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Recombinant Rabbit 72 kDa type IV collagenase (MMP2), partial

Recombinant Rabbit 72 kDa type IV collagenase (MMP2), partial

Code
MSDS	MSDS Datasheet
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Source
Conjugate
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Product Details
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Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

MMP2

Uniprot NO.

P50757

Species

Oryctolagus cuniculus (Rabbit)

Source

Yeast

Expression Region

110-662

Target Protein Sequence

Y NFFPRKPKWD KNQITYRIIG YTPDLDPETV DDAFARAFQV WSNVTPLRFS RIHDGEADIM INFGRWEHGD GYPFDGKDGL LAHAFAPGTG VGGDSHFDDD ELWTLGEGQV VRVKYGNADG EYCKFPFLFN GKEYTSCTDT GRSDGFLWCS TTYNFEKDGK YGFCPHEALF TMGGNADGQP CKFPFRFQGT SYSSCTTEGR TDGYRWCGTT EDYDRDKKYG FCPETAMSTI GGNSEGAPCV FPFTFLGNKY ESCTSAGRSD GKMWCATSTN YDDDRKWGFC PDQGYSLFLV AAHEFGHAMG LEHSQDPGAL MAPIYTYTKN FRLSQDDIKG IQELYGASPD AGTDAGTGPT PTLGPVTPEI CTQDIVFDGI AQIRGEIFFF KDRFIWRTVT PGDKPMGPLL VATFWPELPE KIDAVYEAPQ EEKAVFFAGN EYWVYSASTL ERGYPKPLTS LGLPPDVQRV DAAFNWSKNK KTYIFAGDKF WRYNEVKKKM DPGFPRLIAD AWNAIPDHLD AVVDLQGSGH SYFFKGTYYL KLENQSLKSV KVGSIKTDWL GC
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Protein Length

Partial

Tag Info

N-terminal His-tagged/Tag-Free
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.

Storage

Store at -20°C, for extended storage, conserve at -20°C or -80°C.

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.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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Target Background

Function(From Uniprot)

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

These results show that MMP-2 activates the EGFR and triggers downstream signaling pathways increasing Reactive Oxygen Species formation and promoting vasoconstriction. PMID:30029165
The present study demonstrated the ability of 30 and 100 ng/ml TIMP3 to attenuate migration and proliferation, and to inhibit the activity of MMP2, MMP9 and TNFalpha secretion of NA SMCs. In conclusion, TIMP3 may be considered a potential therapeutic drug for use in a novel drugeluting stent, to attenuate the progressive dilation of the aortic NA. PMID:29956789
Selenium suppressed high-fat diet-induced MMP2 over-expression in vivo by improving lipid metabolism. PMID:28595793
Repetitive mechanical stimulation of tendon cells results in a small increase in matrix metalloproteinase2 levels, but it appears unlikely that serum matrix metalloproteinase2 will be a useful indicator of tendon overuse injury. PMID:26909661
Inflammatory factors such as TNF-alpha can stimulate MMP-2/9 activity in corneal epithelium cells. This may be a potential manipulating mechanism of MMP expression in the pathogenesis of corneal diseases PMID:26125840
Results provide evidence that MMP-2 bears the potentiality to cleave alpha-DG enriched from rabbit skeletal muscle indicating that this degradation indeed might also occur in vivo. PMID:25483986
These data suggest that OxyHb suppresses K V currents through both reactive oxygen species-dependent and independent pathways involving MMP activation. PMID:25366605
In conclusion, MMP-2 could be responsible for the proteolysis of dystrophin. PMID:24791785
Castor oil polymer induces bone formation with high matrix metalloproteinase-2 expression. PMID:23670892
MMP2 spinal cord expression is increased in cervical spondylotic myelopathy. PMID:22673181
Ulinastatin effectively inhibited the increased expression of MMP-2, MMP-3, and iNOS in degenerated NP cells induced by IL-1beta in vitro. PMID:22853554
Hemoperfusion could obviously reduce oxidative stress and the expression levels of MMP-2, MMP-9 and TIMP-1 in rabbits with acute paraquat poisoning. PMID:22801080
Exposure to long periods of light irrespective of its characteristics leads to the increased expression of some matrix metalloprpteases. PMID:20238014
The RNA interference targeting COX-2 can effectively inhibit the expression of COX-2 and MMP-2 in IL-1alpha stimulated rabbit corneal stromal cells in vitro. PMID:19175164
Our results strongly suggest that ischaemic postconditioning may exert part of its cardioprotective effects through the inhibition of MMP-2 activity. PMID:19880538