Recombinant Human TIMP2 protein (hFc Tag)

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• Recombinant Human TIMP2 protein (hFc Tag) (Eg0418)

Species

Human

Purity

>90 %, SDS-PAGE

Tag

hFc Tag

Activity

not tested

Cat no : Eg0418

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Validation Data Gallery

• 

  Purity of Recombinant Human TIMP2 was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

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Product Information

• Purity: >90 %, SDS-PAGE
• Endotoxin: <0.1 EU/μg protein, LAL method
• Activity:

  Not tested

• Expression: HEK293-derived Human TIMP2 protein Cys27-Pro220 (Accession# P16035) with a human IgG1 Fc tag at the C-terminus.
• GeneID: 7077
• Accession: P16035
• PredictedSize: 47.8 kDa
• SDS-PAGE: 45-55 kDa, reducing (R) conditions
• Formulation: Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
• Reconstitution: Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
• Storage Conditions:
  It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
• Shipping: The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

TIMP2, a 21-kDa protein, is a member of the family of matrix metalloproteinase inhibitors, which contains four members (TIMP1, TIMP2, TIMP3, and TIMP4). Tissue inhibitors of metalloproteinases (TIMPs) are multifaceted molecules that exhibit properties beyond their classical proteinase inhibitory function. TIMP-2 is the only TIMP functioning as both an MMP inhibitor and an activator, because it can interact with membrane type 1 MMP and pro-MMP2 to facilitate the activation of pro-MMP2 to its active form. TIMP2 can regulate many physiological progression such as tumor growth, metastasis, and angiogenesis through matrix metalloproteinases (MMPs). TIMP2 knockout resulted in constitutive MMP9 activation abundantly and adverse MI remodeling in vivo.

References:

1. Stetler-StevensonWG.et al.(2008) Sci Signal.1(27):re6. 
2. Hernandez-Barrantes S.et al. (2000).J Biol Chem.275(16):12080-9. 
3. Seo DW.et al. (2003) Cell.114(2):171-80. 
4. KandalamV.et al.(2010) Circ Res.106(4):796-808.