Recombinant Mouse Metalloproteinase inhibitor 1(Timp1)

Code CSB-EP023560MO
Size US$2466
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names Timp1
Uniprot No. P12032
Research Area Others
Alternative Names Timp1; Timp; Timp-1; Metalloproteinase inhibitor 1; Collagenase inhibitor 16C8 fibroblast; Erythroid-potentiating activity; EPA; TPA-S1; TPA-induced protein; Tissue inhibitor of metalloproteinases 1; TIMP-1
Species Mus musculus (Mouse)
Source E.coli
Expression Region 25-205aa
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 36.2kDa
Protein Length Full Length of Mature Protein
Tag Info N-terminal 6xHis-SUMO-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

Function Metalloproteinase inhibitor that functions by forming one to one complexes with target metalloproteinases, such as collagenases, and irreversibly inactivates them by binding to their catalytic zinc cofactor. Acts on MMP1, MMP2, MMP3, MMP7, MMP8, MMP9, MMP10, MMP11, MMP12, MMP13 and MMP16. Does not act on MMP14 (By similarity). Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades via CD63 and ITGB1. Plays a role in integrin signaling.
Gene References into Functions
  1. Study implicated TIMP1, released from the vasculature, as a mediator of the tumorpromoting effects of endothelial PECAM1, thus suggesting its potential role in the progression of metastatic tumors. PMID: 29845213
  2. miR-138 and ER stress were induced in osteoporosis and then promoted the apoptosis of osteoblasts, at least in part, through TIMP-1. PMID: 29291636
  3. TIMP-1 is upregulated in liver fibrosis and hepatocellular carcinoma, potentially implying diagnostic relevance in the non-invasive assessment of liver fibrosis or in HCC detection6. However, our study in TIMP-1-deficient mice did not confirm a functional role of TIMP-1 in the development of liver fibrosis or hepatocellular carcinoma. PMID: 28386095
  4. gingival fibroblasts cell-based therapy is a promising approach to inhibit aneurysm progression and rupture through local production of Timp-1 PMID: 28582477
  5. These results show that MMP-9/TIMP-1 system disturbance and changes of histological structure in uteri tissue are involved in fluoride-induced reproductive dysfunctions. PMID: 28064417
  6. Tissue inhibitor of matrix metalloproteinases 1 (TIMP1) inhibition resensitized tumors to gemcitabine and radiotherapy. PMID: 28765154
  7. proteomic analysis of the mesenchymal stem cells secretome identified the TIMP-1 as a potential effector molecule responsible for the anti-angiogenic properties of MSC PMID: 26898191
  8. TIMP1 signaling via CD63 leads to activation of hepatic stellate cells, which create an environment in the liver that increases its susceptibility to pancreatic tumor cells. PMID: 27506299
  9. This study highlights a previously undescribed integral role for TIMP1 in both vascular network maturation and adaptations to ischemia or alterations in flow. PMID: 27430487
  10. TIMP-1 was identified as a selectively upregulated component secreted from immature astrocytes from human pluripotent stem cells. PMID: 27134175
  11. demonstrate that TIMP-2 plays a greater protective role than TIMP-1 during the pathogenesis of atherosclerosis PMID: 26645981
  12. Our findings reveal that elevated levels of TIMP-1 impact on neutrophil homeostasis via signaling through CD63. PMID: 26001794
  13. TIMP-1 is a ligand of LRP-1 and we highlight a new example of its MMP-independent, cytokine-like functions. PMID: 25075518
  14. RAB37 regulates the exocytosis of TIMP1 in a nucleotide-dependent manner to inactivate MMP9 migration axis in vitro and in vivo and to suppress tumor metastasis. PMID: 25183545
  15. PDGF-D intensifies fibrogenesis by interfering with the fibrolytic activity of the TIMP-1/MMP-2/MMP-9 system, and PDGF-D signaling is mediated through both PDGF-alpha and -beta receptors. PMID: 25576870
  16. 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 signaling pathway. PMID: 25204377
  17. Expansion of stem cells counteracts age-related mammary regression in compound Timp1/Timp3-deficient mice. PMID: 25706237
  18. essential promoter of hepatic premetastatic niche formation PMID: 25131778
  19. TNF-alpha produced by cholestasis can promote liver fibrosis via TIMP-1 production from hepatic stellate cells. PMID: 23755201
