Recombinant Human TIMP-2 Protein (C-6His)

Name: Recombinant Human TIMP-2 Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-0480NP
Availability: InStock

BL-0480NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

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

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Tissue Inhibitor of Metalloproteinases 2 is produced by our Mammalian expression system and the target gene encoding Cys27-Pro220 is expressed with a 6His tag at the C-terminus.
Accession	P16035
Synonym	Metalloproteinase Inhibitor 2; CSC-21K; Tissue Inhibitor of Metalloproteinases 2; TIMP-2; TIMP2
Gene Background	Tissue inhibitors of metalloproteinases or TIMPs are a family of proteins that regulate the activation and proteolytic activity of the zinc enzymes known as matrix metalloproteinases (MMPs). There are four members of the family, TIMP-1, TIMP-2, TIMP-3, and TIMP-4. Tissue Inhibitor of Metalloproteinases 2 (TIMP-2) is a non N-glycosylated protein with a molecular mass of 22 kDa. It produced by a wide range of cell types, which inhibits MMPs non-covalently by the formation of binary complexes and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-2 also has erythroid‑potentiating and cell growth promoting activities.
Molecular Mass	22.79 KDa
Apmol Mass	26 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.2.
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	Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.
Subcellular Location	Secreted.
Protein Families	Protease inhibitor I35 (TIMP) family
Database References	HGNC: 11821 OMIM: 188825 KEGG: hsa:7077 STRING: 9606.ENSP00000262768 UniGene: PMID: 30284418 UV-induced expression of DNMT1 may be responsible for mediating DNA hypermethylation in TIMP2, and thus, silencing its expression, in UV-exposed human skin. PMID: 29685765 Overexpression of TIMP2 inhibited cell viability, migration and EMT process. PMID: 29432996 TIMP2 was confirmed to be a direct downstream target of miR616. Inhibition of TIMP2 expression was required for the promoting effects of miR616 on the metastasis and EMT of ovarian cancer cells. PMID: 29658596 TIMP2 promotes tumor progression and miR2055p directly regulates TIMP2, thereby suppressing proMMP2 activation and inhibiting oral squamous cell carcinoma cell invasiveness. PMID: 29393341 Urine levels of TIMP2 (and IGFBP7) are predictive of acute kidney injury following cardiac surgical procedures. PMID: 28803769 MMP-9 and TIMP-2 genes are upregulated in cancerous tissues when compared to normal bladder tissues. PMID: 28980922 Overexpression of MMP2 and MMP16 in endometrial cancerous tissues corresponded to down-regulation of miR-377, miR-382 and miR-410, while decreased expression of TIMP2 was associated with miR-200b up-regulation. PMID: 28871006 MiR-106a was inversely correlated with TIMP2. PMID: 28731196 In squamous cell carcinoma of the cervix (SCCC), higher levels of MMP-14 expression were established in tumor cells, as evidenced by IHC (+3) and RT-PCR.Furin activity in the tumor was much higher than that in normal tissues. The expression of TIMP-2 mRNA was sufficiently obvious in both the tumor and normal tissues to the bottom of the uterine cavity. PMID: 29265076 methylation differences within the TIMP2 gene promoter are not related to patellar tendinopathy PMID: 28888475 This study provides evidence that TIMP-2 is a knee OA susceptibility gene in the Chinese population and a potential diagnostic and preventive marker for the disease. PMID: 27901480 Tissue inhibitor of metallopeptidases 2 (TIMP2) protein and mRNA levels were downregulated after miR-15b overexpression in A549 and LTEP-a-2 cells, respectively. Our results indicate that high expression of miR-15b is associated with non-small cell lung cancer (NSCLC)and suggest that miR-15b expression may be a novel biomarker for predicting clinical outcomes in NSCLC patients PMID: 28498424 study results suggest an association between matrix metalloproteinase 2, matrix metalloproteinase 9 and tissue inhibitor of metalloproteinase 2 single nucleotide polymorphisms with sperm parameters, but not infertility PMID: 27401679 Long noncoding RNA DANCR promotes prostate cancer invasion and metastasis through repressing the expression of TIMP2/3 PMID: 27191265 MMP2-1306C/T and TIMP2-418 G/C gene variants as risk factors for patients with relapsing remitting multiple sclerosis, was studied. PMID: 27174941 biomarker for acute kidney injury PMID: 27174659 epithelial cells and leukocytes from the urinary sediment. CONCLUSION: The gene expression pattern of IGFBP7 and TIMP-2 from urinary sediment, which contains desquamated renal tubular epithelial cells, did not correlate with [IGFBP7]x[TIMP-2] protein, indicating that IGFBP7 and TIMP-2 measured in the NephroCheck(R) test originated predominantly from intact but stressed cells of the kidney itself PMID: 29145491 This study demonstrated that TIMP2 higher expression in glioblastoma PMID: 27633774 Data show that tissue inhibitor of metalloproteinase 2 (TIMP2) is a direct target of miR-492 that modulates cervical cancer cell invasion. PMID: 28802022 A higher risk of incidence or recurrent depressive disorder(OR=9.376) was confirmed in the case of a set of T/T-G/C genotypes of the MMP-9T-1702A and TIMP-2G-418C polymorphisms PMID: 27434116 High TIMP2 expression is associated with acute kidney injury. PMID: 27342580 expression of TIMP2 was inversely associated with miR-106a in nodule