Matrix Metalloproteinase-9 Human HEK293

Cat. No.	Size	Price 1 - 4 pcs / 5 - 9 pcs / 10+ pcs
RD172439100	0.1 mg	$421 / $370 / On request

Technical Data

Type

Recombinant protein

Description

Total 694 AA. MW: 77.2 kDa (calculated). UniProtKB acc. No. P14780 (Ala20–Asp707). C-terminal His-tag (6 AA). Protein identity confirmed by MS.

Amino Acid Sequence

APRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTRDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPEDHHHHHH

Source

HEK293

Purity

˃ 90 % by SDS-PAGE

SDS-PAGE Gel

12 % SDS-PAGE separation of Human Matrix Metalloproteinase-9:

M.W. marker – 14, 21, 31, 45, 66, 97 kDa
Reduced and boiled sample, 2.5 μg/lane
Non-reduced and non-boiled sample, 2.5 μg/lane

Endotoxin

< 1.0 EU/µg

Formulation

Filtered (0.4 μm) and lyophilized from 0.5 mg/ml solution in phosphate buffered saline pH7.5 + 5% (w/v) Threalose.

Reconstitution

Add deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely.

Applications

Western blotting, ELISA

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store lyophilized protein at -80°C. Lyophilized protein remains stable until the expiry date when stored at -80°C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at -80°C for long term storage. Reconstituted protein can be stored at 4°C for a week.

Quality Control Test

BCA to determine quantity of the protein.
SDS PAGE to determine purity of the protein. Endotoxin level determination.

Note

This product is intended for research use only.

Summary

Research topic

Bone and cartilage metabolism, Cardiovascular disease, Extracellular matrix, Immune Response, Infection and Inflammation, Neural tissue markers, Oncology, Others, Pulmonary diseases

Summary

Matrix metalloproteinases (MMPs) are a group of enzymes engaged in the degradation and remodeling of extracellular matrix (ECM). Nowadays six groups of these enzymes have been distinguished (collagenases, gelatinases, stromelysins, matrilysins, membrane-type, and a sixth group encompassing several other MMPs not classified in the previous categories), differing in structure, cellular localization, and substrate specificity. Since these enzymes are involved in connective tissue remodeling occurring in the course of morphogenetic processes, therefore, they are a subject of a very strict regulation, which is executed, among others, by the expression of their specific inhibitors—tissue inhibitors of metalloproteinases (TIMPs). MMPs 2 and 9 are named type IV collagenases, or alternatively gelatinase A and B, respectively. Their degrading substrates are gelatine, the denatured form of collagen, and type IV collagen, the main component of the basement membrane. One of the members of the MMP family, MMP-9, is a gelatinase that has been implicated in the pathogenesis of atherosclerosis and chronic obstructive pulmonary disease (COPD) in addition to tumor formation and metastasis. Accordingly, a number of studies have associated elevated serum levels of MMP-9 with many chronic inflammatory conditions including coronary artery disease (CAD), COPD ,arthritis and metabolic syndrome. Notably, high levels of MMP-9 have been associated with plaque progression, destability and rupture. These various effects exaggerate the inflammatory process, promoting atherosclerosis and increasing the risk of atherothrombosis and cardiovascular (CV) events. Thus, MMP-9 has emerged as a novel disease marker as well as a therapeutic target. MMP9, like other MMPs, belongs to a superfamily of zinc containing proteases and has been shown to associate with tumorigenesis. Overexpression of tissue MMPs has been correlated with progression in many tumour types, and overexpression of MMP9 has been found in colorectal adenomas and carcinomas. A significant positive correlation has also been found between tissue MMP9 and the stage of colorectal tumours at diagnosis. Elevated expression of MMP-9, along with MMP-2 is usually seen in invasive and highly tumorigenic cancers such as colorectal tumors, gastric carcinoma, pancreatic carcinoma, breast cancer, oral cancer, melanoma, malignant gliomas, chondrosarcoma, gastrointestinal adenocarcinoma. Levels are also increased in malignant astrocytomas, carcinomatous meningitis, and brain metastases. Clinical use and areas of investigation: - Multiple sclerosis - Inflammatory diseases - Cancer

Product References (3)

References

Johannsen B, Karpíšek M, Baumgartner D, Klein V, Bostanci N, Paust N, Früh SM, Zengerle R, Mitsakakis K. One-step, wash-free, bead-based immunoassay employing bound-free phase detection. Anal Chim Acta. 2021 Apr 8;1153:338280. doi: 10.1016/j.aca.2021.338280. Epub 2021 Feb 5. PubMed PMID: 33714441. See more on PubMed
Paqué PN, Herz C, Wiedemeier DB, Mitsakakis K, Attin T, Bao K, Belibasakis GN, Hays JP, Jenzer JS, Kaman WE, Karpíšek M, Körner P, Peham JR, Schmidlin PR, Thurnheer T, Wegehaupt FJ, Bostanci N. Salivary Biomarkers for Dental Caries Detection and Personalized Monitoring. J Pers Med. 2021 Mar 23;11(3):235. doi: 10.3390/jpm11030235. PubMed PMID: 33806927. PubMed CentralPMCID: PMC8004821. See more on PubMed
Johannsen B, Müller L, Baumgartner D, Karkossa L, Früh SM, Bostanci N, Karpíšek M, Zengerle R, Paust N, Mitsakakis K. Automated Pre-Analytic Processing of Whole Saliva Using Magnet-Beating for Point-of-Care Protein Biomarker Analysis. Micromachines (Basel). 2019 Nov 30;10(12):833. doi: 10.3390/mi10120833. PubMed PMID: 31801193. PubMed CentralPMCID: PMC6952956. See more on PubMed

