Matrix Metallopeptidase 3 (Stromelysin 1, Progelatinase) Protéines (MMP3)

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. De plus, nous expédions Matrix Metallopeptidase 3 (Stromelysin 1, Progelatinase) Anticorps (397) et Matrix Metallopeptidase 3 (Stromelysin 1, Progelatinase) Kits (47) et beaucoup plus de produits pour cette protéine.

afficher tous les protéines Gène GeneID UniProt
MMP3 4314 P08254
MMP3 17392 P28862
MMP3 171045  
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Top Matrix Metallopeptidase 3 (Stromelysin 1, Progelatinase) Protéines sur anticorps-enligne.fr

Showing 10 out of 51 products:

Catalogue No. Origin Source Conjugué Images Quantité Livraison Prix Détails
Cellules d'insectes Humain His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg 50 Days
$6,570.39
Détails
Escherichia coli (E. coli) Souris His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg 30 to 35 Days
$5,227.64
Détails
Escherichia coli (E. coli) Humain Inconjugué 10 μg 6 to 7 Days
$461.81
Détails
Escherichia coli (E. coli) Humain His tag,T7 tag 100 μg 15 to 18 Days
$716.00
Détails
Human Cells Humain His tag   50 μg 4 Days
$522.50
Détails
Escherichia coli (E. coli) Humain Inconjugué Validation with Western Blot 10 μg 4 to 8 Days
$330.00
Détails
Escherichia coli (E. coli) Rat His tag,T7 tag 100 μg 15 to 18 Days
$640.00
Détails
Escherichia coli (E. coli) Souris His tag,T7 tag 100 μg 15 to 18 Days
$732.00
Détails
Escherichia coli (E. coli) Humain Inconjugué   100 μg 14 to 16 Days
$958.29
Détails
HEK-293 Cells Humain His tag Validation with Western Blot 10 μg 4 to 8 Days
$396.00
Détails

MMP3 Protéines protéines par origine et source

Origin Exprimée danse Conjugué
Human , , , ,
, , , ,
Mouse (Murine)
,
Rat (Rattus) ,
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Plus protéines pour Matrix Metallopeptidase 3 (Stromelysin 1, Progelatinase) (MMP3) partenaires d'interaction

Human Matrix Metallopeptidase 3 (Stromelysin 1, Progelatinase) (MMP3) interaction partners

  1. esults show that rs2252070 inMMP-13 may confer protection effect against oral and oropharyngeal squamous cell carcinoma (SCC). In addition, the combined effects of IL-8 (rs4073), MMP-1 (rs2071230 and rs470558) and MMP-13 (rs2252070) with environmental carcinogens, such as tobacco and alcohol, are related to increased risk for oral and oropharyngeal SCC development

  2. High expression of MMP3 is associated with Systemic Lupus Erythematosus (Meta-analysis).

  3. Cyclic tensile force-upregulated IL6 increases MMP3 expression by human periodontal ligament cells

  4. genetic polymorphisms in MMP3 and TIMP2 are significantly associated with chronic Achilles tendinopathy risk in a Chinese Han population

  5. proMMP-9 from Congenital Disorder of Glycosylation patients, compared to healthy controls, showed a higher activation rate by MMP-3

  6. These results support the hypothesis that genetic variation within MMP3 contributes to inter-individual susceptibility to non-contact ACLR.

  7. MMP3 levels were significantly increased during severe rejection.

  8. KLF15 regulates the expression of MMP-3 in human chondrocytes; results suggest that KLF15 might be a novel therapeutic target of osteoarthritis

  9. Our findings indicate that MMP-3 plays an important role in Intracranial venous hypertension-related angiogenesis and the promotion of vascular remodeling

  10. Synergistic effect of l-ascorbic acid and hyaluronic acid on the expressions of matrix metalloproteinase-3 and -9 in human chondrocytes.

  11. 5A/6A polymorphism in the promoter region of the MMP3 gene may influence its transcriptional activity and impact on the degradation or push-up of extracellular matrix

  12. The levels of MMP-3 in serum and gingival crevicular fluid of patients with rheumatoid arthritis (RA) and chronic periodontitis (CP) were significantly increased. MMP-3 may be associated with the development of CP and RA.

  13. MMP-3 (-1171) 5A/6A and Lys45Glu (A/G) polymorphisms resulting in upregulation of MMP-3 in serum were associated with the decline of lung function among chronic obstructive pulmonary disease.

