Browse our Metalloproteinase Inhibitor 2 Proteins (TIMP2)

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Metalloproteinase Inhibitor 2 Proteins (TIMP2)
On are 43 Metalloproteinase Inhibitor 2 (TIMP2) Proteins from 15 different suppliers available. Additionally we are shipping Metalloproteinase Inhibitor 2 Antibodies (308) and Metalloproteinase Inhibitor 2 Kits (103) and many more products for this protein. A total of 466 Metalloproteinase Inhibitor 2 products are currently listed.
CSC-21K, D11Bwg1104e, DDC8, etID32613.12, fa96h09, Timp-2, timp2, wu:fa96h09, zgc:136726
list all proteins Gene Name GeneID UniProt
TIMP2 7077 P16035
TIMP2 29543 P30121
TIMP2 21858  

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Metalloproteinase Inhibitor 2 Proteins (TIMP2) by Origin

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Top referenced Metalloproteinase Inhibitor 2 Proteins

  1. Human TIMP2 Protein expressed in HEK-293 - ABIN2666719 : Bourboulia, Stetler-Stevenson: Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs): Positive and negative regulators in tumor cell adhesion. in Seminars in cancer biology 2010 (PubMed)
    Show all 5 references for 2666719

  2. Human TIMP2 Protein expressed in Human Cells - ABIN2002771 : Seo, Li, Guedez, Wingfield, Diaz, Salloum, Wei, Stetler-Stevenson: TIMP-2 mediated inhibition of angiogenesis: an MMP-independent mechanism. in Cell 2003 (PubMed)
    Show all 3 references for 2002771

  3. Human TIMP2 Protein expressed in Human Cells - ABIN2002769 : Stetler-Stevenson, Krutzsch, Liotta: TIMP-2: identification and characterization of a new member of the metalloproteinase inhibitor family. in Matrix (Stuttgart, Germany). Supplement 1993 (PubMed)
    Show all 3 references for 2002769

  4. Human TIMP2 Protein expressed in HEK-293 Cells - ABIN2181824 : Stetler-Stevenson, Krutzsch, Liotta: Tissue inhibitor of metalloproteinase (TIMP-2). A new member of the metalloproteinase inhibitor family. in The Journal of biological chemistry 1989 (PubMed)
    Show all 3 references for 2181824

  5. Human TIMP2 Protein expressed in Escherichia coli (E. coli) - ABIN1098377 : Bahudhanapati, Zhang, Sidhu, Brew: Phage display of tissue inhibitor of metalloproteinases-2 (TIMP-2): identification of selective inhibitors of collagenase-1 (metalloproteinase 1 (MMP-1)). in The Journal of biological chemistry 2011 (PubMed)
    Show all 2 references for 1098377

  6. Human TIMP2 Protein expressed in Escherichia coli (E. coli) - ABIN1047368 : Stetler-Stevenson, Brown, Onisto, Levy, Liotta: Tissue inhibitor of metalloproteinases-2 (TIMP-2) mRNA expression in tumor cell lines and human tumor tissues. in The Journal of biological chemistry 1990 (PubMed)
    Show all 2 references for 1047368

More Proteins for Metalloproteinase Inhibitor 2 Interaction Partners

Human Metalloproteinase Inhibitor 2 (TIMP2) interaction partners

  1. High TIMP2 expression is associated with acute kidney injury.

  2. High TIMP2 expression is associated with acute kidney injury.

  3. expression of TIMP2 was inversely associated with miR (show MLXIP Proteins)-106a in nodule tissues. Apoptotic body was also seen under electron microscope accompanied by silencing of miR (show MLXIP Proteins)-106a. Together, this data indicated that miR (show MLXIP Proteins)-106a may act as an oncogene (show RAB1A Proteins) and contribute to gastric cancer development.

  4. Data show that the mean values for TIMP1 (show TIMP1 Proteins), TIMP2 and MMP2 (show MMP2 Proteins) were lower in survivors, MMP9 (show MMP9 Proteins) was higher in survivors.

  5. Urine [TIMP-2]*[IGFBP7 (show IGFBP7 Proteins)] is a promising candidate for early detection of AKI, especially in ruling-out AKI

  6. We conclude that in the resected esophageal cancer an increased mRNA expression of MMP-7 (show MMP7 Proteins), MMP-10 (show MMP10 Proteins) and TIMP-1 (show TIMP1 Proteins) correlated with clinicopathologic features. We suggest that these genes may play a role during progression of the disease. MMP-10 (show MMP10 Proteins), MMP-7 (show MMP7 Proteins), TIMP-1 (show TIMP1 Proteins), TIMP-2 were overexpressed in 73%, 85%, 55% and 42% of esophageal cancer samples, respectively.