tissues. Apoptotic body was also seen under electron microscope accompanied by silencing of miR-106a. Together, this data indicated that miR-106a may act as an oncogene and contribute to gastric cancer development. PMID: 27142596 Urine [TIMP-2][IGFBP7] is a promising candidate for early detection of AKI, especially in ruling-out AKI PMID: 28107490 We conclude that in the resected esophageal cancer an increased mRNA expression of MMP-7, MMP-10 and TIMP-1 correlated with clinicopathologic features. We suggest that these genes may play a role during progression of the disease. MMP-10, MMP-7, TIMP-1, TIMP-2 were overexpressed in 73%, 85%, 55% and 42% of esophageal cancer samples, respectively. PMID: 28510611 At hospital admission, all viral gastroenteritis (GE) patients viral gastroenteritis (GE) patients demonstrated increased MMP-9 and decreased MMP-2 and TIMP-2 serum levels; kinetics of serum MMP-2, MMP-9, 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 PMID: 26765397 Meta-analysis indicated that urinary [TIMP-2].[IGFBP7] may be a reliable biomarker for the early detection of acute kidney injury in adults. PMID: 28682920 Results show that resistant hypertension was associated with higher TIMP-2 levels and low MMP-2/TIMP-2 ratio, suggesting that these regulators of ECM remodeling play a key role in blood pressure control in this high-risk subset of hypertensive individuals. PMID: 27412873 important regulator of extracellular matrix degradation and hepatocellular carcinoma metastasis PMID: 27018975 TIMP-2 is both expressed and secreted preferentially by cells of distal tubule origin, while IGFBP7 is equally expressed across tubule cell types yet preferentially secreted by cells of proximal tubule origin. In human kidney tissue, strong staining of IGFBP7 was seen in the luminal brush-border region of a subset of proximal tubule cells, and TIMP-2 stained intracellularly in distal tubules. PMID: 28003188 Myopia development in mammals is associated with reduced expression of TIMP-2, which contributes to increased degradative activity in the sclera. PMID: 28384717 our results revealed miR-483-5p directly targeted to the cartilage matrix protein matrilin 3 (Matn3) and tissue inhibitor of metalloproteinase 2 (Timp2) to stimulate chondrocyte hypertrophy, extracellular matrix degradation, and cartilage angiogenesis, and it consequently initiated and accelerated the development of OA. PMID: 28139355 Stromal TIMP-2 expression reflected its role in regulating tumor progression in ameloblastoma and in regulating developmental processes in tooth germs by their inhibitory effect on MMP-9 PMID: 26067137 No significant differences were found between MMP-7 A-181G, C-115T, and TIMP-2 G-418C polymorphism and coronary artery disease and myocardial infarction in a Turkish population. PMID: 28137415 High TIMP2 expression is associated with chronic myelogenous leukemia. PMID: 28035415 MMP-2 and TIMP-2 were secreted by both tumor cells and stromal cells. PMID: 27853937 that miR-22 acts to regulate invasion of 1321N1 astrocytoma cells by targeting TIMP2 expression PMID: 27834627 Results show decreased expression of MMP-2, MMP-9 and TIMP-2 genes on both mRNA and protein levels in depression; there elevated expression positively affects cognitive efficiency. PMID: 26856768 TIMP- 2 expression decreased in cervical disc herniation patients. PMID: 27173256 Changes in MMPs and TIMP expression may be a common element in, or perhaps even a marker for, recurrent depressive disorders and somatic diseases. PMID: 27098106 quantitative urine test is available to assess the risk of developing AKI by measuring the concentrations of two protein biomarkers, TIMP-2 and IGFBP-7 PMID: 26797672 miR-22 significantly upregulated the invasion capacity of 1321N1 cells. In silico analysis predicted that TIMP2 is a target gene of miR-22 which was confirmed by qPCR and Western blotting. Luciferase reporter assays demonstrated that miR-22 directly bound the 3'-untranslated regions of TIMP2. These data suggest that miR-22 acts to regulate invasion of 1321N1 astrocytoma cells by targeting TIMP2 expression. PMID: 27834627 Pathogenesis and progression of nasal polyps is closely related with elevated MMP-9 and suppressed TIMP-2 expression PMID: 26823777 our results demonstrate that TIMP-2 stimulates lung adenocarcinoma cell proliferation PMID: 26556867 new evidence that promoter polymorphisms in TIMP2 are functional and may affect gene transcription with possible effects on craniofacial development leading to NSCL/P. PMID: 24799419 This study shows that urinary [TIMP-2][IGFBP7] has a good diagnostic performance in predicting adverse outcomes in neonatal and pediatric AKI of heterogeneous etiology. PMID: 26606754 showed a significant association between the variants of MMP-2 and TIMP-2 promoters and spontaneous intracerebral hemorrhage PMID: 26551785 TIMP2 is elevated in patients with non-alcoholic fatty liver disease. PMID: 26329758 TIMP-2 interaction with MT1-MMP provides tumor cells with either pro- or anti-apoptotic signaling depending on the extracellular environment and apoptotic stimulus. PMID: 26331622 MiR-761 directly targeted ING4 and TIMP2. PMID: 26278569

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

📧 inquiry@betalifesci.com 📞 +1(201) 888-7983

Contact Us Now for Inquiries, Orders, and Questions

Recombinant Human TIMP-2 Protein (C-6His)

Recombinant Human TIMP-2 Protein (C-6His)

Product Overview

Target Details

FAQs