  14. MMP3 was higher in rheumatoid factor negative rheumatoid arthritis than in rheumatoid factor positive rheumatoid arthritis, undifferentiated arthritis, and controls.

  15. Our results indicated that the levels of MMP-3 in gastric mucosa were not different between H. pyloripositive and H. pylori-negative patients and there was no correlation between the MMP-3 levels and virulence factor (cagA and vacA allelic variants), and type of disease (gastritis and PUD) in patients infected with H. pylori.

  16. This experiments showed that MMP3 is dynamically regulated by seizures as shown by increased expression in TLE tissue and during different phases of epileptogenesis.

  17. IL-1beta C/T and MMP3 5A/6A polymorphisms are associated with an increased risk of developing hepatocellular carcinoma in Egyptian patients.

  18. High circulating MMP3 levels were independently associated with sarcopenia in rheumatoid arthritis patients.

  19. The prevalence of knee chondrocalcinosis was low in the Japanese population and was positively correlated with serum MMP-3 concentration.

  20. Matrix Metalloproteinase-3 (MMP3) is a direct target of miR-519d.

Mouse (Murine) Matrix Metallopeptidase 3 (Stromelysin 1, Progelatinase) (MMP3) interaction partners

  1. Study in transgenic mice found that barrier breakdown and expression of inflammatory factors contribute to development of serrated polyps. Subsets of cecal PDGFRA+ fibroblasts are activated by release of Il1b from myeloid cells during the early stages of serrated polyp development. Mmp3 produced by PDGFRA+ fibroblasts is important for serrated polyp development.

  2. Targeted knockdown of MMP3 attenuates proliferation, migration, and invasion of the metastatic adenocarcinoma cells. Nuclear PEX domain/MMP3 localized in primary tumor-stroma marginal area and lung-metastatic tumor nodules.

  3. Thrombin exclusively induced MCP-1 via the MAPK-ERK and PI3K-AKT pathways. MCP-1 produced by mIVDs induced macrophage migration and thrombin treatment increased MMP-3 production to induce mIVD degeneration. These effects of thrombin on mIVDs were abrogated by a PAR1 inhibitor and suggest that thrombin may be a novel factor capable of stimulating cytokine activity implicated in the regulation several aspects of mIVDs

  4. SOST(transgenic) had approximately 2-fold less MMP activation than WT or Sost(-/-) , and this was supported by a significant reduction in MMP2/3 protein levels.

  5. that the impact of MMP3 on neuronal morphology may be regionspecific

  6. BMAL1 Deficiency Contributes to Mandibular Dysplasia by Upregulating MMP3.

  7. Estrogen-related receptor gamma (ERRgamma) overexpression in chondrocytes directly upregulates matrix metalloproteinase (MMP)-3 and MMP13, which are known to play crucial roles in cartilage destruction in osteoarthritis (OA).

  8. MMP3 contributes to the pathogenesis of ARDS by affecting the pulmonary inflammatory response in female mice in relevant models of lung injury.

  9. endogenously secreted chemerin plays an autocrine/paracrine role in white adipose tissue, identifying chemerin as a therapeutic target to modulate adipose remodelling.

  10. Overexpression of Mmp3 in 3T3-L1 preadipocytes inhibited differentiation. High fat diet-induced obesity downregulates adipocyte MMP3 expression to trigger adipogenesis, and adipocyte TIMP4 may modulate this process to regulate hyperplastic vs. hypertrophic adipose tissue expansion, fat distribution, and metabolic health in a sex- and depot-dependent manner.

  11. Matrix metalloprotease 3 (MMP3), an endogenous neuronal activator of microglia, increased cytokine release from YAC128 microglia compared to wildtype microglia. We found elevated MMP levels in Huntington's Disease (HD) CSF, and MMP levels correlate with disease severity in HD. These data support a novel role for MMPs and microglial activation in HD pathogenesis.

  12. These results indicate that periodic induction, via use of an eye drop, of AAV-mediated secretion of MMP-3 into aqueous humour could have therapeutic potential for those cases of glaucoma that are sub-optimally responsive to conventional pressure-reducing medications.

  13. Data show that loss of loss of matrix metalloproteinase-3 (MMP-3) repressed the upregulation of the chemokines monocyte chemoattractant protein (MCP)-1 and (C-X-C motif) ligand 1 (CXCL1).

  14. Mmp3-knockout mice maintained higher arterial oxygenation compared to wild-type mice in a model of acute lung injury.

