Recombinant TIMP-1 Protein, Rat Recombinant Proteins The rat TIMP1 (P01860) (Met1-Ala217) was expressed and purified The recombinant rat TIMP1 consists of 194a.a and has a predicted molecular weight of 21.5 kDa. As a result of glycosylation, the apparent molecular weight of the recombinant protein is approximately 28 kDa in SDS-PAGE under reducing conditions.
$ $99 In stock
Formulation: The recombinant rat TIMP1 consists of 194a.a and has a predicted molecular weight of 21.5 kDa. As a result of glycosylation, the apparent molecular weight of the recombinant protein is approximately 28 kDa in SDS-PAGE under reducing conditions.
Source: HEK293 Cells
Usage: Our products are for research use only. This product is not intended or approved for human, diagnostics or veterinary use

Recombinant TIMP-1 Protein, Rat

The product is for non-human research only. Not for therapeutic or veterinary use.

Catalog Number: BT-200384

Molecular Weight: The recombinant rat TIMP1 consists of 194a.a and has a predicted molecular weight of 21.5 kDa. As a result of glycosylation, the apparent molecular weight of the recombinant protein is approximately 28 kDa in SDS-PAGE under reducing conditions.

Formulation: Recombinant TIMP-1 Protein was lyophilized from sterile 50mM Tris, 100mM NaCl, pH 7.0.1

Source: HEK293 Cells

Product Name Recombinant TIMP-1 Protein, Rat
Molecular Weight The recombinant rat TIMP1 consists of 194a.a and has a predicted molecular weight of 21.5 kDa. As a result of glycosylation, the apparent molecular weight of the recombinant protein is approximately 28 kDa in SDS-PAGE under reducing conditions.
AA Sequence Met1-Ala217
Bioactivity Measured by its ability to inhibit human MMP2 cleavage of a fluorogenic peptide substrate MCA-PLGLDPA-AR-NH2, AnaSpec Catalog # 27076.The IC50 value is approximately 4 nM.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Recombinant TIMP-1 Protein was lyophilized from sterile 50mM Tris, 100mM NaCl, pH 7.0.1
Host Species Rat
Description The rat TIMP1 (P01860) (Met1-Ala217) was expressed and purified
Product Background 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.
Product Type Recombinant Protein
Purity Greater than 97% as determined by SDS-PAGE
Source HEK293 Cells
Storage Store recombinant protein under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Terminal Cys 24
Uniprot No P01860
Usage Our products are for research use only. This product is not intended or approved for human, diagnostics or veterinary use
Last Modified Aug 20 2021