SRP3117
MMP-1 human
recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture
Synonyme(s) :
Fibroblast collagenase
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About This Item
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32
Produits recommandés
Source biologique
human
Produit recombinant
expressed in E. coli
Essai
≥98% (HPLC)
≥98% (SDS-PAGE)
Forme
lyophilized
Poids mol.
42.7 kDa
Conditionnement
pkg of 10 μg
Technique(s)
cell culture | mammalian: suitable
Impuretés
<0.1 EU/μg endotoxin, tested
Couleur
white to off-white
Numéro d'accès UniProt
Conditions d'expédition
wet ice
Température de stockage
−20°C
Informations sur le gène
human ... MMP1(4312)
Catégories apparentées
Description générale
Matrix metalloproteinases (MMPs) are a family of endoproteases that require zinc and calcium for expressing catalytic activity. MMP-1 is expressed in various cells, including fibroblasts, keratinocytes, chondrocytes, monocytes and macrophages, hepatocytes and many tumor cells. The gene is mapped to human chromosome 11q22. Recombinant human MMP-1 is a 42.7kDa protein containing the entire catalytic N-terminal domain and the C-terminal domain which is involved in substrate specificity and in binding TIMP-1 (tissue inhibitor of metalloproteinases 1).
Application
MMP-1 (matrix metalloproteinase 1) human has been used to study effect of NF (nuclear factor)κB-mediated expression of MMP-1 in breast cancer spheroids.
Actions biochimiques/physiologiques
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, has been implicated in various degenerative disorders, including arthritis, cardiovascular disease, skeletal growth-plate disorders, and cancer metastasis. MMP-1 is a secreted collagenase with specificity toward Type I, II, III, VII, and X collagens, aggrecan, serpins, and α2-macroglobulin. It is overexpressed in lumbar intervertebral disc degeneration (IDD). It might also be associated with osteoarthritis. MMP-1 is linked with Jjuvenile idiopathic arthritis. Genetic variations in MMP-1 can affect the susceptibility and severity of this disease.
Séquence
MFVLTEGNPR WEQTHLTYRI ENYTPDLPRA DVDHAIEKAF QLWSNVTPLT FTKVSEGQAD IMISFVRGDH RDNSPFDGPG GNLAHAFQPG PGIGGDAHFD EDERWTNNFR EYNLHRVAAH ELGHSLGLSH STDIGALMYP SYTFSGDVQL AQDDIDGIQA IYGRSQNPVQ PIGPQTPKAC DSKLTFDAIT TIRGEVMFFK DRFYMRTNPF YPEVELNFIS VFWPQLPNGL EAAYEFADRD EVRFFKGNKY WAVQGQNVLH GYPKDIYSSF GFPRTVKHID AALSEENTGK TYFFVANKYW RYDEYKRSMD PGYPKMIAHD FPGIGHKVDA VFMKDGFFYF FHGTRQYKFD PKTKRILTLQ KANSWFNCRK N
Forme physique
Lyophilized from 20 mM TRIS, pH 9.0 + 0.1 mM Calcium Chloride + 100 mM Arginine.
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.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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Les clients ont également consulté
Chi Huu Nguyen et al.
Oncotarget, 6(36), 39262-39275 (2015-10-30)
RELA, RELB, CREL, NFKB1 and NFKB2, and the upstream regulators NEMO and NIK were knocked-down in lymph endothelial cells (LECs) and in MDA-MB231 breast cancer spheroids to study the contribution of NF-κB in vascular barrier breaching. Suppression of RELA, NFKB1
Haplotypes in matrix metalloproteinase gene cluster on chromosome 11q22 contribute to the risk of lung cancer development and progression.
Clinical Cancer Research, 12, 7009-7017 (2006)
Regulation of matrix metalloproteinase expression in tumor invasion.
Westermarck J and Kahari VM
Faseb Journal, 13, 781-792 (1999)
Influence of Matrix metalloproteinase 1 and 3 genetic variations on susceptibility and severity of juvenile idiopathic arthritis.
Abd-Allah SH
IUBMB Life, 67, 934-942 (2015)
Joanna Sikora et al.
Journal of biomedical optics, 20(5), 051039-051039 (2015-03-13)
The concentration of collagen degradation products (CDPs) may reflect the process of left ventricular remodeling (LVR). The aim of this study was to evaluate the potential diagnostic usefulness of time-resolved fluorescence spectroscopy (TRFS) in assessment of CDPs. The preliminary experiment
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