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ALX-200-005 Revised 12-Apr-07
Calmodulin (human brain) (high purity)
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SYNONYMS CaM (human brain) (high purity)
Phosphodiesterase 3':5'-cyclic Nucleotide Activator (human brain) (high purity)
PRODUCT LINE Signal Transduction
PRODUCT CATEGORY Calmodulins
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ALX-200-005-C500   500 µg 135.00 USD Add To Cart
Product Specification
CAS NUMBER: 73298-54-1
MERCK INDEX: 14: 1719
SOURCE/HOST: Isolated from human brain. Tested negative for infectious diseases.
PURITY: ≥95% (native reducing PAGE in presence of EGTA)
PURITY DETAIL: Ion-exchange chromatography and gel filtration.
FORMULATION: Lyophilized. Contains 2mM EDTA.
RECONSTITUTION: Reconstitute with distilled water.
SPECIFIC ACTIVITY: ~40'000U/mg protein. One unit is defined as the amount of calmodulin that stimulates 0.016 activated units of phosphodiesterase 3':5'-cyclic nucleotide (Prod. No. ALX-202-035) to 50% of the maximum activity of the enzyme when saturated with activator, in the presence of 0.01mM Ca2+ at 30°C, pH 7.5.
SHIPPING: SHIPPED ON BLUE ICE
LONG TERM STORAGE: -20°C
General Information
BACKGROUND/TECHNICAL INFORMATION Swiss-Prot link P02593: Calmodulin (human)
AfCS Signalling Gateway link A000452: Calmodulin I (mouse)
Further Categories Containing This Product:
Natural Proteins
 
 
ALX-200-082 Revised 14-Sep-06
Vitronectin (human)
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PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY Vitronectin / Related Products
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ALX-200-082-C100   100 µg 295.00 USD Add To Cart
Product Specification
MW: Bands of ~65kDa and ~75kDa are detected, which both have cell adhesion activity.
SOURCE/HOST: Isolated from human plasma. Negative for HBs antigen and HIV antibody.
CONCENTRATION: 1mg/ml
PURITY: ≥95% (SDS-PAGE). 
PURITY DETAIL: Purified by heparin-agarose column in 8M urea and sterilized by 0.22µm-filtration.
FORMULATION: Liquid. In sterile 0.15M PBS, pH 7.4.
ACTIVITY: Cell adhesion activity to NRK-49F cells is observed at concentrations ≥0.5µg/ml.
SHIPPING: SHIPPED ON BLUE ICE
LONG TERM STORAGE: -20°C
HANDLING: Avoid freeze/thaw cycles.
Product Description
Multifunctional adhesion glycoprotein with binding sites for e.g. collagen, heparin, perforin and integrins. Vitronectin is a ligand for the Ca2+-dependent CD41/CD61 complex, the major integrin of platelets.
Product Specific Literature References
Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin: S. Suzuki, et al.; EMBO J. 4, 2519 (1985) Abstract
Structure and biological role of vitronectin: K.T. Preissner; Ann. Rev. Cell Biol. 7, 275 (1991) Abstract
Vitronectin and its receptors: B. Felding-Habermann & D.A. Cheresh; Curr. Opin. Cell Biol. 5, 864 (1993) Abstract
General Information
BACKGROUND/TECHNICAL INFORMATION

Activity Assay:
1) Serially dilute Vitronectin 10-fold with PBS. Place 100µl of each dilution in a microtiter plate, cover and incubate at 37°C for 2 hours.
2) After washing wells with PBS, add 200µl of 1% BSA-PBS solution and incubate at 37°C for 1 hour.
3) After washing wells with PBS, incubate the coated wells with NRK-49F cells suspended in SF-DMEM (Serum Free-Dulbecco’s Modified Eagle Medium) at 37°C for 4 hours under 5% CO2.
4) Check cells by microscope.

