Recombinant Bovine 72 kDa type IV collagenase (MMP2)

Code CSB-YP861945BO
MSDS
Size Pls inquire
Source Yeast
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Code CSB-EP861945BO
MSDS
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Source E.coli
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Code CSB-EP861945BO-B
MSDS
Size Pls inquire
Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP861945BO
MSDS
Size Pls inquire
Source Baculovirus
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Code CSB-MP861945BO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
MMP2; 72 kDa type IV collagenase; EC 3.4.24.24; 72 kDa gelatinase; Matrix metalloproteinase-2; MMP-2) [Cleaved into: PEX]
Species
Bos taurus (Bovine)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, and atherosclerotic plaque rupture. As well as degrading extracellular matrix proteins, can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. Also cleaves KISS at a Gly-|-Leu bond. Appears to have a role in myocardial cell death pathways. Contributes to myocardial oxidative stress by regulating the activity of GSK3beta. Cleaves GSK3beta in vitro. Involved in the formation of the fibrovascular tissues.; PEX, the C-terminal non-catalytic fragment of MMP2, posseses anti-angiogenic and anti-tumor properties and inhibits cell migration and cell adhesion to FGF2 and vitronectin. Ligand for integrin alpha-v/beta-3 on the surface of blood vessels.
Gene References into Functions
  1. this study shows that differential FFAR1 signaling is associated with gene expression or gelatinase granule release in bovine neutrophils PMID: 27363707
  2. NADPH oxidase plays an important role in proMMP-2 expression and activation and MMP-2 mediated SMC proliferation occurs through the involvement of Spm-Cer-S1P signaling axis under ANG II stimulation of PASMCs PMID: 27210740
  3. The expression patterns of MMP1, MMP2, and MMP8 were explored during fetal and postnatal development of longissimus dorsi muscle in cattle, and the relationships of MMP1, MMP2, and MMP8 expression levels with meat quality traits were analyzed in cattle. The expression of MMP1, MMP2, and MMP8 were also tested in four kinds of fat tissues and three kinds of skeletal muscle tissues. PMID: 26985938
  4. The results showed that a decrease in MMP-1 and MMP-2 gene expression is accompanied with a decrease in NO concentrations in infertile cows affected with ovarian cysts. PMID: 25496672
  5. Activation of cytosolic MMP-9 and MMP-2 was investigated in the retinal endothelial cells incubated in high glucose for 6-96 h, and correlated with their mitochondrial accumulation and mitochondrial damage. PMID: 23891690
  6. Data indicate the involvement of PKC-alpha in proMMP-2 activation and inhibition of TIMP-2 expression by NF-kappaB-MT1-MMP-dependent and -independent pathway. PMID: 23266860
  7. Data suggest that EMMPRIN derived from endometrial epithelial cells regulates expression of matrix metalloproteinases (MMP-2; MMP-14) in endometrial stromal cells; expression of stromal MMPs is significantly higher in coculture with epithelial cells. PMID: 23115270
  8. Adding pure bovine MMP-2 to the smooth muscle membrane suspension causes an increase in Ca(2+)-ATPase activity, but the pretreatment with TIMP-2 inhibits the increase in the enzyme activity PMID: 22905396
  9. A differential pattern of matrix metalloproteinase-2 and Tissue inhibitor metalloproteinase-2 was observed in cow uteri with adenomyosis. PMID: 21626345
  10. MMP-14, MMP-2 and TIMP-2 are co-localized in the fetal compartment and therefore could influence the timely release of fetal membranes in cattle. PMID: 21247626
  11. Results describe distinct changes in expression of MMP2, MMP14, and the metallopeptidase inhibitor TIMP2 between different phases of the estrous cycle indicating an endocrine regulation. PMID: 20887771
  12. EMMPRIN from the luminal epithelium may regulate the expression of stromal MMP-2 and MMP-14 suggesting a role in adhesion and fusion of embryo to luminal epithelium. PMID: 20540754
  13. High shear stress up-regulates type IV collagen synthesis and down-regulates MMP-2 secretion in endothelial cells. PMID: 20490867
  14. increased MMP-2 activity subsequently played a pivotal role in stimulating Ca2+ ATPase activity in bovine pulmonary vascular smooth muscle plasma membrane PMID: 12102173
  15. MMP2 has a role in the oxidant activation of Ca2+Atpase PMID: 12236590
  16. results suggest a significant role of matrix metalloproteinase-2 and-9 in growth and development of bovine follicle PMID: 12586316
  17. Cells constitutively produced proMMP-9 and proMMP-2, and treatment with TNFalpha, hepatocyte growth factor, and 12-O-tetradecanoylphorbol 13-acetate resulted in significant increase in level of proMMP-9 but not in level of proMMP-2. PMID: 12606436
  18. MMP-2 and MMP-9 production in blastocysts attached to the endometrial cells is regulated by TNF-alpha and TNF-beta PMID: 14967948
  19. study suggests that MMP-2 plays an important role in regulating Ca2+ATPase activity, and ATP-dependent and Na+-dependent Ca2+ uptake in microsomes of bovine pulmonary artery smooth muscle during treatment with peroxynitrite PMID: 15026147
  20. reveal a potentially novel role for strain-induced endothelial matrix metalloproteinase-2 in regulating vascular smooth muscle cell migration PMID: 15219830
  21. Results describe the isolation of matrix metalloproteinase 2 (MMP-2) from the MMP-2/tissue inhibitor of metalloproteinase 2 (TIMP-2) complex, and the characterization of both isolated MMP-2 and the complex itself. PMID: 15374620
  22. MMP-2 is predominantly produced by large luteal cells and endothelial cells, and plays an essential role in luteal remodeling and angiogenesis. PMID: 15570615
  23. oxidants inactivate TIMP-2, and the resulting activation of MMP-2 subsequently inhibits Na+ dependent Ca2+ uptake in the microsomes PMID: 15792356
  24. Results suggest that MMP-2, MMP-9, and TIMP-2 mRNAs are expressed in bovine placentomes during the gestational and postpartum periods and that these enzymes, in conjunction with steroidogenic enzymes, mediate fetal membrane detachment after parturition. PMID: 17154296
  25. MMP2 is responsible for collagen denaturation in the last part of gradual cervical ripening. PMID: 18361420
  26. Relative expression of MMP-9 and MMP-2 increased in synovial fluid from calves with experimentally induced septic arthritis, with relative expression remaining high for several days after E. coli infection. PMID: 18672966
  27. MMP-2 gene expression declined with the progress of gestation, but its intensity was maintained at a high level during the peri-implantation period and increased in late gestation. PMID: 19116037

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Subcellular Location
Secreted, extracellular space, extracellular matrix. Membrane. Nucleus.
Protein Families
Peptidase M10A family
Database Links
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