Ugrás a tartalomra
Merck

SRP3118

Sigma-Aldrich

MMP-2 human

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

Szinonimák:

Gelatinase A

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

UNSPSC kód:
12352204
NACRES:
NA.32

biológiai forrás

human

rekombináns

expressed in E. coli

Teszt

≥98% (HPLC)
≥98% (SDS-PAGE)

Forma

lyophilized

molekulatömeg

62.0 kDa

kiszerelés

pkg of 10 μg

technika/technikák

cell culture | mammalian: suitable

szennyeződések

<0.1 EU/μg endotoxin, tested

szín

white to off-white

UniProt elérési szám

kiszállítva

wet ice

tárolási hőmérséklet

−20°C

Géninformáció

human ... MMP2(4313)

Általános leírás

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).

Biokémiai/fiziológiai hatások

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.

Szekvencia

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

Fizikai forma

Lyophilized from 10 mM Sodium Phosphate, pH 7.5 + 0.1 mM Calcium Chloride.

Feloldás

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.

Tárolási osztály kódja

11 - Combustible Solids

WGK

WGK 3

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


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Analitikai tanúsítványok (COA)

Lot/Batch Number

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Dokumentumtár megtekintése

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
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

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