  20. These data suggest an MMP-independent role of TIMP-1 in regulating CD4 T cell access into the CNS parenchyma during acute JHMV encephalitis PMID: 24156369
  21. miR-21 contributes to renal fibrosis by mediating MMP9/TIMP1 PMID: 23443810
  22. Gene expression of Mmp-12 and Mmp-13, and Timp-1 was strongly upregulated at all time points in RD compared with controls. Timp-2, Mmp-2, and Mmp-9 expression was modest. PMID: 24526442
  23. TIMP-1 protein was detected in synovium. PMID: 24108368
  24. Acute and chronic elevated laminar shear stress act to maintain vessel integrity through increasing TIMP-1 production, and the TGFbeta signaling pathway is essential to maintain TIMP-1 expression during chronic shear stress. PMID: 24471921
  25. study provides a unifying molecular mechanism for high angiogenic capacity of TIMP-free proMMP-9 PMID: 24174628
  26. These observations showed that Serpine-1 and Tissue inhibitor of metalloprotease type-1 did not impact the number of Staphylococcus aures bacteria accumulating at the site of skin infection. PMID: 23776165
  27. Report TIMP-1 induction in aortic smooth muscle during the development of abdominal aortic aneurysms. PMID: 24279124
  28. 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. PMID: 23825222
  29. These results not only indicate that TIMP-1 is conducive to HSPC homing; they also identify CD63 and beta1-integrin as a TIMP-1 receptor complex on HSPCs. PMID: 23660069
  30. Tpl2 is an important signal transducer for TLR activation of gene expression in Kupffer and stellate cells by the ERK pathway and that suppression of its catalytic activity may be a route toward suppressing fibrosis caused by hepatocellular injuries. PMID: 23080298
  31. Spread of Lewis lung carcinoma cells from serum to the lungs was associated with increased serum content of TIMP-1 and TIMP-2. PMID: 23113307
  32. Results show enhanced expression and widespread distribution of MMP-2, MMP-9 and their tissue inhibitors TIMP-1 and TIMP-2 in thymus from infected animals. PMID: 23089194
  33. Inhibition of MMPs by TIMP-1-overexpression results in decreased plaque progression, increased stabilization and decreased plaque rupture complications in murine vein grafts. PMID: 23071737
  34. NO. Our data support the hypothesis that reduced NO levels leads to the dysregulation of plaque clearance by decreasing the MMP-9/TIMP-1 ratio PMID: 23016931
  35. We demonstrate that ATP, acting through the P2X7 receptor, induces release of cathepsin B into the extracellular space where it degrades TIMP-1, permitting the MMP-9-dependent migration of glial cells. PMID: 23017058
  36. presence of the MMP-9/TIMP-1 heterodimers and the activated MMP-9 enzyme in the injured sciatic nerve within the first 24 h post-injury PMID: 22438979
  37. Results support the use of MMP-9 and TIMP-1 as early biomarkers for the presence and extent of perinatal brain injury in human term newborns. PMID: 22289852
  38. Results suggest the possible application of IKK2 and Timp-1 inhibitors in treating lung cancer. PMID: 22327365
  39. Results show that microglia play a central role in regulating glial cell expression of TIMP-1 and -2, and identify microglial IL-1beta as playing a key role in mediating microglial-astrocyte communication. PMID: 21631912
  40. Overexpression of intracellular tissue inhibitor of metalloproteinase 1 stimulated fibroblast proliferation in a matrix metalloproteinase independent manner by activating the p-Akt pathway and related cell cycle progression PMID: 21350939
  41. TIMP1 is a negative regulator of adipogenesis. TIMP1 leads to enlarged adipocytes in the state of overnutrition. PMID: 21437772
  42. A role for TIMP-1 in regulating HSC function, suggesting a novel mechanism presiding over stem cell quiescence in the framework of the bone marrow milieu. PMID: 21521782
  43. Both MMP-9 and TIMP-1 are highly expressed in Lewis lung cancer, and are correlated to tumor invasion and metastasis. PMID: 19624892
  44. IL-10, through regulation of the balance between MMPs and TIMP-1, suppresses the foreign body reaction against implanted biomaterials. PMID: 20661871
  45. these findings describe a previously uncharacterized role for TIMP-1 in the regulation of oligodendrocytes and astrocytes during development and provide a novel function for TIMP-1 on myelination in the developing CNS. PMID: 21508247
  46. Elevated levels of TIMP-1 in the microenvironment of tumour cells can promote metastasis by inducing HIF-1alpha-dependent HGF-signaling. PMID: 21053058
