SRP3173
TIMP-1 human
recombinant, expressed in E. coli, ≥95% (SDS-PAGE), ≥95% (HPLC), suitable for cell culture
Synonym(s):
Erythroid-Potentiating activity, Fibroblast collagenase inhibitor, Tissue inhibitor of metalloproteinase
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.32
biological source
human
recombinant
expressed in E. coli
Assay
≥95% (HPLC)
≥95% (SDS-PAGE)
form
lyophilized
potency
0.5 μg/mL
mol wt
20.6 kDa
packaging
pkg of 10 μg
technique(s)
cell culture | mammalian: suitable
impurities
<0.1 EU/μg endotoxin, tested
color
white
suitability
suitable for molecular biology
UniProt accession no.
shipped in
wet ice
storage temp.
−20°C
Gene Information
human ... TIMP1(7076)
General description
Research area: Cell SignalingTIMP1 (tissue inhibitor of metalloproteinase 1) is a glycoprotein and belongs to the TIMP family of endogenous MMP (matrix metalloproteinase) inhibitors. Humans contain four TIMPs. All TIMPs contain an N-terminal of 125 residues, a 65-residue C-terminal, and both these domains with three disulfide bonds. The N-terminal domain inhibits MMPs by folding into a separate unit. Recombinant human TIMP-1 is a 20.6 kDa protein containing 184 amino acid residues.
Application
TIMP-1 human has been used for inhibition assays in enzymatic activity assays of Mmp1-CD and Mmp2-CD. It has also been used in interaction immunoassay.
Biochem/physiol Actions
TIMP1 functions as a poor inhibitor of MT1 (membrane type 1)-MMP, MT3-MMP, MT5-MMP and MMP-19. It inhibits ADAM10 (a disintegrin and metalloproteinase domain-containing protein 10) protein. In HUVECs, the down-regulation of TIMP1 and up-regulation of MMP-3 results in aberrant endothelium-dependent vasodilation, EC (endothelial cell) death, and endothelial interruption in a FOXO3 (forkhead box O3)-mediated manner. In patients with CAD (coronary artery disease) and acute coronary syndrome (ACS), the urine levels of this protein are elevated. This protein interacts with Bcl-2 (B cell lymphoma) protein, and induces apoptosis in lung adenocarcinoma cells. The plasma levels of this protein are increased in patients with obesity and obesity-related disorders, such as steatosis, where it participates in pathogenesis of diet-induced hepatic steatosis and glucose intolerance.
Physical form
Lyophilized from 10 mM Sodium Phosphate, pH 7.5.
Preparation Note
Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.
Other Notes
CTCVPPHPQT AFCNSDLVIR AKFVGTPEVN QTTLYQRYEI KMTKMYKGFQ ALGDAADIRF VYTPAMESVC GYFHRSHNRS EEFLIAGKLQ DGLLHITTCS FVAPWNSLSL AQRRGFTKTY TVGCEECTVF PCLSIPCKLQ SGTHCLWTDQ LLQGSEKGFQ SRHLACLPRE PGLCTWQSLR SQIA
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Tissue Inhibitor Of Matrix Metalloproteinase-1 Is Required for High-Fat Diet-Induced Glucose Intolerance and Hepatic Steatosis in Mice.
Fj?re E, et al.
PLoS ONE, 10(7) (2015)
TIMP-1 Inhibits Apoptosis in Lung Adenocarcinoma Cells via Interaction with Bcl-2.
Nalluri S, et al.
PLoS ONE, 10(9) (2015)
Matrix metalloproteinase inhibitors as investigative tools in the pathogenesis and management of vascular disease.
Benjamin MM1 and Khalil RA.
EXS, 103, 209-279 (2012)
Gary J Litherland et al.
Arthritis & rheumatology (Hoboken, N.J.), 66(8), 2175-2187 (2014-04-24)
To assess the role of glycogen synthase kinase 3 (GSK-3) as a regulator of cartilage destruction in human tissue and a murine model of osteoarthritis (OA). Surgical destabilization of the medial meniscus (DMM) was performed to induce experimental murine OA
Helena Pulido-Olmo et al.
Frontiers in immunology, 8, 853-853 (2017-08-10)
The protocol describes a novel, rapid, and no-wash one-step immunoassay for highly sensitive and direct detection of the complexes between matrix metalloproteinases (MMPs) and their tissue inhibitor of metalloproteinases (TIMPs) based on AlphaLISA® technology. We describe two procedures: (i) one
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