Swiss-Prot link P04004: Vitronectin (human) (precursor)
AfCS Signalling Gateway link 002367: Vitronectin (mouse)
Further Categories Containing This Product:
Natural Proteins
 
 
ALX-200-087 Revised 18-Dec-06
Cystatin C (human)
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PRODUCT LINE Signal Transduction
PRODUCT CATEGORY Cystatins / Related Products
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ALX-200-087-C100   100 µg 235.00 USD Add To Cart
Product Specification
MW: ~13.3kDa
SOURCE/HOST: Isolated from human urine.
PURITY: ≥96% (SDS-PAGE)
PURITY DETAIL: All starting materials used were tested negative for HIV 1 and 2 antibodies, hepatitis B surface antigen and HCV antibodies.
FORMULATION: Lyophilized from 0.05M acetate buffer, pH 4.5.
RECONSTITUTION: Reconstitute with 0.1M acetate buffer, pH 4.5.
SHIPPING: SHIPPED ON BLUE ICE
LONG TERM STORAGE: -20°C
USE/STABILITY: Stable for at least 2 years after receipt when stored at -20°C.
Further Categories Containing This Product:
Natural Proteins
 
 
ALX-200-088 Revised 26-Mar-08
TGF-β1 (human)
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PRODUCT LINE Chemokines & Cytokines
PRODUCT CATEGORY Transforming Growth Factor beta [TGFbeta] & Receptors / Related Products
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ALX-200-088-C002   2 µg 240.00 USD Add To Cart
Product Specification
MW: 12.5kDa for one subunit.
SOURCE/HOST: Human platelets tested negative for HBsAG-, HCV- and HIV-antibodies.
CONCENTRATION: 10μg/ml (determined by induction of 5-lipoxygenase activity in Mono Mac 6 cells)
PURITY: ≥95% (SDS-PAGE)
PURITY DETAIL: Acid-ethanol extraction of platelets followed by gel filtration and cation exchange column chromatography.
FORMULATION: Liquid. In 25% actonitrile containing 0.1% BSA and 0.1% trifluoroacetic acid.
SHIPPING: SHIPPED ON BLUE ICE
SHORT TERM STORAGE: +4°C
LONG TERM STORAGE: -20°C
USE/STABILITY: Stable for at least 3 months when stored at +4°C.
HANDLING: Avoid freeze/thaw cycles.
Further Categories Containing This Product:
Natural Proteins
 
 
ALX-200-089 Revised 18-Mar-08
Ceruloplasmin (human)
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SYNONYMS Ferroxidase (human)
PRODUCT LINE Nitric Oxide Pathway
PRODUCT CATEGORY Nitric Oxide Pathway Other Products
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ALX-200-089-M001   1 mg 210.00 USD Add To Cart
Product Specification
MW: ~134kDa
CAS NUMBER: 9031-37-2
EC: 1.16.3.1
MERCK INDEX: 14: 2006
SOURCE/HOST: Isolated from human plasma.
CONCENTRATION: 1mg/ml after reconstitution.
PURITY: ≥95% (SDS-PAGE)
PURITY DETAIL: Plasma has been tested negative for HBsAg and for antibodies to HIV and HCV.
FORMULATION: Lyophilized from 50mM potassium phosphate, pH 6.8, containing 100mM potassium chloride, 20mM ε-aminocaproic acid and 5mM EDTA.
RECONSTITUTION: Reconstitute with water.
SHIPPING: SHIPPED ON BLUE ICE
LONG TERM STORAGE: -20°C
Product Description
Serum copper transport and iron-oxidizing protein. Expressed in plasma at concentrations of 1-5µM. Contains six copper centers and is known to oxidize amines in a process coupled to the reduction of molecular oxygen. Has ferroxidase activity that is responsible for the oxidation of ferrous iron to its ferric form, which is necessary for efficient iron efflux from the cell (e.g. during hypoxia). Has previously been considered a target for nitric oxide (NO) and an inhibitor of endothelial nitric oxide synthase (eNOS/NOS III). Catalyzes S-nitrosothiol formation in cell culture media. Is a NO oxidase and nitrite synthase that determines endocrine NO homeostasis.
Product Specific Literature References
The reaction of nitric oxide with ceruloplasmin: R. Wever, et al.; Biochim. Biophys. Acta 302, 236 (1973) Abstract
Copper transport: an overview: E.D. Harris; Proc. Soc. Exp. Biol. Med. 196, 130 (1991) Abstract
Ceruloplasmin inhibits carbonyl formation in endogenous cell proteins: J.A. Krsek-Staples & R.O. Webster; Free Radic. Biol. Med. 14, 115 (1993) Abstract
Antioxidant protection against organic and inorganic oxygen radicals by normal human plasma: the important primary role for iron-binding and iron-oxidising proteins: J.M. Gutteridge & G.J. Quinlan; Biochim. Biophys. Acta 1156, 144 (1993) Abstract
Inhibition of endothelial nitric-oxide synthase by ceruloplasmin: A. Bianchini, et al.; J. Biol. Chem. 274, 20265 (1999) Abstract; Full Text
The reactions of copper proteins with nitric oxide: J. Torres and M.T. Wilson; Biochim. Biophys. Acta 1411, 310 (1999) Abstract
Role of ceruloplasmin in macrophage iron efflux during hypoxia: J. Sarkar, et al.; J. Biol. Chem. 278, 44018 (2003) Abstract; Full Text
Does oxidative stress change ceruloplasmin from a protective to a vasculopathic factor?: N. Shukla, et al.; Atherosclerosis 187, 238 (2006) Abstract
Ceruloplasmin is a NO oxidase and nitrite synthase that determines endocrine NO homeostasis: S. Shiva, et al.; Nat. Chem. Biol. 2, 486 (2006) Abstract
General Information
BACKGROUND/TECHNICAL INFORMATION Swiss-Prot link P00450: Ceruloplasmin (human) [Precursor]
Further Categories Containing This Product:
Natural Proteins • Serum Proteins Other Products
 
