Recombinant Human MMP-1 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

Order Details

Recombinant Human MMP-1 Protein, CF Summary

Details of Functionality
Measured by its ability to cleave a fluorogenic peptide substrate Mca-KPLGL-Dpa-AR-NH2 (Catalog # ES010). The specific activity is > 400 pmol/min/µg, as measured under the described conditions.
Source
Mouse myeloma cell line, NS0-derived human MMP-1 protein
Phe20-Asn469
Accession #
N-terminal Sequence
Phe20
Structure / Form
Pro form
Protein/Peptide Type
Recombinant Enzymes
Gene
MMP1
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
52 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
52-55 kDa, reducing conditions
Publications
Read Publications using
901-MP in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -20 to -70 °C as supplied.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Buffer
Supplied as a 0.2 μm filtered solution in MES, NaCl, CaCl2 and Brij-35.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Assay Procedure
  • Assay Buffer: 50 mM Tris, 10 mM CaCl2, 150 mM NaCl, 0.05% (w/v) Brij-35, pH 7.5 (TCNB)
  • Recombinant Human MMP-1 (rhMMP-1) (Catalog # 901-MP)
  • p-aminophenylmercuric acetate (APMA), (Sigma, Catalog # A-9563), 100 mM stock in DMSO
  • Substrate: MCA-Lys-Pro-Leu-Gly-Leu-DPA-Ala-Arg-NH2 (R&D Systems, Catalog # ES010)
  • F16 Black Maxisorp Plate (Nunc, Catalog # 475515)
  • Fluorescent Plate Reader (Model: SpectraMax Gemini EM by Molecular Devices) or equivalent
  1. Dilute rhMMP-1 to 50 µg/mL in Assay Buffer.
  2. Activate 50 µg/mL rhMMP-1 by adding APMA to a final concentration of 1 mM.
  3. Incubate at 37 °C for 2 hours.
  4. Dilute activated rhMMP-1 to 1 ng/µL in Assay Buffer.
  5. Dilute Substrate to 20 µM in Assay Buffer.
  6. Load into a black well plate 50 µL of 1 ng/µL rhMMP-1 and start the reaction by adding 50 µL of 20 µM Substrate. Include a Substrate Blank containing 50 µL Assay Buffer, 50 µL Substrate, and no rhMMP-1.
  7. Read at excitiation and emission wavelengths of 320 nm and 405 nm, respectively, in kinetic mode for 5 minutes.
  8. Calculate specific activity:

     Specific Activity (pmol/min/µg) =

Adjusted Vmax* (RFU/min) x Conversion Factor** (pmol/RFU)
amount of enzyme (µg)

     *Adjusted for Substrate Blank

     **Derived using calibration standard MCA-Pro-Leu-OH (Bachem, Catalog # M-1975).

Per Well:
  • rhMMP-1: 0.050 µg
  • Substrate: 10 µM

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human MMP-1 Protein, CF

  • CLGmatrix metalloprotease 1
  • CLGN
  • EC 3.4.24
  • EC 3.4.24.7
  • Fibroblast collagenase
  • interstitial collagenase
  • matrix metallopeptidase 1 (interstitial collagenase)
  • matrix metalloproteinase 1 (interstitial collagenase)
  • Matrix metalloproteinase-1
  • MMP1
  • MMP-1

Background

Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-1 (interstitial collagenase), can degrade a broad range of substrates including types I, II, III, VII, VIII, and X collagens as well as casein, gelatin, alpha ‑1 antitrypsin, myelin basic protein, L-Selectin, pro-TNF, IL-1 beta, IGF-BP3, IGF-BP5, pro MMP-2 and pro MMP-9. A significant role of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling, characterized by the cleavage of the interstitial collagen triple helix into ¾, ¼ fragments. However, as the list of substrates above illustrates, the role of MMP-1 is more diverse than originally envisaged, and may involve enzyme cascades, cytokine regulation and cell surface molecule modulation. MMP-1 is expressed by fibroblasts, keratinocytes, endothelial cells, monocytes and macrophages. Structurally, MMP-1 may be divided into several distinct domains; a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a short hinge region and a carboxyl terminal (hemopexin-like) domain.

  1. Cawston, T.E. (2004) in Interstitial Collagenase. Barrett, A.J. et al. (eds): Handbook of Proteolytic Enzymes, San Diego: Academic Press, p. 472.