  15. NMP4 deficiency suppressed the arthritis-induced increase in bone resorption, expression of RANKL and MMP-3 mRNA.

  16. MMP-3 produced in blood vessel endothelial cells after spinal cord injury serves as an endogenous molecule for microglial activation followed by p38MAPK activation and proNGF production

  17. genetic inactivation of MMP-3 has profound effects on the structural integrity and plasticity response of the visual cortex of adult mice

  18. study found significant increases of MMP-3 and MMP-12 mRNA levels and MMP12 zymographic activities in response to Cryptococcus neoformans infection but not C. gattii infection

  19. This study demonstrates the sequential involvement of Wnt5, MMP-3, DMP-1 expression, and DMP-1 degradation products by MMP-3, in effecting IL-1beta-induced proliferation of ESC-derived odontoblast-like cells.

  20. Study suggests that MMP-3 modulates intracellular MAP kinase signaling pathway and as such, influences a molecular chaperone that regulates cytoskeletal components important for neurite outgrowth, neuronal migration and dendritic arborization

Pig (Porcine) Matrix Metallopeptidase 3 (Stromelysin 1, Progelatinase) (MMP3) interaction partners

  1. The present study was aimed to determine the association between metalloproteinase 3 (MMP3), transforming growth factor beta 1 (TGFbeta1) and collagen type X alpha I (COL10A1) gene polymorphisms with traits related to leg weakness in pigs.

  2. the identification of MMP1 and MMP10 genes in swine is reported.

  3. contribution of MMPs to the inflammatory breakdown of the blood-CSF barrier in vitro

  4. Results indicate that leukemia inhibitory factor (LIF) and Oncostatin M increase the expression of MMP-1, MMP-3, and TIMP-1 several fold, and that their expression is reduced to basal levels in the presence of the LIF antagonist MH35-BD.

Rabbit Matrix Metallopeptidase 3 (Stromelysin 1, Progelatinase) (MMP3) interaction partners

  1. Compromised autophagy may be related to the osteoarthritis progression; JNK and p38 MAPKs up-regulate MMP3 and down-regulate autophagy.

  2. the total content and active forms of matrix metalloproteinases (MMPs)-1, -3, and -13 was measured to assess the potential role of the mechanical environment in regulation of matrix turnover by ligament fibroblasts.

  3. chitosan-pDNA nanoparticles encoding shRNA targeting MMP-3 and -13 had great potential in silencing the dedifferentiation-related genes for regenerating prolonged and endurable cartilage.

  4. Ulinastatin effectively inhibited the increased expression of MMP-2, MMP-3, and iNOS in degenerated NP cells induced by IL-1beta in vitro.

  5. Exposure to long periods of light irrespective of its characteristics leads to the increased expression of some matrix metalloprpteases.

  6. Tongxinluo can inhibit the expression of MMP-3 and 9 and increase the expression of PPARgamma in atherosclerotic rabbits.

Profil protéine Matrix Metallopeptidase 3 (Stromelysin 1, Progelatinase) (MMP3)

Profil protéine

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. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.

Gene names and symbols associated with MMP3

  • matrix metallopeptidase 3 (MMP3)
  • matrix metallopeptidase 3 (Mmp3)
  • matrix metallopeptidase 3 (stromelysin 1, progelatinase) (MMP3)
  • matrix metallopeptidase 3 L homeolog (mmp3.L)
  • chds6 Protéine
  • mmp-3 Protéine
  • mmp3 Protéine
  • MMP10 Protéine
  • mmp13 Protéine
  • sl-1 Protéine
  • SLN-1 Protéine
  • SLN1 Protéine
  • stmy Protéine
  • stmy1 Protéine
  • STR-1 Protéine
  • str1 Protéine

Protein level used designations for MMP3

matrix metalloproteinase 3 (stromelysin 1, progelatinase) , matrix metalloproteinase-3 , proteoglycanase , stromelysin-1 , transin-1 , EMS-2 , MMP-3 , SL-1 , matrix metalloproteinase 3 , progelatinase , stromelysin 1 , PTR1 protein , stromelysin , metalloproteinase 3 receptor , matrix metallopeptidase 3 (stromelysin 1, progelatinase) , matrix metallopeptidase 3 L homeolog , matrix metalloproteinase 13 (collagenase 3)

GENE ID SPECIES
4314 Homo sapiens
17392 Mus musculus
171045 Rattus norvegicus
396769 Sus scrofa
100009111 Oryctolagus cuniculus
100034195 Equus caballus
403445 Canis lupus familiaris
281309 Bos taurus
101118895 Ovis aries
446898 Xenopus laevis
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