 
ALX-200-310 Revised 27-Jun-06
Cathepsin G (human neutrophils)
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PRODUCT LINE Cancer
PRODUCT CATEGORY Cathepsins
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ALX-200-310-C100   100 µg 190.00 USD Add To Cart
Product Specification
MW: ~23.5kDa.
EC: 3.4.21.20
MERCK INDEX: 14: 1905
SOURCE/HOST: Isolated from whole human blood (from single donors). Negative for HBSAG-, HCV- and HIV-antibodies.
PURITY: ≥95% (SDS-PAGE)
PURITY DETAIL: Essentially salt free.
FORMULATION: Lyophilized.
RECONSTITUTION: Reconstitute with 50mM sodium acetate, pH 5.5, containing 150mM sodium chloride.
SPECIFIC ACTIVITY: ~2-4U/mg protein. One unit is defined as the amount of enzyme that hydrolyzes 1µmol Suc-Ala-Ala-Pro-Phe-pNA (1mM) per min. at 25°C in 160mM TRIS/HCl and 1.6M NaCl, pH 7.4.
SHIPPING: SHIPPED ON BLUE ICE
LONG TERM STORAGE: -20°C
Product Specific Literature References
Isolation, characterization, and amino-terminal amino acid sequence analysis of human neutrophil cathepsin G from normal donors: L.W. Heck, et al.; Anal. Biochem. 158, 217 (1986) Abstract
General Information
BACKGROUND/TECHNICAL INFORMATION Swiss-Prot link P08311: Cathepsin G (human) (precursor)
AfCS Signalling Gateway link A000512: Cathepsin G (mouse)
Further Categories Containing This Product:
Natural Proteins • Enzymes
 
 
ALX-200-314 Revised 27-Jun-06
Cathepsin L (human)
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PRODUCT LINE Cancer
PRODUCT CATEGORY Cathepsins
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ALX-200-314-1   1 Vial 270.00 USD Add To Cart
Product Specification
MW: ~29kDa.
EC: 3.4.22.15
MERCK INDEX: 14: 1905
SOURCE/HOST: Isolated from human liver. Negative for HBSAG-, HCV- and HIV-antibodies.
QUANTITY: 25µg
PURITY: ≥95% (SDS-PAGE)
FORMULATION: Liquid. In 20mM malonate buffer, pH 5.5, containing 1mM EDTA and 400mM sodium chloride.
SPECIFIC ACTIVITY: ≥0.5U/mg protein. One unit is defined as the amount of enzyme that hydrolyzes 1µmol Z-Phe-Arg-AFC (Prod. No. ALX-260-129) per min. at 25°C in 400mM Na acetate, pH 5.5 with 4mM EDTA and 8mM DTT.
SHIPPING: SHIPPED ON DRY ICE
LONG TERM STORAGE: -80°C
Product Description
The most powerful of the lysosomal proteinases. It has a higher specific activity than cathepsin B and H in the degradation of a variety of physiological protein substrates.
Product Specific Literature References
Cathepsin B, Cathepsin H, and cathepsin L: A.J. Barrett & H. Kirschke; Methods Enzymol. 80 Pt C, 535 (1981) Abstract
Active center differences between cathepsins L and B: the S1 binding region: H. Kirschke, et al.; FEBS Lett 228, 128 (1988) Abstract
Complete nucleotide and deduced amino acid sequences of human and murine preprocathepsin L. An abundant transcript induced by transformation of fibroblasts: L.J. Joseph, et al.; J. Clin. Invest. 81, 1621 (1988) Abstract
The role of lysosomal proteinases in MHC class II-mediated antigen processing and presentation: T.Y. Nakagawa & A.Y. Rudensky; Immunol. Rev. 172, 121 (1999) Abstract
Proteases involved in MHC class II antigen presentation: J.A. Villadangos, et al.; Immunol. Rev. 172, 109 (1999) Abstract
Distinct roles of cathepsin K and cathepsin L in osteoclastic bone resorption: N. Furuyama & Y. Fujisawa; Endocr. Res. 26, 189 (2000) Abstract
General Information
BACKGROUND/TECHNICAL INFORMATION May contain trace cathepsin B contaminant (<1.5U/mg protein using Z-Arg-Arg-β-NA as a substrate. One unit is defined as the amount of enzyme that hydrolyzes 1µmol of 2-naphtylamine per min. at 40°C, pH 6.0. Please note that the specific activity of pure cathepsin B is >200U/mg protein)