  7. At hospital admission, all viral gastroenteritis (GE) patients viral gastroenteritis (GE) patients demonstrated increased MMP-9 (show MMP9 Proteins) and decreased MMP-2 (show MMP2 Proteins) and TIMP-2 serum levels; kinetics of serum MMP-2 (show MMP2 Proteins), MMP-9 (show MMP9 Proteins), and TIMP-2 levels were similar among the viral GE patients but distinct from bacterial enteritis patients; involvement of MMPs and TIMPs in the pathophysiology of gastrointestinal symptoms likely varies depending on the

  8. Meta-analysis indicated that urinary [TIMP-2].[IGFBP7 (show IGFBP7 Proteins)] may be a reliable biomarker for the early detection of acute kidney injury in adults.

  9. Results show that resistant hypertension was associated with higher TIMP-2 levels and low MMP-2 (show MMP2 Proteins)/TIMP-2 ratio, suggesting that these regulators of ECM (show MMRN1 Proteins) remodeling play a key role in blood pressure control in this high-risk subset of hypertensive individuals.

  10. TIMP-2 is both expressed and secreted preferentially by cells of distal tubule origin, while IGFBP7 (show IGFBP7 Proteins) is equally expressed across tubule cell types yet preferentially secreted by cells of proximal tubule origin. In human kidney tissue, strong staining of IGFBP7 (show IGFBP7 Proteins) was seen in the luminal brush-border region of a subset of proximal tubule cells, and TIMP-2 stained intracellularly in distal tubules.

Cow (Bovine) Metalloproteinase Inhibitor 2 (TIMP2) interaction partners

  1. Data indicate the involvement of PKC-alpha (show PKCa Proteins) in proMMP-2 activation and inhibition of TIMP-2 expression by NF-kappaB (show NFKB1 Proteins)-MT1-MMP (show MMP14 Proteins)-dependent and -independent pathway.

  2. A differential pattern of matrix metalloproteinase-2 (show MMP2 Proteins) and Tissue inhibitor metalloproteinase-2 was observed in cow uteri with adenomyosis.

  3. MMP-14 (show MMP14 Proteins), MMP-2 (show MMP2 Proteins) and TIMP-2 are co-localized in the fetal compartment and therefore could influence the timely release of fetal membranes in cattle.

  4. Results describe distinct changes in expression of MMP2 (show MMP2 Proteins), MMP14 (show MMP14 Proteins), and the metallopeptidase (show ECEL1 Proteins) inhibitor TIMP2 between different phases of the estrous cycle indicating an endocrine regulation.

  5. Production of TIMP-1 (show TIMP1 Proteins) was augmented by IL-1alpha, TNFalpha (show TNF Proteins), and hepatocyte growth factor (show HGF Proteins) at level of translation and was transcriptionally increased by 12-O-tetradecanoylphorbol 13-acetate. Level of TIMP-2 mRNA was not affected by any treatments.

  6. the different temporal expression patterns of TIMP-1 (show TIMP1 Proteins) and TIMP-2 suggest that TIMP-1 (show TIMP1 Proteins) may be important for luteal formation and development, while TIMP-2 may play significant roles during luteal development and maintenance

  7. Identification, purification and partial characterization of timp-2 in bovine pulmonary artery smooth muscle

  8. Results describe the isolation of matrix metalloproteinase 2 (MMP-2 (show MMP2 Proteins)) from the MMP-2 (show MMP2 Proteins)/tissue inhibitor of metalloproteinase 2 (TIMP-2) complex, and the characterization of both isolated MMP-2 (show MMP2 Proteins) and the complex itself.

  9. oxidants inactivate TIMP-2, and the resulting activation of MMP-2 (show MMP2 Proteins) subsequently inhibits Na+ dependent Ca2 (show CA2 Proteins)+ uptake in the microsomes

  10. TIMP-2 has a role in the pericyte-induced stabilization of newly formed vascular networks that are predisposed to undergo regression and reveal specific molecular targets of the inhibitors regulating these events.

Horse (Equine) Metalloproteinase Inhibitor 2 (TIMP2) interaction partners

  1. The pathology of laminitis is associated with increased and lowered transcription of MMP-14 (show MMP14 Proteins) and TIMP-2, respectively.

Mouse (Murine) Metalloproteinase Inhibitor 2 (TIMP2) interaction partners

  1. the protein expression levels of TIMP-2 and PBEF (show NAMPT Proteins) in cloned placentae, were examined.