  47. Data demonstrate that long-term CNS expression of TIMP1 with complete suppression of gelatinolytic activity does not interfere with physiological brain function. PMID: 20558576
  48. Data show that leptin regulates MMP-2 and TIMP-1 activity, and collagen synthesis via p38 MAPK in mouse cardiomyocytes. PMID: 20683677
  49. These results indicate that type 1 diabetes can be prevented by TRAIL overexpression through enhancement of TIMP-1 function. PMID: 21047948
  50. Data show that wild-type mice had significantly higher levels of SOCS-3 and significantly lower levels of TIMP-1 mRNA and protein than did adiponectin KO mice exposed to both CCl(4) and leptin. PMID: 20564215
  51. A mouse model of renal insufficiency with arteriovenous fistula was developed that had increased expression of TIMP-1 at the outflow vein with venous stenosis. PMID: 20598569
  52. results suggest that BMP-2 regulates the formation of oral sulcus by altering the balance between TIMP-1 and MMP-13 PMID: 20665818
  53. TIMP-1 emerges as a modulator of neuronal outgrowth and morphology in a paracrine and autrocrine manner through the inhibition, at least in part, of MMP-2 and not MMP-9. PMID: 20011518
  54. TIMP-1 is neuroprotective against traumatic and ischemic brain injury in mice PMID: 19469687
  55. TIMP-1 expression correlates with virulence following neurotropic mouse hepatitis virus infection PMID: 12097550
  56. Tissue inhibitor of metalloproteinases-1 attenuates spontaneous liver fibrosis resolution in the transgenic mouse. PMID: 12297832
  57. observations suggests that expression of tissue inhibitor of metalloproteinase-1 during early luteal development may participate in regulation of progesterone production via its ability to regulate ovarian matrix metalloproteinase activity PMID: 12488323
  58. In a murine model of nutritionally induced obesity, TIMP-1 promotes adipose tissue development. PMID: 12574803
  59. TIMP-1 displays paradoxical effects on tumor progression suggesting that circulating TIMP-1 is efficient in suppressing lung colonization of melanoma cells. PMID: 12655789
  60. TIMP-1 has a role in inhibiting tumor growth by angiogenesis suppression PMID: 12704667
  61. TIMP-1 is upregulated in developing gonads up to 2 weeks of age and has role in the early postnatal testicular growth PMID: 12815621
  62. The gene expression and protein distribution of Timp-1 was analyzed during molar development. PMID: 12950084
  63. steroids induce uterine TIMP-1 expression and, in turn, that TIMP-1 influences TIMP-3 mRNA expression and uterine edema. PMID: 14568914
  64. tissue inhibitor of metalloproteinase 1 either directly or through modulation of matrix metalloproteinase activity may regulate myocardial remodeling following infliction of a discrete injury PMID: 14630637
  65. during early postnatal uterine development, TIMP-1 may be critical for proper endometrial gland development. PMID: 15084483
  66. TIMP-1 and TIMP-2, were significantly reduced in the urine of mice with normally regenerating livers. PMID: 15502710
  67. Myocardial TIMP-1 plays regulatory role in post-myocardial infarction remodeling, and accelerated myocardial remodeling induced by TIMP-1 gene deletion can be pharmacologically "rescued" by matrix metalloproteinase inhibition. PMID: 15598866
  68. In deficient mice after PAI-1- and TIMP-1-gene transfer, cardiomyocyte hypertrophy was moderate. PMID: 15631996
  69. protective effects of TIMP-1 in an experimental abdominal aortic aneurysm model PMID: 15680392
  70. TIMP-1 loss of function accelerated hepatocyte cell cycle progression. TIMP-1 gain of function delayed cell cycle progression. Increased hepatocyte growth factor in Timp-1(-/-)-regenerating livers. PMID: 15726641
  71. TIMP-1 contributes significantly to the regulation of acute lung injury, functioning to limit inflammation and lung permeability PMID: 15947421
  72. TIMP-1 expression is selectively upregulated in fat cells by proinflammatory adipocytokines and might play a role in maintaining adipose tissue mass in obesity. PMID: 16288749
  73. this study provides the first in vivo evidence for the implication of TIMP-1 in neuronal death and axonal sprouting in a pathological situation PMID: 16307599
  74. Astrocyte reactivity to Fas activation is attenuated in TIMP-1 deficient mice. PMID: 16316466
