Recombinant Mouse Metalloproteinase Inhibitor 3 (TIMP3) Protein (His&Myc)

Name: Recombinant Mouse Metalloproteinase Inhibitor 3 (TIMP3) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-06230P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Metalloproteinase Inhibitor 3 (TIMP3) Protein (His&Myc) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Activity	Not tested.
Uniprotkb	P39876
Target Symbol	TIMP3
Synonyms	Tissue inhibitor of metalloproteinases 3;TIMP-3
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-10His&C-Myc
Target Protein Sequence	CTCSPSHPQDAFCNSDIVIRAKVVGKKLVKEGPFGTLVYTIKQMKMYRGFSKMPHVQYIHTEASESLCGLKLEVNKYQYLLTGRVYEGKMYTGLCNFVERWDHLTLSQRKGLNYRYHLGCNCKIKSCYYLPCFVTSKNECLWTDMLSNFGYPGYQSKHYACIRQKGGYCSWYRGWAPPDKSISNATDP
Expression Range	24-211aa
Protein Length	Full Length of Mature Protein
Mol. Weight	29.1 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli.
Subcellular Location	Secreted, extracellular space, extracellular matrix.
Protein Families	Protease inhibitor I35 (TIMP) family
Database References	KEGG: mmu:21859 STRING: 10090.ENSMUSP00000020234 UniGene: PMID: 29456135 altered cortical and trabecular bone mineralization and increased compositional heterogeneity were found in Timp-3 (-/-) bone, all being indicative of high bone remodeling PMID: 28236102 In a clinically relevant CADASIL mouse model, we show that exogenous ADAM17 or HB-EGF restores cerebral arterial tone and blood flow responses, and identify upregulated voltage-dependent potassium channel (KV) number in cerebral arterial myocytes as a heretofore-unrecognized downstream effector of TIMP3-induced deficits. PMID: 27476853 TIMP3 promotes normal microvascular endothelial cell barrier function, at least partially, through inhibition of metalloproteinase-dependent disruption of adherens junctions, and septic downregulation of TIMP3 may contribute to septic MVEC barrier dysfunction. PMID: 26993226 data strongly suggest that TIMP3 has direct neuroprotective effects that can mitigate the deleterious effects associated with TBI, an area with few if any therapeutic options. PMID: 26299440 Elevated levels of TIMP3 and vitronectin, acting downstream of Notch3(ECD) deposition, play a role in CADASIL, producing divergent influences on early CBF deficits and later white matter lesions. PMID: 26648042 4-Hydroxyisoleucine improved insulin resistant-like state in 3T3-L1 adipocytes by targeting TACE/TIMP3 and the insulin signaling pathway. PMID: 26527864 In a mouse model of prostate cancer, increased tumor growth, proliferation index, increased microvascular density, and invasion was observed in Pten(-/-), Timp3(-/-) prostate tumors compared to Pten(-/-), Timp3(+/+) tumors. PMID: 26332574 Timp3 status determines p53, p38 and Notch coactivation to instruct hepatic cell fate and transformation. PMID: 25347747 lack of TIMP3 increases inflammation and polarizes macrophages towards a more inflammatory phenotype resulting in increased atherosclerosis. PMID: 24943223 TIMP-3 KO mice exhibit enhanced metabolism, as reflected by a higher body temperature than WT mice, possibly due to increased mitochondrial activity. PMID: 24736588 TIMP3 protects kidney from damage PMID: 23760282 TIMP3 reduction is due, at least in part, to increased expression of certain TIMP3-targeting microRNAs in diabetic kidneys compared to healthy controls. PMID: 23797704 Demonstrate a critical role for TIMP3, among all TIMPs, in preserving arterial remodelling in response to Ang II-induced hypertension. PMID: 23524300 TIMP-3 functions to moderate the differentiation of macrophages into proinflammatory (M1) cells. PMID: 23742180 DNA methylation changes were noted in the Timp3 gene during chronic cystitis in a murine model. PMID: 23806407 Loss of Timp3 gene leads to abdominal aortic aneurysm formation in response to angiotensin II. PMID: 23144462 Loss of TIMP3 selectively exacerbates diabetic nephropathy. PMID: 22896043 Pericyte-derived TIMP3 stabilized and ADAMTS1 destabilized the capillary tubular networks PMID: 22383695 we show that TIMP3 produced by the hepatic stroma regulates the basal lymphocyte populations in the liver and prevents autoimmune hepatitis PMID: 22323541 Data suggest that focal ischemia leads to proliferation of immature oligodendrocytes in white matter and that TIMP-3 contributes to a caspase-3-dependent immature OL death via TNF-alpha/TACE-mediated neuroinflammation. PMID: 21871134 macrophage-specific overexpression of TIMP3 protects from metabolic inflammation and related metabolic disorders such as insulin resistance, glucose intolerance, and nonalcoholic steatohepatitis. PMID: 