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Manufactured by BioVendor

Matrix Metalloproteinase-9 Human HEK293

  • Regulatory status:RUO
  • Type:Recombinant
  • Source:HEK293
  • Other names:Matrix Metalloproteinase-9. MMP9
  • Species:Human
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Cat. No. Size Price


New RD172439100 0.1 mg
PubMed Product Details
Technical Data

Type

Recombinant

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 LC-MS/MS.

Amino Acid Sequence

APRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTRDGNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFPFTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSERPTAGPTGPPSAGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKWPALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGRRLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYDILQCPEDHHHHHH

Source

HEK293

Purity

Purity as determined by densitometric image analysis: >95%

SDS-PAGE Gel

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

  1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
  2. Reduced and boiled sample, 2.5 μg/lane
  3. 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.

LAL to determine quantity of endotoxin.

Note

This product is intended for research use only.

Summary

Research topic

Immune Response, Infection and Inflammation, Neural tissue markers, Oncology, Others

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

References to Summary

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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