Recombinant Mouse TIMP-1 Protein

Name: Recombinant Mouse TIMP-1 Protein
Brand: Beta LifeScience
SKU: BL-1918NP
Availability: InStock

BL-1918NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Tissue Inhibitors Of Metalloproteinases 1 is produced by our Mammalian expression system and the target gene encoding Cys25-Arg205 is expressed.
Accession	P12032
Synonym	Metalloproteinase Inhibitor 1; Erythroid-Potentiating Activity; EPA; Fibroblast collagenase Inhibitor; Collagenase Inhibitor; Tissue Inhibitor of Metalloproteinases 1; TIMP-1; TIMP1; CLGI; TIMP
Gene Background	Mouse Tissue Inhibitor of Metalloproteinases 1 (TIMP-1) is a member of TIMP family. The homologous proteins of TIMPs regulate the activity of matrix metalloproteinases (MMPs), including inhibition of active MMPs, proMMP activation, cell growth promotion, matrix binding, inhibition of angiogenesis and the induction of apoptosis. Timp-1 complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. It also mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. It is known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13, and MMP-16, without MMP-14.
Molecular Mass	20.2 KDa
Apmol Mass	26 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, pH 8.0.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

Target Details

Target 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. 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.
Subcellular Location	Secreted.
Protein Families	Protease inhibitor I35 (TIMP) family
Database References	KEGG: mmu:21857 STRING: 10090.ENSMUSP00000009530 UniGene: PMID: 29845213 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 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 gingival fibroblasts cell-based therapy is a promising approach to inhibit aneurysm progression and rupture through local production of Timp-1 PMID: 28582477 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 Tissue inhibitor of matrix metalloproteinases 1 (TIMP1) inhibition resensitized tumors to gemcitabine and radiotherapy. PMID: 28765154 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 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 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 TIMP-1 was identified as a selectively upregulated component secreted from immature astrocytes from human pluripotent stem cells. PMID: 27134175 demonstrate that TIMP-2 plays a greater protective role than TIMP-1 during the pathogenesis of atherosclerosis PMID: 26645981 Our findings reveal that elevated levels of TIMP-1 impact on neutrophil homeostasis via signaling through CD63. PMID: 26001794 TIMP-1 is a ligand of LRP-1 and we highlight a new example of its MMP-independent, cytokine-like functions. PMID: 25075518 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 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 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 Expansion of stem cells counteracts age-related mammary regression in compound Timp1/Timp3-deficient mice. PMID: 25706237 essential promoter of hepatic premetastatic niche formation PMID: 25131778 TNF-alpha produced by cholestasis can promote liver fibrosis via TIMP-1 production from hepatic stellate cells. PMID: 23755201 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 miR-21 contributes to renal fibrosis by mediating MMP9/TIMP1 PMID: 23443810 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 TIMP-1 protein was detected in synovium. PMID: 24108368 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 study provides a unifying molecular mechanism for high angiogenic capacity of TIMP-free proMMP-9 PMID: 24174628 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 Report TIMP-1 induction in aortic smooth muscle during the development of abdominal aortic aneurysms. PMID: 24279124 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 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 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 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 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 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 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 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 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 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 Results suggest the possible application of IKK2 and Timp-1 inhibitors in treating lung cancer. PMID: 22327365 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 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 TIMP1 is a negative regulator of adipogenesis. TIMP1 leads to enlarged adipocytes in the state of overnutrition. PMID: 21437772 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 Both MMP-9 and TIMP-1 are highly expressed in Lewis lung cancer, and are correlated to tumor invasion and metastasis. PMID: 19624892 IL-10, through regulation of the balance between MMPs and TIMP-1, suppresses the foreign body reaction against implanted biomaterials. PMID: 20661871 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 Elevated levels of TIMP-1 in the microenvironment of tumour cells can promote metastasis by inducing HIF-1alpha-dependent HGF-signaling. PMID: 21053058 Data demonstrate that long-term CNS expression of TIMP1 with complete suppression of gelatinolytic activity does not interfere with physiological brain function. PMID: 20558576 Data show that leptin regulates MMP-2 and TIMP-1 activity, and collagen synthesis via p38 MAPK in mouse cardiomyocytes. PMID: 20683677 These results indicate that type 1 diabetes can be prevented by TRAIL overexpression through enhancement of TIMP-1 function. PMID: 21047948 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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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Recombinant Mouse TIMP-1 Protein

Recombinant Mouse TIMP-1 Protein

Product Overview

Target Details

FAQs