TIMP-1 Protein, Human, Recombinant

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TIMP-1 Protein, Human, Recombinant: Product Information

Purity
> 97 % as determined by SDS-PAGE
Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method
Activity
Measured by its ability to inhibit human MMP-2 cleavage of a fluorogenic peptide substrate MCA-PLGL-DPA-AR-NH2(R&D Systems, Catalog # ES001) . The IC50 value is < 6 nM.
Protein Construction
A DNA sequence encoding the mature form of human TIMP1 (NP_003245.1) (Cys 24-Ala 207) was expressed.
Accession#
Expressed Host
HEK293 Cells
Species
Human
Predicted N Terminal
Cys 24
Molecule Mass
The recombinant human TIMP1 comprises 184 amino acids with a predicted molecular mass of 21 kDa. It migrates as an approximately 26 kDa band in SDS-PAGE under reducing conditions.
Formulation
Lyophilized from sterile 20mM NaAC, 200mM NaCl, pH 5.5
Please contact us for any concerns or special requirements.
Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
Shipping
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.
Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃
Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

TIMP-1 Protein, Human, Recombinant: Images

TIMP-1 Protein, Human, Recombinant: Alternative Names

CLGI Protein, Human; EPA Protein, Human; EPO Protein, Human; HCI Protein, Human; TIMP Protein, Human; TIMP-1 Protein, Human

TIMP-1 Background Information

TIMP metallopeptidase inhibitor 1, also known as TIMP-1/TIMP1, Collagenase inhibitor 16C8 fibroblast Erythroid-potentiating activity, TPA-S1TPA-induced proteinTissue inhibitor of metalloproteinases 1, is a natural inhibitors of the matrix metalloproteinases (MMPs), a group of peptidases involved in degradation of the extracellular matrix. TIMP-1/TIMP1 is found in fetal and adult tissues. Highest levels are found in bone, lung, ovary and uterus. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. In addition to its inhibitory role against most of the known MMPs, the protein is able to promote cell proliferation in a wide range of cell types, and may also have an anti-apoptotic function. Transcription of this protein encoding gene is highly inducible in response to many cytokines and hormones. In addition, the expression from some but not all inactive X chromosomes suggests that this gene inactivation is polymorphic in human females. This encoding gene is located within intron 6 of the synapsin I gene and is transcribed in the opposite direction. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 is Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-1, MMP-11, MMP-12, MMP-13 and MMP-16.
Full Name
TIMP metallopeptidase inhibitor 1
References
  • Hornebeck W (2004). Down-regulation of tissue inhibitor of matrix metalloprotease-1 (TIMP-1) in aged human skin contributes to matrix degradation and impaired cell growth and survival.. Pathol. Biol. 51 (10): 569-73.
  • Soini Y, et al. (2001) Expression of MMP2, MMP9, MT1-MMP, TIMP-1, and TIMP2 mRNA in valvular lesions of the heart. J Pathol. 194(2):225-31.
  • Wang X, et al. (1999) Analysis of coding sequences for tissue inhibitor of metalloproteinases 1 (TIMP-1) and 2 (TIMP2) in patients with aneurysms. Matrix Biol. 18(2):121-4.
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