Rat tissue inhibitors of metalloproteinase 1,TIMP-1 ELISA Kit

Code CSB-E08005r
Size 96T,5×96T,10×96T
Trial Size 24T ELISA kits trial application
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Product Details


This Rat Tissue Inhibitors of Metalloproteinase 1 (TIMP-1) ELISA Kit is an accurate and reliable solution for measuring TIMP-1 levels in serum, plasma, cell culture supernates, and tissue homogenates of Rattus norvegicus (Rat).

This ELISA kit has been specifically designed to detect and quantify TIMP-1 levels, an important protein involved in regulating matrix metalloproteinase activity, which is a key process in cardiovascular research.Also functions as a growth factor that regulates cell differentiation, migration and cell death and activates cellular signaling cascades.

With a detection range of 0.156 ng/mL to 10 ng/mL and a sensitivity of 0.224 ng/mL, this quantitative assay can provide precise and reproducible results in just 1 to 5 hours. The sample volume required is only 50-100ul, making it an economical and efficient option for researchers.

The assay principle is based on a sandwich ELISA method, which utilizes specific antibodies to capture and detect TIMP-1 in the sample. The detection wavelength is 450 nm, ensuring accurate and reliable measurements.

Target Name TIMP metallopeptidase inhibitor 1
Alternative Names
Timp1 ELISA Kit; Timp-1 ELISA Kit; Metalloproteinase inhibitor 1 ELISA Kit; Tissue inhibitor of metalloproteinases 1 ELISA Kit; TIMP-1 ELISA Kit
Abbreviation TIMP1
Uniprot No. P30120
Species Rattus norvegicus (Rat)
Sample Types serum, plasma, cell culture supernates, tissue homogenates
Detection Range 0.156 ng/mL-10 ng/mL
Sensitivity 0.224 ng/mL
Assay Time 1-5h
Sample Volume 50-100ul
Detection Wavelength 450 nm
Research Area Cardiovascular
Assay Principle quantitative
Measurement Sandwich


Intra-assay Precision (Precision within an assay): CV%<8%

Three samples of known concentration were tested twenty times on one plate to assess.

Inter-assay Precision (Precision between assays): CV%<10%

Three samples of known concentration were tested in twenty assays to assess.




To assess the linearity of the assay, samples were spiked with high concentrations of Rat TIMP-1 in various matrices and diluted with the Sample Diluent to produce samples with values within the dynamic range of the assay.


Typical Data


These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed.

ELISA Data Analysis ELISA Standard Curve & Curve Expert software
and FAQs
Storage Store at 2-8°C. Please refer to protocol.
Lead Time 3-5 working days


