinases (MMPs) and their inhibitors (TIMPs) in lung fibrosis. MMP and TIMP expression, collagenolytic activity and collagen content
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