  75. expression of MMP-13 and TIMP-1 is regulated by Wnt3a signaling combined with BMP-2 in osteoblastic differentiation, and this signaling may in part mediate MMP-13 and TIMP-1 production during bone formation and/or remodeling PMID: 16368545
  76. TIMP-1 contributes to the development of airway fibrosis in the heterotopic tracheal transplant model, and suggest a potential role for this proteinase inhibitor in the pathogenesis of OB in patients with lung transplant. PMID: 16388023
  77. Distinct temporal and spatial expression patterns of TIMPs suggest divergent functions of these factors in incisor organogenesis. PMID: 16418837
  78. These data suggest that TIMP-1 antiapoptotic actions are mediated via the PI3-kinase and JNK signaling pathways and independent of TIMP-1 inhibition of MMP activities. PMID: 16691494
  79. These findings suggest that induction of TIMP-1 by astrocytes during EAE in WT mice represents an inherent cytoprotective response that mitigates CNS myelin injury through the regulation of both immune cell infiltration and microglial activation. PMID: 17148673
  80. Matrix metalloproteinases (MMPs) such as MMP-3 and MMP-9 were up-regulated, as further revealed by the reverse transcriptase-polymerase chain reaction (RT-PCR) and immunohistochemistry assays. PMID: 17235437
  81. Conditioned medium from an TIMP-1-overexpressing cell line demonstrates that H(2)O(2)-induced apoptosis in the H9c2 cells was significantly inhibited. PMID: 17545477
  82. Our findings suggest that TIMP-1 and TIMP-2 have a protective role for the progression of cerebral aneurysms. PMID: 17569872
  83. plasminogen activator inhibitor type 1 and tissue inhibitor of metalloproteinase 1 seem to possess gender-dependent regulatory properties, and their potential role in pathological conditions are reported. PMID: 17652357
  84. TIMP-1 may mediate atrial natriuretic peptide-induced attenuation of norepinephrine-induced hypertrophy in the mouse heart. PMID: 17982264
  85. We conclude that although TIMP-1 expression is differentially regulated in fibrosis-sensitive and fibrosis-resistant strains, epithelial overexpression of TIMP-1 does not appear to substantially alter fibrotic lung disease in mice. PMID: 18178676
  86. the role of melatonin in arresting peritoneal endometriosis in mice and a novel marker, expression ratio of proMMP-9 versus TIMP-1, was identified for assessing severity and progression of endometriosis. PMID: 18298469
  87. TIMP-1 interacts with matrix metalloproteinases and regulates matrilysin activity during airway epithelial repair. PMID: 18385523
  88. TIMP-1 may control activity of serine proteases through modulation of serine protease inhibitors such as serpinb7. PMID: 18537133
  89. TIMP-1 inhibits MMP-9 activity and can play a neuroprotective role in cerebral ischemia PMID: 18560439
  90. increased expression of MMP-2 and -9 and their protein inhibitors TIMP-1 and -2 in PMID: 18596727
  91. Plasminogen activator inhibitor-2, but not cystatin C, inhibits the prometastatic activity of tissue inhibitor of metalloproteinases-1 in the liver.( PMID: 18681831
  92. Results show differential trafficking of MMP-2, MMP-9 and TIMP-1-containing vesicles in neuronal cells and suggest that these vesicles could play a role in neuronal and synaptic plasticity. PMID: 18817873
  93. TIMP-1 plays a protective role by preventing airway hyperactivity and modulating inflammation, remodeling, and cytokine expression in an animal model of asthma. PMID: 18955015
  94. The data reveal that Timp1 mRNA is induced by leptin in the hypothalamus and that expression and action of Timp1 contributes to the regulation of feeding and energy balance. PMID: 19036876
  95. the novel TIMP-free MMP-9/FGF-2/FGFR-2 pathway in proMMP-9-induced angiogenesis in a mammalian setting. PMID: 19608737
  96. The effect of the in vivo over-expression of the TIMP-1 in osteoblasts on the severe osteopenic phenotype in Runx2 mice, was analyzed. PMID: 19780057

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Subcellular Location Secreted
Protein Families Protease inhibitor I35 (TIMP) family
Tissue Specificity Found in fetal and adult tissues. Highest levels are found in bone. Also found in lung, ovary and uterus.
Database Links

KEGG: mmu:21857

STRING: 10090.ENSMUSP00000009530

UniGene: Mm.8245

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