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Target Background

(From Uniprot)
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. Also stimulates steroidogenesis by Leydig and ovarian granuloma cells; procathepsin L is required for maximal activity.
Gene References into Functions
  1. Tissue kallikrein 1 and TIMP1 expressed in a coexpression vector synergistically inhibited the proliferation of rat vascular smooth muscle cells. PMID: 26252163
  2. In a normoglycemic rat model of wound healing, pentoxifylline significantly increased TIMP-1 gene expression. PMID: 26087281
  3. Our findings clearly demonstrate that despite their dramatic spatial rearrangement, cones and second-order neuron processes maintain their synaptic connections before and after TIMP-1 treatment. PMID: 26277580
  4. Data indicate that adiponectin promoted tissue inhibitor of metalloproteinase-1 (TIMP-1) expression and limited hepatic stellate cell migration . PMID: 25575598
  5. Basic fibroblast growth factor could up-regulate TIMP-1 expression and down-regulate MMP-9 activation in CFs in perivascular spaces, leading to inhibited progression of cardiac fibrosis during hypertensive heart failure. PMID: 24322055
  6. 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
  7. Inducible TIMP1 can modulate the expression of fibrosis-related genes in the liver. PMID: 23456624
  8. Data indicate that increased TIMP-1 levels inhibit the proteolytic processing of Reelin under epileptic conditions. PMID: 23493620
  9. study aimed to identify genomic biomarkers for early and sensitive detection of renal papillary injury in rats; Timp1, Igf1, and Lamc2 exhibited the best prediction performance PMID: 23142791
  10. TIMP-1 increased in the rats treated with doxycycline ahead and might compensate for the activity of MMP-9 in lung injury following cardiopulmonary bypass. PMID: 22449799
  11. Recombinant human TIMP-1 is distributed quickly into rat ischemic brain tissue and is slowly eliminated in both blood and brain tissue of rats. PMID: 21535944
  12. Data show that the protein and mRNA expression level of TIMP-1 was high in asthmatic rat's lung tissues. PMID: 16191269
  13. Dahuang Zhechong Pill can down-regulate the expressions of TIMP-1 and PAI-1 mRNAs in renal tissues of rats with focal segmental glomerulosclerosis. PMID: 18471418
  14. higher levels of MMP-9 messenger RNA and protein expression were detected in the diabetic group compared with the control group (P < .05), and expression of TIMP-1 messenger RNA and protein was significantly decreased. PMID: 19917734
  15. TIMPs are involved in cell viability and tissue remodelling in the ischemic brain PMID: 11860503
  16. role of TIMP-1 in the airway extracellular matrix (ECM) remodelling of chronic obstructive pulmonary disease (COPD) rat models PMID: 12137602
  17. TIMP-1 induction by ANG II in aortic smooth muscle cells occurs in the absence of histological changes at the vascular wall. PMID: 12388255
  18. tissue inhibitor of metalloproteinase-1 mRNA was observed surrounding the developing corpus luteum (CL), with less intense expression present in granulosa-lutein cells PMID: 12444073
  19. oxidative stress-stimulated up-regulation of TIMP-1 may play an important role in the deposition of collagen or extracellular matrix elements in the glomeruli during hyperhomocysteinemia. PMID: 12631082
  20. TIMP-1 expression increased transiently but significantly during junction assembly in Sertoli cells and germ cells PMID: 12826691
  21. An imbalance between collagenases and TIMPs, excessive gelatinolytic activity, and epithelial apoptosis participate in the fibrotic response in this experimental model. PMID: 12882763
  22. TIMP1 gene transcription is regulated by RUNX1 and RUNX2 PMID: 15051730
  23. Administration of anti-TIMP-1 resulted in a marked decrease in alpha-SMA staining. TIMP-1 antibody attenuated CCl(4)-induced liver fibrosis and decreased hepatic stellate cell activation and MMP-2 activity. PMID: 15389776
  24. PANC-1 CM stimulates PSC proliferation and TIMP-1 through the MAP kinase (ERK 1/2) pathway. PMID: 15451430
  25. TIMP-1 may play an important role in the process of liver aging PMID: 15968723
  26. NO by induction of the Smad signaling pathway modulates TIMP-1 expression. PMID: 16183640
  27. In immune-induced model of rat liver fibrosis, serum TIMP-1 level could reflect severity of liver fibrosis, while in CCL4-induced model, the correlation between the serum TIMP-1 level and the severity of hepatic fibrosis was not statistically significant PMID: 16718785
  28. suggests a novel extracellular mechanism of late long-term potentiation in the PFC, engaging TIMP-1-controlled proteolysis as an element of information integration PMID: 17210139
  29. Expression of Timp1 was decreased by treatment with the protective agent from Aspergillus. PMID: 17485851
  30. Shear stress-induced Ets-1 modulates TIMP-1 expression in microvascular endothelial cells. PMID: 18636553
  31. Gene expression of Timp1 fibroblasts from the medial collateral ligament, anterior cruciate ligament and patellar tendon was not significantly different. PMID: 18807189
  32. W256 cells do not express or secrete TIMP-1 protein, although RT-PCR analysis indicated low-level TIMP-1 mRNA expression. PMID: 19330523
  33. Increased expression of TIMP-1 in venous endothelium and plasma may serve as an early indicator of endothelial dysfunction. PMID: 19467832
  34. These data are the first to show that the elevated vascular expression of TIMP-1, associated with breakdown of the blood-brain barrier following focal ischemia, are transcriptionally regulated via the MEK/ERK pathway. PMID: 19497125

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Subcellular Location Secreted.
Protein Families Protease inhibitor I35 (TIMP) family
Database Links

KEGG: rno:116510

STRING: 10116.ENSRNOP00000013745

UniGene: Rn.25754

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