Swiss-Prot link P07711: Cathepsin L (human) (precursor)
AfCS Signalling Gateway link A000515: Cathepsin L (mouse)
Further Categories Containing This Product:
Natural Proteins • Enzymes
 
 
ALX-200-418 Revised 04-Sep-08
MMP-1 Proenzyme (human)
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SYNONYMS Collagenase (Type I) (human)
Matrix Metalloproteinase 1 (human)
Interstitial Collagenase (human)
PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY MMPs
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ALX-200-418-C005   5 µg 182.00 USD Add To Cart
Product Specification
MW: ~56kDa.
EC: 3.4.24.7
SOURCE/HOST: Isolated from human rheumatoid synovial fibroblasts. Requires activation.
CONCENTRATION: ~100µg/ml (Pierce-BCA)
PURITY: ≥90% (SDS-PAGE, Western blot)
PURITY DETAIL: No other MMP contaminants are detectable.
FORMULATION: Liquid. In 50mM TRIS-HCl, pH 7.0, 300mM NaCl, 5mM CaCl2, 1µM ZnCl2, 0.05% BRIJ35 and 0.05% sodium azide.
SPECIFIC ACTIVITY: ≥100mU/mg protein (Y. Masui, et al.; Biochem. Med. 17, 215 (1977)). One unit is defined as the amount of enzyme that hydrolyzes 1µmol Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min. at 37°C, pH 7.0. APMA activation 1 hour at 37°C; enzyme dilution for assay 1:10/5-10µl for enzyme activity assay - incubation time 30min.
SHIPPING: SHIPPED ON DRY ICE
LONG TERM STORAGE: -80°C
HANDLING: Avoid freeze/thaw cycles.
Product Specific Literature References
Synthetic substrates for vertebrate collagenase: Y. Masui, et al.; Biochem. Med. 17, 215 (1977) Abstract
Secreted forms of human neutrophil collagenase: K.A. Hasty, et al.; J. Biol. Chem. 261, 5645 (1986) Abstract; Full Text
Human fibroblast collagenase: glycosylation and tissue-specific levels of enzyme synthesis: S.M. Wilhelm, et al.; PNAS 83, 3756 (1986) Abstract
Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl)mercuric acetate: H. Nagase, et al.; Biochemistry 29, 5783 (1990) Abstract
Mechanisms of activation of tissue procollagenase by matrix metalloproteinase 3 (stromelysin): K. Suzuki, et al.; Biochemistry 29, 10261 (1990) Abstract
Stepwise activation mechanisms of the precursors of matrix metalloproteinases 1 (tissue collagenase) and 3 (stromelysin): H. Nagase, et al.; Biomed. Biochim. Acta 50, 749 (1991) Abstract
A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases: C.G. Knight, et al.; FEBS Lett. 296, 263 (1992) Abstract
The activity of collagenase-1 is required for keratinocyte migration on a type I collagen matrix: B.K. Pilcher, et al.; J. Cell Biol. 137, 1445 (1997) Abstract
The catalytic domain of activated collagenase I (MMP-1) is absolutely required for interaction with its specific inhibitor, tissue inhibitor of metalloproteinases-1 (TIMP-1): R. Vallon, et al.; Eur. J. Biochem. 244, 81 (1997) Abstract
General Information
MMP-1, the classical matrix metalloproteinase, is expressed by a large number of cell types. As an example, in basal keratinocytes migrating across the dermal matrix the enzyme is invariably expressed and cleaves fibrilliar collagen type I. It was shown that the interaction of the α2β1 integrin with dermal collagen mediates induction of MMP-1 in keratinocytes at the onset of healing and that the activity of MMP-1 is needed to initiate cell movement. The cleavage of dermal collagen provides keratinocytes with a mechanism to maintain their directionality during reepithelialization (Pilcher et al. 1997).
The MMP-1 zymogens of ~56/52kDa can be activated by a stepwise mechanism through which sequential processing events occur in the propeptide region. Both proenzymes can be activated by limited digestion with trypsin or by treatment with APMA generating their respective active enzyme forms of ~46/42kDa (Wilhelm et al. 1986).
BACKGROUND/TECHNICAL INFORMATION Activity:
We recommend to dilute this enzyme preparation at least 1:10 and to take 5µl or less for the determination of activity. Specific activity can be assayed with the synthetic substrate N-(2,4)-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg (Dnp-peptide) (Masui et al.). Substrate concentration should be 0.5mg/ml in buffer 50mM TRIS-HCl, pH 7.0, 200mM NaCl, 5mM CaCl2, 1µM ZnCl2, 0.05% BRIJ35, 0.05% sodium azide, containing 0.05mg/ml albumin. One unit MMP catalyzes the hydrolysis of 1µmol Dnp-peptide/min at 37°C and pH 7.0.
We recommend to employ the fluorogenic substrate (7-Methoxycoumarin-4-yl)acetyl-Pro-Leu-Gly-Leu-N-β-Dnp-L-α,β-diaminopropionyl-Ala-Arg-NH2) (Knight et al. 1992). The hydrolysis of the Gly-Leu bond separates the highly fluorescent (7-Methoxycoumarin-4-yl)acetyl group from the 2,4-dinitrophenyl resulting in an increase of fluorogenic intensity. The substrate should be kept as a 9.15mM stock solution in DMSO (10mg/ml). In the assay the substrate concentration should be ~25mM. The assay can be performed in a 96-well microtiter plate (200µl per well) suitable for fluorogenic measurements (excitation wavelength of 328nm; emission wavelength of 393nm).

