SRP3118
MMP-2 human
recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture
Synonym(s):
Gelatinase A
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
UNSPSC Code:
12352204
NACRES:
NA.32
biological source
human
recombinant
expressed in E. coli
Assay
≥98% (HPLC)
≥98% (SDS-PAGE)
form
lyophilized
mol wt
62.0 kDa
packaging
pkg of 10 μg
technique(s)
cell culture | mammalian: suitable
impurities
<0.1 EU/μg endotoxin, tested
color
white to off-white
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... MMP2(4313)
General description
Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. MMP-2 is a secreted collagenase with specificity toward Type IV, V, VII, and X collagens. The gene is mapped to human chromosome 16q12.2. Recombinant human MMP-2 is a 62kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain (552 amino acids).
Biochem/physiol Actions
Matrix metalloproteinases (MMPs) enzymes play a central role in the maintenance and remodeling of the extracellular matrix. Elevated expression of their activity, caused either by up-regulation of their expression or down-regulation of their cognate inhibitors, which has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. High levels of MMP-2 are observed in the acute phase of transverse myelitis. It is upregulated in colorectal carcinoma and is associated with poor survival outcome. MMP-2 gene haplotypes are also linked with risk of thoracic aortic dissection, a cardiovascular disorder with high death rate.
Sequence
MYNFFPRKPK WDKNQITYRI IGYTPDLDPE TVDDAFARAF QVWSDVTPLR FSRIHDGEAD IMINFGRWEH GDGYPFDGKD GLLAHAFAPG TGVGGDSHFD DDELWTLGEG QVVRVKYGNA DGEYCKFPFL FNGKEYNSCT DTGRSDGFLW CSTTYNFEKD GKYGFCPHEA LFTMGGNAEG QPCKFPFRFQ GTSYDSCTTE GRTDGYRWCG TTEDYDRDKK YGFCPETAMS TVGGNSEGAP CVFPFTFLGN KYESCTSAGR SDGKMWCATT ANYDDDRKWG FCPDQGYSLF LVAAHEFGHA MGLEHSQDPG ALMAPIYTYT KNFRLSQDDI KGIQELYGAS PDIDLGTGPT PTLGPVTPEI CKQDIVFDGI AQIRGEIFFF KDRFIWRTVT PRDKPMGPLL VATFWPELPE KIDAVYEAPQ EEKAVFFAGN EYWIYSASTL ERGYPKPLTS LGLPPDVQRV DAAFNWSKNK KTYIFAGDKF WRYNEVKKKM DPGFPKLIAD AWNAIPDNLD AVVDLQGGGH SYFFKGAYYL KLENQSLKSV KFGSIKSDWL GC
Physical form
Lyophilized from 10 mM Sodium Phosphate, pH 7.5 + 0.1 mM Calcium Chloride.
Reconstitution
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.5-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Suppression of local invasion of ameloblastoma by inhibition of matrix metalloproteinase-2 in vitro.
Anxun Wang et al.
BMC cancer, 8, 182-182 (2008-07-01)
Ameloblastomas are odontogenic neoplasms characterized by local invasiveness. This study was conducted to address the role of matrix metalloproteinase-2 (MMP-2) in the invasiveness of ameloblastomas. Plasmids containing either MMP-2 siRNA or tissue inhibitor of metalloproteinase-2 (TIMP-2) cDNA were created and
The association between inflammation-related genes and serum androgen levels in men: the prostate, lung, colorectal, and ovarian study.
Meyer TE
Prostate, 72, 65-71 (2012)
Takashi Temma et al.
PloS one, 9(7), e102180-e102180 (2014-07-11)
Since matrix metalloproteinase-2 (MMP-2) is an important marker of tumor malignancy, we developed an original drug design strategy, MMP-2 activity dependent anchoring probes (MDAP), for use in MMP-2 activity imaging, and evaluated the usefulness of this probe in in vitro
Annie Pardo et al.
The international journal of biochemistry & cell biology, 37(2), 283-288 (2004-10-12)
The matrix metalloproteinases (MMPs) are a family of zinc-containing endopeptidases that play a key role in both physiological and pathological tissue remodeling. Human fibroblast collagenase (MMP-1) was the first vertebrate collagenase purified as a protein and cloned as a cDNA
High expression of matrix metalloproteinases: MMP-2 and MMP-9 predicts poor survival outcome in colorectal carcinoma.
Salem N
Future Oncology, 12, 323-331 (2016)
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service