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Merck
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SRP3173

TIMP-1 human

recombinant, expressed in E. coli, ≥95% (SDS-PAGE), ≥95% (HPLC), suitable for cell culture

别名:

Erythroid-Potentiating activity, Fibroblast collagenase inhibitor, Tissue inhibitor of metalloproteinase

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关于此项目

NACRES:
NA.32
UNSPSC Code:
12352200
Form:
lyophilized
Assay:
≥95% (HPLC), ≥95% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in E. coli
Mol wt:
20.6 kDa
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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)

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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

存储类别

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

法规信息

常规特殊物品
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分析证书(COA)

Lot/Batch Number

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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)
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
Matrix metalloproteinase inhibitors as investigative tools in the pathogenesis and management of vascular disease.
Benjamin MM1 and Khalil RA.
EXS, 103, 209-279 (2012)
TIMP-1 Inhibits Apoptosis in Lung Adenocarcinoma Cells via Interaction with Bcl-2.
Nalluri S, et al.
PLoS ONE, 10(9) (2015)
D E Gomez et al.
European journal of cell biology, 74(2), 111-122 (1997-11-14)
Four members of the tissue inhibitor of metalloproteinases (TIMP) family have been characterized so far, designated as TIMP-1, TIMP-2, TIMP-3, and TIMP-4. TIMP-1 and TIMP-2 are capable of inhibiting the activities of all known matrix metalloproteinases (MMPs) and as such

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