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Recombinant Human TIMP-1 protein (His Tag)

Recombinant Human TIMP-1 protein (His Tag)
  • Recombinant Human TIMP-1 protein (His Tag)
  • Recombinant Human TIMP-1 protein (His Tag)

Price: ¥3600.00 ¥1200.00

Size:
100 μg 20 μg
  • 表达系统: HEK293 Cells
  • 蛋白编码: P01033
别称
CLGI;Collagenase Inhibitor;EPA;EPO;Erythroid-Potentiating Activity;Fibroblast collagenase Inhibitor;HCI;Metalloproteinase Inhibitor 1;TIMP;TIMP-1;TIMP1;Tissue Inhibitor of Metalloproteinases 1
表达系统
HEK293 Cells
序列
Met1-Ala207
蛋白编码
P01033
种属
Human
计算分子量
22.7 kDa
表观分子量
30 kDa
标签
C-His
生物活性
Not validated for activity
纯度
> 95% as determined by reducing SDS-PAGE.
内毒素
< 1.0 EU/mg of the protein as determined by the LAL method
保存条件
Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.
运输条件
This product is provided as lyophilized powder which is shipped with ice packs.
制剂
Lyophilized from a 0.2 μm filtered solution in PBS with 5% Trehalose and 5% Mannitol.
复溶方法
It is recommended that sterile water be added to the vial to prepare a stock solution of 0.5 mg/mL. Concentration is measured by UV-Vis.
背景
Tissue Inhibitor of Metalloproteinases 1 (TIMP-1) is a member of TIMP family. The homologous proteins of TIMPs regulate the activity of matrix metalloproteinases (MMPs), including inhibition of active MMPs, proMMP activation, cell growth promotion, matrix binding, inhibition of angiogenesis and the induction of apoptosis. Timp-1 complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. It also mediates erythropoiesis in vitro, but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. It is known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13, and MMP-16, without MMP-14.
> 95 % as determined by reducing SDS-PAGE.


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