Summary References (23)

References to MMP-9

Atkinson JJ, Senior RM. Matrix metalloproteinase-9 in lung remodeling. Am J Respir Cell Mol Biol. 2003 Jan;28 (1):12-24
Chakraborti S, Mandal M, Das S, Mandal A, Chakraborti T. Regulation of matrix metalloproteinases: an overview. Mol Cell Biochem. 2003 Nov;253 (1-2):269-85
Corbel M, Belleguic C, Boichot E, Lagente V. Involvement of gelatinases (MMP-2 and MMP-9) in the development of airway inflammation and pulmonary fibrosis. Cell Biol Toxicol. 2002;18 (1):51-61
Creemers EE, Cleutjens JP, Smits JF, Daemen MJ. Matrix metalloproteinase inhibition after myocardial infarction: a new approach to prevent heart failure?. Circ Res. 2001 Aug 3;89 (3):201-10
Fridman R, Toth M, Chvyrkova I, Meroueh SO, Mobashery S. Cell surface association of matrix metalloproteinase-9 (gelatinase B). Cancer Metastasis Rev. 2003 Jun-Sep;22 (2-3):153-66
Gingis-Velitski S, Loven D, Benayoun L, Munster M, Bril R, Voloshin T, Alishekevitz D, Bertolini F, Shaked Y. Host response to short-term, single-agent chemotherapy induces matrix metalloproteinase-9 expression and accelerates metastasis in mice. Cancer Res. 2011 Nov 15;71 (22):6986-96
Hofmann UB, Westphal JR, Van Muijen GN, Ruiter DJ. Matrix metalloproteinases in human melanoma. J Invest Dermatol. 2000 Sep;115 (3):337-44
John A, Tuszynski G. The role of matrix metalloproteinases in tumor angiogenesis and tumor metastasis. Pathol Oncol Res. 2001;7 (1):14-23
Kanayama H. Matrix metalloproteinases and bladder cancer. J Med Invest. 2001 Feb;48 (1-2):31-43
Kelly EA, Jarjour NN. Role of matrix metalloproteinases in asthma. Curr Opin Pulm Med. 2003 Jan;9 (1):28-33
Klein G, Vellenga E, Fraaije MW, Kamps WA, de Bont ES. The possible role of matrix metalloproteinase (MMP)-2 and MMP-9 in cancer, e.g. acute leukemia. Crit Rev Oncol Hematol. 2004 May;50 (2):87-100
Matusiewicz M, ORCID: 0000-0003-4624-0109, Neubauer K, ORCID: 0000-0003-3650-9311, Mierzchala-Pasierb M, ORCID: 0000-0001-9640-4883, Gamian A, Krzystek-Korpacka M. Matrix metalloproteinase-9: its interplay with angiogenic factors in inflammatory bowel diseases. Dis Markers. 2014;2014:643645
Nakada M, Okada Y, Yamashita J. The role of matrix metalloproteinases in glioma invasion. Front Biosci. 2003 Jan 1;8:e261-9
Niimi T, Keck-Waggoner CL, Popescu NC, Zhou Y, Levitt RC, Kimura S. UGRP1, a uteroglobin/Clara cell secretory protein-related protein, is a novel lung-enriched downstream target gene for the T/EBP/NKX2.1 homeodomain transcription factor. Mol Endocrinol. 2001 Nov;15 (11):2021-36
Ohbayashi H. Matrix metalloproteinases in lung diseases. Curr Protein Pept Sci. 2002 Aug;3 (4):409-21
Opdenakker G, Nelissen I, Van Damme J. Functional roles and therapeutic targeting of gelatinase B and chemokines in multiple sclerosis. Lancet Neurol. 2003 Dec;2 (12):747-56
Opdenakker G, Van den Steen PE, Dubois B, Nelissen I, Van Coillie E, Masure S, Proost P, Van Damme J. Gelatinase B functions as regulator and effector in leukocyte biology. J Leukoc Biol. 2001 Jun;69 (6):851-9
Opstad TB, Pettersen AA, Arnesen H, Seljeflot I. The co-existence of the IL-18+183 A/G and MMP-9 -1562 C/T polymorphisms is associated with clinical events in coronary artery disease patients. PLoS One. 2013;8 (9):e74498
Owen JL, Iragavarapu-Charyulu V, Lopez DM. T cell-derived matrix metalloproteinase-9 in breast cancer: friend or foe?. Breast Dis. 2004;20:145-53
Sellebjerg F, Sorensen TL. Chemokines and matrix metalloproteinase-9 in leukocyte recruitment to the central nervous system. Brain Res Bull. 2003 Aug 15;61 (3):347-55
Shah BH, Catt KJ. Matrix metalloproteinases in reproductive endocrinology. Trends Endocrinol Metab. 2004 Mar;15 (2):47-9
Snitker S, Xie K, Ryan KA, Yu D, Shuldiner AR, Mitchell BD, Gong DW. Correlation of circulating MMP-9 with white blood cell count in humans: effect of smoking. PLoS One. 2013;8 (6):e66277
Thompson MM, Squire IB. Matrix metalloproteinase-9 expression after myocardial infarction: physiological

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