SRP6271
MMP-9 human
recombinant, expressed in HEK 293 cells, ≥95% (SDS-PAGE)
Synonym(s):
CLG4B, GELB, MANDP2, MMP-9, Matrix Metalloproteinase-9
Sign Into View Organizational & Contract Pricing
All Photos(1)
About This Item
UNSPSC Code:
12352202
NACRES:
NA.32
biological source
human
recombinant
expressed in HEK 293 cells
tag
6-His tagged (C-terminus)
Assay
≥95% (SDS-PAGE)
form
lyophilized powder
mol wt
calculated mol wt 50.8 kDa
observed mol wt 55-65 kDa (DTT-reduced. Protein migrates due to different glycosylation. Ala 20 is the predicted N-terminus.)
packaging
pkg of 10 and 50 μg
impurities
<1 EU/μg endotoxin (LAL test)
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... MMP-9(4318)
General description
Most MMPs (matrix metalloproteinases) are secreted as inactive pro-proteins which are activated when cleaved by extracellular proteinases. MMP-9, also known as 92kDa type IV collagenase, 92kDa gelatinase/gelatinase B (GELB), CLG4B, is secreted from neutrophils, macrophages, and a number of transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. Structurally, MMP-9 maybe be divided into five distinct domains: a pro-domain which is cleaved upon activation, a gelatin binding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a proline rich linker region, and a carboxyl terminal hemopexin like domain.
Application
MMP-9 human has been used as a standard in gelatin zymography.
Biochem/physiol Actions
Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Studies in rhesus monkeys suggest that MMP-9 is involved in IL-8 (interleukin-8)-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling. Thrombospondins, intervertebral disc proteins, regulate the effective levels of MMP-2 and -9, which are key effectors of ECM (extracellular matrrix) remodeling. This enzyme degrades various substrates including gelatin, collagen types IV and V, and elastin. MMP-9 is involved in a variety of autoimmune diseases such as systemic lupus erythematosus, rheumatoid arthritis, and multiple sclerosis, and be regarded as a potential therapeutic target. It is also associated with lumbar-disc herniation and metaphyseal anadysplasia.
Physical form
Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Generally 5-8% Mannitol or trehalose is added as a protectant before lyophilization.
Reconstitution
Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 μg/mL. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
Already Own This Product?
Find documentation for the products that you have recently purchased in the Document Library.
Thrombospondin-1 suppresses spontaneous tumor growth and inhibits activation of matrix metalloproteinase-9 and mobilization of vascular endothelial growth factor.
Rodriguez-Manzaneque JC, et al.
Proceedings of the National Academy of Sciences of the USA, 98, 12485-12490 (2001)
Prevention of interleukin-8-induced mobilization of hematopoietic progenitor cells in rhesus monkeys by inhibitory antibodies against the metalloproteinase gelatinase B (MMP-9).
Pruijt JF, et al.
Proceedings of the National Academy of Sciences of the USA, 96, 10863-10868 (1999)
Shimin Zhang et al.
Theriogenology, 151, 144-150 (2020-04-29)
Successful implantation is closely linked to the expression of MMP-2 and MMP-9, which greatly influence the ability of an embryo to degrade the basement membrane of the uterine epithelium, mainly composed of type IV collagen, and invade the uterine stroma.
Enhanced expression of MMP-7 and MMP-9 in demyelinating multiple sclerosis lesions.
Cossins JA, et al.
Acta Neuropathologica, 94, 590-598 (1997)
Xuan Gao et al.
ACS applied materials & interfaces, 9(35), 29457-29468 (2017-08-12)
Interstitial fluid pressure (IFP) in tumor is much higher than that in normal tissue, and it constitutes a great obstacle for the delivery of antitumor drugs, thus becoming a potential target for cancer therapy. In this study, cationic nanostructured lipid
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
Contact Technical Service