Recombinant Cynomolgus Monkey MMP-9 Protein, CF

Name: Recombinant Cynomolgus Monkey MMP-9 Protein, CF
Brand: R&D Systems
SKU: 10833-MP

R&D Systems, Inc. a Bio-Techne Brand

Catalog # 10833-MP

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Key Product Details

Source:	CHO
Accession #:	XP_005569271.2
Structure / Form:	Proform

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Product Specifications for Recombinant Cynomolgus Monkey MMP-9 Protein, CF

Source	Chinese Hamster Ovary cell line, CHO-derived cynomolgus monkey MMP-9 protein Ala20-Asp707
Purity	>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin level	<0.10 EU per 1 μg of the protein by the LAL method.
N-terminal sequence Analysis	Ala20
Predicted Molecular Mass	76 kDa
SDS-PAGE	83-95 kDa, under reducing conditions
Activity	Measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH₂ (Catalog # ES001). The specific activity is >750 pmol/min/μg, as measured under the described conditions.

Scientific Data Examples for Recombinant Cynomolgus Monkey MMP-9 Protein, CF

	Recombinant Cynomolgus Monkey MMP-9 Enzyme Activity Recombinant Cynomologous Monkey MMP-9 Protein (Catalog # 10833-MP) is measured by its ability to cleave the fluorogenic peptide substrate, Mca-PLGL-Dpa-AR-NH2 (ES001).
	Recombinant Cynomolgus Monkey MMP-9 Protein SDS-PAGE. 2 μg/lane of Recombinant Cynomolgus Monkey MMP-9 (Catalog # 10833-MP) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at ~90 kDa under reducing conditions.

Formulation, Preparation and Storage

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

What formulation is right for me?

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

10833-MP

Formulation	Supplied as a 0.2 μm filtered solution in Tris, CaCl₂, NaCl and Brij-35.
Shipping	The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage:	Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 6 months from date of receipt, -20 to -70 °C as supplied. 3 months, -20 to -70 °C under sterile conditions after opening.

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Background: MMP-9

Matrix metalloproteinase 9 (MMP-9), also known as gelatinase B, is a member of the MMP zinc-dependent family of endopeptidases. It cleaves and degrades a variety of targets including important extracellular matrix (ECM) proteins: gelatin, collagen, and elastin, as well as chemokines and extracellular domain plasma membrane proteins (1-3). MMP-9 is synthesized and secreted by several cells including neutrophils, macrophages, fibroblasts, and endothelial cells (4). The monomeric MMP-9 protein is composed of several distinct domains including a signal sequence, a pro-domain which is cleaved upon activation, and a catalytic domain at the n-terminus followed by a hinge region and the c-terminal hemopexin-like domains that contribute to substrate recognition and specificity (5,6). The catalytic domain contains fibronectin type II domains, an active site, and a zinc binding site. MMP-9 can exist as a monomer, disulfide-linked homodimer, or heterodimer in complex with lipocalin‑2 (7,8). MMP-9 activity is regulated at several levels via transcription, post-transcription, translation, secretion, activation, and inhibition. As MMP-9 is involved in ECM remodeling and membrane protein cleavage, it has been widely associated to play a role in several diseases including cancers (9), autoimmune, and cardiovascular diseases (9-11). MMP-9 is consequently an important target of interest for inhibition (11-13). Additionally, it has been found to be a potential biomarker for many types of cancer including pancreatic, osteosarcoma, lung, ovarian, and breast (9).

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References	Kridel, S.J. et al. (2001) J. Biol. Chem. 276:20572. Vaisar, T. et al. (2009) Mol. Cell. Proteom. MCP 8:1044. Dufour, A. and C.M. Overall. (2013) Trends Pharmacol. Sci. 34:233. Vandooren, J. et al. (2013) Crit. Rev. Biochem. Mol. Biol. 48:222. Roeb, E. et al. (2002) J. Biol. Chem. 277:50326. Rosenblum, G. et al. (2007) Structure 15:1227. Kjeldsen, L. et al. (1993) J. Biol. Chem. 268:10425. Olson, M.W. et al. (2000) J. Biol. Chem. 275:2661. Huang, H. (2018) Sensors 18:3249. Ram, M. et al. (2006) J. Clin. Immunol. 26:299. Hu, J. et al. (2007) Nat. Rev. Drug. Discov. 6:480. Fields, G.B. (2019) Cells. 8:984. Kumar, G.B. et al. (2019) Medchemcomm. 10:2024.
Long Name	Matrix Metalloproteinase 9
Entrez Gene IDs	4318 (Human); 17395 (Mouse); 81687 (Rat); 102117693 (Cynomolgus Monkey)
Alternate Names	92 kDa gelatinase, 92 kDa type IV collagenase, CLG4B, EC 3.4.24, EC 3.4.24.35, GELB, Gelatinase B, MANDP2, MMP-9, MMP9, macrophage gelatinase, matrix metallopeptidase 9, matrix metalloproteinase 9, matrix metalloproteinase-9, type V collagenase

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