22228717 TIMP3 differentially impacts apoptosis and inflammatory cell influx, based on involvement of TNF, during the process of mammary involution. PMID: 22053204 macrophage-specific overexpression of TIMP3 decreases the inflammatory content and the amplitude of atherosclerotic plaques in low-density lipoprotein receptor knockout mice PMID: 22015660 Placental growth factor finely tunes a balanced regulation of the tissue inhibitor of metalloproteinases-3/tumor necrosis factor-alpha-converting enzyme axis and the consequent TNF-alpha activation in response to transverse aortic constriction. PMID: 21900081 TIMP3 was identified as a potential miR-206 target by TargetScan prediction analysis; further, in cultured cardiac fibroblasts, miR-206 gain- and loss-of-function studies and luciferase reporter assays showed that TIMP3 is a direct target of miR-206. PMID: 21731608 deficiency in TIMP-3 increases cardiac rupture post-myocardial infarction PMID: 21243368 Timp3, an endogenous regulator of metalloproteinases, stimulates hematopoietic stem cells proliferation by recruiting quiescent hematopoietic stem cells into the cell cycle. PMID: 20798233 demonstrated that TNF signaling promoted hepatotoxicity, while excessive TNF receptor 1 (TNFR1) shedding in Timp3-/- mice was protective. PMID: 20628198 TIMP3 functions to promote the resolution of inflammation in the lung. PMID: 20008147 We have identified novel mechanisms, governed by the TACE-Timp3 interaction, involved in the determination of insulin resistance and liver steatosis during overfeeding in mice. PMID: 19877183 Overexpression of TIMP-3 can inhibit angiogenesis and associated tumor growth, and that the antiangiogenic effects of TIMP-3 appear to be mediated through the inhibition of functional capillary morphogenesis. PMID: 12384438 The gene expression and protein distribution of Timp-3 was analyzed during molar development. PMID: 12950084 TIMP-3 deficiency disrupts matrix homeostasis and the balance of inflammatory mediators, eliciting the transition to cardiac dilation and dysfunction. PMID: 15262835 Here we show that deletion of the mouse gene Timp3 resulted in an increase in TNF-alpha converting enzyme activity, constitutive release of TNF and activation of TNF signaling in the liver. PMID: 15322543 Timp3 has a role in diabetes and vascular inflammation through the insulin receptor and TNF-alpha PMID: 16294222 loss of TIMP3 impacts innate immunity by dysregulating cleavage of TNF and its receptors PMID: 16393953 TIMP-3 provides an inherent regulation over the kinetics of pro-MMP-2 processing, serving at a level distinct from that of TIMP-2 and TIMP-4 PMID: 16469749 TIMP-3 regulates MMP-2 activation to limit tumor cell extravasation and subsequent colonization of the lung, without augmenting inflammatory cell response. PMID: 16702949 Timp-3 plays an important role in the maintenance of renal macrostructure after unilateral ureteral obstruction PMID: 16778336 TIMP3 can indirectly regulate epithelial cell proliferation via MMP inhibitory activity. While others have demonstrated that TIMP3 controls proliferation in vitro, this is the first evidence of TIMP3 regulating proliferation in vivo. PMID: 16890932 TIMP3 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. PMID: 17030988 Physiologically, Timp3(-/-) mammary glands displayed accelerated mammary ductal elongation during pubertal morphogenesis. PMID: 17327279 Results indicate that TIMP-3 deficiency results in mild cartilage degradation similar to changes seen in patients with osteoarthritis. PMID: 17328064 Laparotomy induced a downregulation of TIMP-3 and an upregulation of PI3-kinase, which increased cancer cell growth, invasion and cell cycle activity in comparison to laparoscopy. PMID: 17342361 The alveolar macrophage is essential for the TIMP-3 null sepsis-induced compliance alterations. PMID: 17586692 Timp-3 plays an important role in L-NAME-induced hypertension and myocardial vascular remodeling. PMID: 17664861 Role of DPPI and TIMP-3 in development of pulmonary fibrosis in early inflammation following bleomycin instillation. PMID: 17673693 TIMP-3 deficiency accelerated maladaptive cardiac remodeling after a myocardial infarction by promoting matrix degradation and inflammatory cytokine expression. PMID: 17945252 TIMP-3 facilitates Fas-mediated neuronal cell death following oxigen-glucose deprivation and plays a pro-apoptotic role in mild cerebral ischemia PMID: 17962815

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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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