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PF140 MMP-9, Active, Human, Recombinant

MMP-9, Active, Human, Recombinant MSDS (material safety data sheet) or SDS, CoA and CoQ, dossiers, brochures and other available documents.

同义词: Gelatinase B (67 kDa), Matrix Metalloproteinase-9 (67 kDa)

PF140
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概述

Replacement Information

Products

产品目录编号包装 数量 / 包装
PF140-5UGCN 塑胶安瓿;塑胶针药瓶 5 μg
Description
OverviewRecombinant, human MMP-9 with a truncated C-terminal hemopexin domain expressed as proenzyme that is activated by APMA. AMPA is removed through a Biogel-P6 column and active MMP-9 is purified.
Catalogue NumberPF140
Brand Family Calbiochem®
SynonymsGelatinase B (67 kDa), Matrix Metalloproteinase-9 (67 kDa)
References
ReferencesParsons, S.L., et al. 1997. Br. J. Surg. 84, 160.
Backstrom, J.R., et al. 1996. J. Neuro. 16, 7910.
Lim, G.P., et al. 1996. J Neurochem. 67.
Xia, T., et al. 1996. Biochim. Biophys. 1293, 259.
Sang, Q.X., et al. 1995. Biochim. Biophys. 1251, 99.
Zempo, N., et al. 1994. J. Vasc. Surg. 20, 209.
Birkedal-Hansen, H. 1993. J. Periodontol 64, 474.
Stetler-Stevenson, W.G., et al. 1993. FASEB J. 7, 1434.
Jeffrey, J.J. 1991. Semin. Perinatol. 15, 118.
Liotta, L.A., et al. 1991. Cell 64, 327.
Harris, E. 1990. N. Engl. J. Med. 322, 1277.
Product Information
ActivityΔA₄₀₅/h/µg protein within the range of 20.0 to 60.0 in a standard thiopeptide hydrolysis assay
FormLiquid
FormulationIn 50 mM Hepes, 10 mM CaCl₂, 20% glycerol, 0.005% BRIJ® 35 Detergent, pH 7.5.
PreservativeNone
Quality LevelMQ100
Applications
Application NotesImmunoblotting (1μg protein/lane)
Zymography (0.1 μg protein/lane, see application references)
Application CommentsThe substrate specificity for MMP-9 is collagen (types IV, V, VII, and X), elastin, and gelatin (type I).
Biological Information
Concentration Label Please refer to vial label for lot-specific concentration
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Dry Ice Only
Toxicity Standard Handling
Storage ≤ -70°C
Avoid freeze/thaw Avoid freeze/thaw
Do not freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
产品目录编号 GTIN
PF140-5UGCN 04055977226935

Documentation

MMP-9, Active, Human, Recombinant MSDS

职位

物料安全数据表 (MSDS) 

MMP-9, Active, Human, Recombinant 分析证书

标题批号
PF140

参考

参考信息概述
Parsons, S.L., et al. 1997. Br. J. Surg. 84, 160.
Backstrom, J.R., et al. 1996. J. Neuro. 16, 7910.
Lim, G.P., et al. 1996. J Neurochem. 67.
Xia, T., et al. 1996. Biochim. Biophys. 1293, 259.
Sang, Q.X., et al. 1995. Biochim. Biophys. 1251, 99.
Zempo, N., et al. 1994. J. Vasc. Surg. 20, 209.
Birkedal-Hansen, H. 1993. J. Periodontol 64, 474.
Stetler-Stevenson, W.G., et al. 1993. FASEB J. 7, 1434.
Jeffrey, J.J. 1991. Semin. Perinatol. 15, 118.
Liotta, L.A., et al. 1991. Cell 64, 327.
Harris, E. 1990. N. Engl. J. Med. 322, 1277.
数据表

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision18-September-2008 RFH
SynonymsGelatinase B (67 kDa), Matrix Metalloproteinase-9 (67 kDa)
ApplicationImmunoblotting (1μg protein/lane)
Zymography (0.1 μg protein/lane, see application references)
DescriptionRecombinant, human MMP-9 with a truncated C-terminal hemopexin domain expressed as proenzyme that is activated by APMA. AMPA is removed through a Biogel-P6 column and active MMP-9 is purified. The substrate specificity for MMP-9 is collagen (types IV, V, VII, and X), elastin, and gelatin (type I). Useful for immunoblotting, substrate cleavage assay, and zymography.

Matrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease, and vascular processes such as angiogenesis, intimal hyperplasia, atherosclerosis and aneurysms. Recently, MMPs have been linked to neurodegenerative diseases such as Alzheimer’s, and amyotrophic lateral sclerosis (ALS). Natural inhibitors of MMPs, tissue inhibitor of matrix metalloproteinases (TIMPs) exist and synthetic inhibitors have been developed which offer hope of new treatment options for these diseases. Regulation of MMP activity can occur at the level of gene expression, including transcription and translation, level of activation, or at the level of inhibition by TIMPs. Thus, perturbations at any of these points can theoretically lead to alterations in ECM turnover. Expression is under tight control by pro- and anti-inflammatory cytokines and/or growth factors and, once produced the enzymes are usually secreted as inactive zymograms. Upon activation (removal of the inhibitory propeptide region of the molecules) MMPs are subject to control by locally produced TIMPs. All MMPs can be activated in vitro with organomercurial compounds (e.g., 4-aminophenylmercuric acetate), but the agents responsible for the physiological activation of all MMPs have not been clearly defined. Numerous studies indicate that members of the MMP family have the ability to activate one another. The activation of the MMPs in vivo is likely to be a critical step in terms of their biological behavior, because it is this activation that will tip the balance in favor of ECM degradation. The hallmark of diseases involving MMPs appear to be stoichiometric imbalance between active MMPs and TIMPs, leading to excessive tissue disruption and often degradation. Determination of the mechanisms that control this imbalance may open up some important therapeutic options of specific enzyme inhibitors.
BackgroundMatrix metalloproteinases are members of a unique family of proteolytic enzymes that have a zinc ion at their active sites and can degrade collagens, elastin and other components of the extracellular matrix (ECM). These enzymes are present in normal healthy individuals and have been shown to have an important role in processes such as wound healing, pregnancy, and bone resorption. However, overexpression and activation of MMPs have been linked with a range of pathological processes and disease states involved in the breakdown and remodeling of the ECM. Such diseases include tumor invasion and metastasis, rheumatoid arthritis, periodontal disease, and vascular processes such as angiogenesis, intimal hyperplasia, atherosclerosis and aneurysms. Recently, MMPs have been linked to neurodegenerative diseases such as Alzheimer’s, and amyotrophic lateral sclerosis (ALS). Natural inhibitors of MMPs, tissue inhibitor of matrix metalloproteinases (TIMPs) exist and synthetic inhibitors have been developed which offer hope of new treatment options for these diseases. Regulation of MMP activity can occur at the level of gene expression, including transcription and translation, level of activation, or at the level of inhibition by TIMPs. Thus, perturbations at any of these points can theoretically lead to alterations in ECM turnover. Expression is under tight control by pro- and anti-inflammatory cytokines and/or growth factors and, once produced the enzymes are usually secreted as inactive zymograms. Upon activation (removal of the inhibitory propeptide region of the molecules) MMPs are subject to control by locally produced TIMPs. All MMPs can be activated in vitro with organomercurial compounds (e.g., 4-aminophenylmercuric acetate), but the agents responsible for the physiological activation of all MMPs have not been clearly defined. Numerous studies indicate that members of the MMP family have the ability to activate one another. The activation of the MMPs in vivo is likely to be a critical step in terms of their biological behavior, because it is this activation that will tip the balance in favor of ECM degradation. The hallmark of diseases involving MMPs appear to be stoichiometric imbalance between active MMPs and TIMPs, leading to excessive tissue disruption and often degradation. Determination of the mechanisms that control this imbalance may open up some important therapeutic options of specific enzyme inhibitors.
FormLiquid
FormulationIn 50 mM Hepes, 10 mM CaCl₂, 20% glycerol, 0.005% BRIJ® 35 Detergent, pH 7.5.
Concentration Label Please refer to vial label for lot-specific concentration
Recommended reaction conditionsZymography Xia, T., et al. 1996. Biochim. Biophys. 1293, 259. Kleiner, D.E. and Stetler-Stevenson W.G. 1994. Anal. Biochem. 218, 325. Heussen, C. and Dowdle, E.B. 1980. Anal. Biochem. 102, 196. Substrate Cleavage Assay Xia, T., et al. 1996. Biochim. Biophys. 1293, 259.
ActivityΔA₄₀₅/h/µg protein within the range of 20.0 to 60.0 in a standard thiopeptide hydrolysis assay
PreservativeNone
CommentsThe substrate specificity for MMP-9 is collagen (types IV, V, VII, and X), elastin, and gelatin (type I).
Storage Avoid freeze/thaw
≤ -70°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Toxicity Standard Handling
ReferencesParsons, S.L., et al. 1997. Br. J. Surg. 84, 160.
Backstrom, J.R., et al. 1996. J. Neuro. 16, 7910.
Lim, G.P., et al. 1996. J Neurochem. 67.
Xia, T., et al. 1996. Biochim. Biophys. 1293, 259.
Sang, Q.X., et al. 1995. Biochim. Biophys. 1251, 99.
Zempo, N., et al. 1994. J. Vasc. Surg. 20, 209.
Birkedal-Hansen, H. 1993. J. Periodontol 64, 474.
Stetler-Stevenson, W.G., et al. 1993. FASEB J. 7, 1434.
Jeffrey, J.J. 1991. Semin. Perinatol. 15, 118.
Liotta, L.A., et al. 1991. Cell 64, 327.
Harris, E. 1990. N. Engl. J. Med. 322, 1277.