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Key Documents

SRP3118

Sigma-Aldrich

MMP-2 human

recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture

Synonym(s):

Gelatinase A

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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.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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’.

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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)
Association of MMP-2 gene haplotypes with thoracic aortic dissection in chinese han population.
Liu O
BMC Cardiovascular Disorders, 16, doi: 10- doi: 10 (2016)
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
S M Wojtowicz-Praga et al.
Investigational new drugs, 15(1), 61-75 (1997-01-01)
The matrix metalloproteinases (MMPs) are a family of at least fifteen secreted and membrane-bound zinc-endopeptidases. Collectively, these enzymes can degrade all of the components of the extracellular matrix, including fibrallar and non-fibrallar collagens, fibronectin, laminin and basement membrane glycoproteins. MMPs

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