Activation:
Do not dilute enzyme for activation! Activation is required by trypsin (2µl trypsin; 1mg/ml) for 10-20 min. at 37°C and stopped by the addition of 10µl trypsin-inhibitor (2mg/ml) or aprotinin or TLCK. Activation can also be done by 2mM (final concentration) APMA for 60 min. at 37°C.

Inhibitors:
Only  the activated and not the latent forms of wild-type MMP-1 protein is able to form a complex with TIMP-1. Quite in contrast to MMP-2 (gelatinase A) and MMP-9 (gelatinase B), in MMP-1 the C-terminal hemopexin domain does not interact with TIMP-1. The integrity of the catalytic domain of MMP-1 and its ability to bind Zn2+ is absolutely required for complex formation with TIMP-1, which further underlines the importance of this region for proper regulation of enzymatic activity of MMP-1 (Vallon et al. 1997). Therefore, the enzyme is also inhibited by chelators of divalent cations like EDTA or o-phenantroline.

Swiss-Prot link P03956: MMP-1 (human)
AfCS Signalling Gateway link A001461: MMP-1 (mouse)
Further Categories Containing This Product:
Natural Proteins • Enzymes
 
 
ALX-200-419 Revised 20-Mar-08
MMP-2 Proenzyme (human)
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SYNONYMS Gelatinase A (human)
Matrix Metalloproteinase 2 (human)
Collagenase (72kDa Type IV) (human)
PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY MMPs
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ALX-200-419-C005   5 µg 166.00 USD Add To Cart
Product Specification
MW: ~72kDa.
EC: 3.4.24.24
SOURCE/HOST: Isolated from human rheumatoid synovial fibroblasts. Requires activation.
CONCENTRATION: 40µg/ml (Pierce-BCA).
PURITY: ≥90% (SDS-PAGE, Western blot)
PURITY DETAIL: No other MMP contaminants are detectable.
FORMULATION: Liquid. In 50mM TRIS-HCl pH 7.0, containing 200mM NaCl, 5mM CaCl2, 1µM ZnCl2, 0.05% BRIJ35 0.05% sodium azide.
SPECIFIC ACTIVITY: ≥850mU/mg protein (Y. Masui, et al.; Biochem. Med. 17, 215 (1977)). One unit is defined as the amount of enzyme that hydrolyzes 1µmol Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min. at 37°C, pH 7.0.
APPLICATION: Immunogen for antibody generation, control in immunoassays and for characterizing interactions with MMP inhibitors.
SHIPPING: SHIPPED ON DRY ICE
LONG TERM STORAGE: -80°C
HANDLING: Avoid freeze/thaw cycles.
Product Specific Literature References
Synthetic substrates for vertebrate collagenase: Y. Masui, et al.; Biochem. Med. 17, 215 (1977) Abstract
A novel coumarin-labelled peptide for sensitive continuous assays of the matrix metalloproteinases: C.G. Knight, et al.; FEBS Lett. 296, 263 (1992) Abstract
Activation of progelatinase A and progelatinase A/TIMP-2 complex by membrane type 2-matrix metalloproteinase: H. Kolkenbrock, et al.; Biol. Chem. 378, 71 (1997) Abstract
General Information
BACKGROUND/TECHNICAL INFORMATION