  2. demonstrate that TIMP-2 plays a greater protective role than TIMP-1 (show TIMP1 Proteins) during the pathogenesis of atherosclerosis

  3. Further investigation of MMP2 (show MMP2 Proteins) inhibitors of TIMP2/TIMP4 (show TIMP4 Proteins) showed an upregulated TIMP2 expression, but not TIMP4 (show TIMP4 Proteins). low-dose pre-radiation attenuates the skin inflammation and ROS (show ROS1 Proteins) production induced by medium-dose UV radiation

  4. TIMP2 and TIMP3 (show TIMP3 Proteins) play fundamental and differential roles in mediating pathological remodelling, independent from their MMP-inhibitory function

  5. Reduced beta(2)GP I plays a role in diabetic mice related to vascular protection, inhibiting vascular lipid deposition, and plaque formation by reducing MMPs/TIMPs expression through down-regulation of the p38MAPK (show MAPK14 Proteins) signaling pathway.

  6. High TIMP2 expression is associated with liver fibrosis.

  7. TIMP2 promotes kidney injury through metalloproteinase (MMP)2 (show MMP2 Proteins) activation

  8. Gene expression of Mmp-12 (show MMP12 Proteins) and Mmp-13 (show MMP13 Proteins), and Timp-1 (show TIMP1 Proteins) was strongly upregulated at all time points in RD compared with controls. Timp-2, Mmp-2 (show MMP2 Proteins), and Mmp-9 (show MMP9 Proteins) expression was modest.

  9. Data indicate a significantly increased expression of type I collagen, TIMP-2, TGF-beta (show TGFB1 Proteins), PAI-1 (show SERPINE1 Proteins) and RAGE (show AGER Proteins) in diabetic db/db (show LEPR Proteins) cells.

  10. This study suggests that miR-17 participates in the regulation of cardiac matrix remodeling and provides a novel therapeutic approach using miR-17 inhibitors to prevent remodeling and heart failure after MI.

Zebrafish Metalloproteinase Inhibitor 2 (TIMP2) interaction partners

  1. To further study the function of TIMP-2 in development, we utilized zebrafish as an experimental model system

  2. membrane-type 1 metalloproteinase, gelatinase A (show MMP2 Proteins) , and tissue inhibitor 2 of metalloproteinases mRNA transcripts were expressed in the blastema

Metalloproteinase Inhibitor 2 (TIMP2) Protein Profile

Protein Summary

This gene is a member of the TIMP gene family. The proteins encoded by this gene family are natural inhibitors of the matrix metalloproteinases, a group of peptidases involved in degradation of the extracellular matrix. In addition to an inhibitory role against metalloproteinases, the encoded protein has a unique role among TIMP family members in its ability to directly suppress the proliferation of endothelial cells. As a result, the encoded protein may be critical to the maintenance of tissue homeostasis by suppressing the proliferation of quiescent tissues in response to angiogenic factors, and by inhibiting protease activity in tissues undergoing remodelling of the extracellular matrix.

Alternative names and synonyms associated with Metalloproteinase Inhibitor 2 (TIMP2)

  • TIMP metallopeptidase inhibitor 2 (TIMP2)
  • TIMP metallopeptidase inhibitor 2 (Timp2)
  • tissue inhibitor of metalloproteinase 2 (Timp2)
  • tissue inhibitor of metalloproteinase 2a (timp2a)
  • CSC-21K protein
  • D11Bwg1104e protein
  • DDC8 protein
  • etID32613.12 protein
  • fa96h09 protein
  • Timp-2 protein
  • timp2 protein
  • wu:fa96h09 protein
  • zgc:136726 protein

Protein level used designations for TIMP2

TIMP-2 , metalloproteinase inhibitor 2 , tissue inhibitor of metalloproteinase 2 , tissue inhibitor of metalloproteinases 2 , collagenase inhibitor , tissue inhibitor of mettaloproteinase 2 , tissue inhibitor of metalloproteinase-2 , tissue inhibitor of matrix metalloproteinase-2 , metalloproteinase inhibitor TIMP-2

7077 Homo sapiens
29543 Rattus norvegicus
282093 Bos taurus
100008689 Oryctolagus cuniculus
374178 Gallus gallus
396988 Sus scrofa
100034134 Equus caballus
403633 Canis lupus familiaris
743167 Pan troglodytes
100217406 Ovis aries
21858 Mus musculus
100135629 Cavia porcellus
359835 Danio rerio
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