Yes, as stated in the PROPERTIES section of the product page, this item includes a 6-His tag at the C-terminus.
SRP6271
MMP-9 human
recombinant, expressed in HEK 293 cells, ≥95% (SDS-PAGE)
Sinônimo(s):
CLG4B, GELB, MANDP2, MMP-9, Matrix Metalloproteinase-9
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About This Item
Código UNSPSC:
12352202
NACRES:
NA.32
Produtos recomendados
fonte biológica
human
recombinante
expressed in HEK 293 cells
etiqueta
6-His tagged (C-terminus)
Ensaio
≥95% (SDS-PAGE)
Formulário
lyophilized powder
peso molecular
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.)
embalagem
pkg of 10 and 50 μg
Impurezas
<1 EU/μg endotoxin (LAL test)
nº de adesão UniProt
Condições de expedição
wet ice
temperatura de armazenamento
−20°C
Informações sobre genes
human ... MMP-9(4318)
Descrição geral
Most MMPs (matrix metalloproteinases) are secreted as inactive pro-proteins which are activated when cleaved by extracellular proteinases.[1] 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.[2] 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.[3][4]
Aplicação
MMP-9 human has been used as a standard in gelatin zymography.[5]
Ações bioquímicas/fisiológicas
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.[1] 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.[2] Thrombospondins, intervertebral disc proteins, regulate the effective levels of MMP-2 and -9, which are key effectors of ECM (extracellular matrrix) remodeling.[6] This enzyme degrades various substrates including gelatin, collagen types IV and V, and elastin.[3] 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.[7][8] It is also associated with lumbar-disc herniation and metaphyseal anadysplasia.[9][10]
forma física
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.
Reconstituição
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.
Código de classe de armazenamento
11 - Combustible Solids
Classe de risco de água (WGK)
WGK 3
Ponto de fulgor (°F)
Not applicable
Ponto de fulgor (°C)
Not applicable
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Enhanced expression of MMP-7 and MMP-9 in demyelinating multiple sclerosis lesions.
Cossins JA, et al.
Acta Neuropathologica, 94, 590-598 (1997)
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.
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)
Lin Liu et al.
Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie, 117, 109096-109096 (2019-06-16)
The distant metastasis in gastric has become an obstacle for treatment in clinic. However, the underlying mechanism is not well illustrated. Here, our aim is to reveal the mechanism and try to explore the potential strategy to overcome the distant
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Does this recombinant protein MMP 9, SRP6271 have a His tag?
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