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901-MP
Species: Hu
Applications: Enzyme Activity

Publications for MMP-1 (901-MP)(15)

We have publications tested in 4 confirmed species: Human, Rat, Bovine, N/A.

We have publications tested in 5 applications: Bioassay, Cleavage, ELISA Standard, EnzAct, Enzyme Assay.


Filter By Application
Bioassay
(3)
Cleavage
(1)
ELISA Standard
(3)
EnzAct
(6)
Enzyme Assay
(2)
All Applications
Filter By Species
Human
(8)
Rat
(1)
Bovine
(1)
N/A
(4)
All Species
Showing Publications 1 - 10 of 15. Show All 15 Publications.
Publications using 901-MP Applications Species
L Kumar, W Colomb, J Czerski, CR Cox, SK Sarkar Efficient protease based purification of recombinant matrix metalloprotease-1 in E. coli Protein Expr. Purif., 2018;0(0):. 2018 [PMID: 29626520] (EnzAct) EnzAct
N Willumsen, CL Bager, DJ Leeming, AC Bay-Jensen, MA Karsdal Nidogen-1 Degraded by Cathepsin S can be Quantified in Serum and is Associated with Non-Small Cell Lung Cancer Neoplasia, 2017;19(4):271-278. 2017 [PMID: 28282545] (EnzAct, Human) EnzAct Human
Shams-Un-Nisa Naveed MMP-1 Activation Contributes to Airway Smooth Muscle Growth and Asthma Severity Am. J. Respir. Crit. Care Med, 2016;0(0):. 2016 [PMID: 27967204] (Bioassay, Human) Bioassay Human
Shashi K Gopal Transformed MDCK cells secrete elevated MMP1 that generates LAMA5 fragments promoting endothelial cell angiogenesis Sci Rep, 2016;6(0):28321. 2016 [PMID: 27324842] (EnzAct, Human) EnzAct Human
Ichikawa T, Sugiura H, Koarai A, Minakata Y, Kikuchi T, Morishita Y, Oka A, Kanai K, Kawabata H, Hiramatsu M, Akamatsu K, Hirano T, Nakanishi M, Matsunaga K, Yamamoto N, Ichinose M TLR3 activation augments matrix metalloproteinase production through reactive nitrogen species generation in human lung fibroblasts. J Immunol, 2014;192(11):4977-88. 2014 [PMID: 24760149] (Bioassay, Human) Bioassay Human
Djokic J, Fagotto-Kaufmann C, Bartels R, Nelea V, Reinhardt D Fibulin-3, -4, and -5 are highly susceptible to proteolysis, interact with cells and heparin, and form multimers. J Biol Chem, 2013;288(31):22821-35. 2013 [PMID: 23782690] (Cleavage, Human) Cleavage Human
Zhang Y, Mao X, Schwend T, Littlechild S, Conrad G Resistance of corneal RFUVA-cross-linked collagens and small leucine-rich proteoglycans to degradation by matrix metalloproteinases. Invest Ophthalmol Vis Sci, 2013;54(2):1014-25. 2013 [PMID: 23322569] (Enzyme Assay, Bovine) Enzyme Assay Bovine
Devel L, Beau F, Amoura M, Vera L, Cassar-Lajeunesse E, Garcia S, Czarny B, Stura E, Dive V Simple pseudo-dipeptides with a P2&#039; glutamate: a novel inhibitor family of matrix metalloproteases and other metzincins. J Biol Chem, 2012;287(32):26647-56. 2012 [PMID: 22689580] (EnzAct, N/A) EnzAct N/A
Zhao X, Qureshi F, Eastman PS, Manning WC, Alexander C, Robinson WH, Hesterberg LK Pre-analytical effects of blood sampling and handling in quantitative immunoassays for rheumatoid arthritis. J. Immunol. Methods, 2012;378(1):72-80. 2012 [PMID: 22366959] (ELISA Standard, N/A) ELISA Standard N/A
Gonzalez RM, Seurynck-Servoss SL, Crowley SA Development and validation of sandwich ELISA microarrays with minimal assay interference. J. Proteome Res., 2008;7(6):2406-14. 2008 [PMID: 18422355] (ELISA Standard, N/A) ELISA Standard N/A
Show All 15 Publications.

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Bioinformatics

Gene Symbol MMP1
Uniprot