Activity:
Specific activity can be assayed with the synthetic substrate N-(2,4)-dinitrophenyl-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg (Dnp-peptide) (Masui et al.). Substrate concentration should be 0.5mg/ml in 50mM TRIS-HCl, pH 7.0, 200mM NaCl, 5mM CaCl2, 1µM ZnCl2, 0.05% sodium azide, 0.05% BRIJ35, containing 0.05mg/ml albumine. One unit MMP catalyzes the hydrolysis of 1µmol Dnp-peptide/min. at 37°C and pH 7.0.
Alternatively the fluorogenic substrate Substrat (7-Methoxycoumarin-4-yl) acetyl-Pro-Leu-Gly-Leu-N-ß-Dnp-L-(α,ß-diaminopropionyl)Ala-Arg-NH2 (Knight et al. 1992) can be used. Hydrolysis of the Gly-Leu bond separates the highly fluorescent (7-Methoxycoumarin-4-yl)acetyl group from the 2,4-dinitrophenyl resulting in an increase of fluorogenic intensity. The Km value for the gelatinase A is 7.0x105M-1s-1. Substrate should be kept as a  9.15mM stock solution in DMSO (10mg/ml). In the assay the substrate concentration should be ~25µM. The assay can be performed in a 96-well microtiter plate (100/200µl per well) suitable for fluorogenic measurements (Ex 328 nm; Em 393 nm).

Activation:
Requires activation by 2mM (final concentration) AMPA or 1mM mersalic acid for 60-120 min. at 37°C. We do not recommend to use trypsin for activation! Do not dilute enzyme for activation!

Inhibitors:
Activated enzyme is inhibited by tissue inhibitors of matrix metalloproteinase-2 (TIMP-2) and by chelators of divalent cations like EDTA or o-phenanthroline.

Swiss-Prot link P08253: MMP-2 (human) (precursor)
AfCS Signalling Gateway link A001471: MMP-2 (mouse)
Further Categories Containing This Product:
Natural Proteins • Enzymes
 
 
ALX-200-420 Revised 18-Mar-08
MMP-2/TIMP-2 Proenzyme Complex (human)
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SYNONYMS Matrix Metalloproteinase 2/Tissue Inhibitor of Metalloproteinase 2 Complex (human)
PRODUCT LINE Cytoskeleton
PRODUCT CATEGORY MMPs
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ALX-200-420-C005   5 µg 166.00 USD Add To Cart
Product Specification
EC: 3.4.24.24 (MMP-2)
SOURCE/HOST: Isolated from human rheumatoid synovial fibroblasts. Requires activation.
CONCENTRATION: ~100µg/ml
PURITY: ≥95% (SDS-PAGE, Western blot)
PURITY DETAIL: No other MMP contaminants are detectable.
FORMULATION: Liquid. In 50mM TRIS-HCl pH 7.0, 200mM sodium chloride, 5mM CaCl2, 1µM ZnCl2, 0.05% NaN3 and 0.05% BRIJ 35.
SPECIFIC ACTIVITY: ≥30mU/mg protein (Y. Masui, et al.; Biochem. Med. 17, 215 (1977)). One unit is defined as the amount of enzyme that hydrolyzes 1µmol Dnp-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg-OH per min. at 37°C, pH 7.0.
SHIPPING: SHIPPED ON DRY ICE
SHORT TERM STORAGE: -20°C
LONG TERM STORAGE: -80°C
USE/STABILITY: Do always keep the enzyme on ice.
HANDLING: