SERPINE2 Mouse

Plasminogen Activator Inhibitor-2 Mouse Recombinant
Cat. No.
BT24438
Source
Sf9, Baculovirus cells.
Synonyms
Serpnie2, B230326M24Rik, PAI-1, PI-7, PI7, PN-1, Spi4, Glia-derived nexin, GDN,Peptidase inhibitor 7, Protease nexin 1, Protease nexin I, Serine protease-inhibitor 4, Serpin E2.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

SERPINE2 produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 386 amino acids (20-397a.a.) and having a molecular mass of 42.9kDa. SERPINE2 is expressed with a 8 amino acid His tag at C-Terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Plasminogen Activator Inhibitor-2 (Serpine2), a member of the Serpin superfamily of serine protease inhibitors, inhibits thrombin, plasmin, and plasminogen activators. This molecule plays a role in transforming human embryonic kidney cells into neuron-like cells. Additionally, overexpression of Serpine2 in mice has been linked to progressive neuronal and motor dysfunction.
Description

Produced in Sf9 Baculovirus cells, SERPINE2 is a single, glycosylated polypeptide chain with a molecular weight of 42.9 kDa. It consists of 386 amino acids (20-397a.a.) and includes an 8 amino acid His tag at the C-terminus. The protein undergoes purification using proprietary chromatographic techniques.

Physical Appearance
Sterile, colorless solution that has been filtered.
Formulation
The SERPINE2 protein solution is provided at a concentration of 0.5 mg/ml and contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the solution should be kept at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. Adding a carrier protein (0.1% HSA or BSA) is advisable for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of the protein is greater than 95.0%, as determined by SDS-PAGE analysis.
Synonyms
Serpnie2, B230326M24Rik, PAI-1, PI-7, PI7, PN-1, Spi4, Glia-derived nexin, GDN,Peptidase inhibitor 7, Protease nexin 1, Protease nexin I, Serine protease-inhibitor 4, Serpin E2.
Source
Sf9, Baculovirus cells.
Amino Acid Sequence
SQFNSLSLEE LGSNTGIQVF NQIIKSRPHE NVVVSPHGIA SILGMLQLGA DGKTKKQLST VMRYNVNGVG KVLKKINKAI VSKKNKDIVT VANAVFLRNG FKMEVPFAVR NKDVFQCEVQ NVNFQDPASA SESINFWVKN ETRGMIDNLL SPNLIDGALT RLVLVNAVYF KGLWKSRFQP ESTKKRTFVA GDGKSYQVPM LAQLSVFRSG STRTPNGLWY NFIELPYHGE SISMLIALPT ESSTPLSAII PHITTKTIDS WMNTMVPKRM QLVLPKFTAV AQTDLKEPLK ALGITEMFEP SKANFTKITR SESLHVSHIL QKAKIEVSED GTKASAATTA ILIARSSPPW FIVDRPFLFS IRHNPTGAIL FLGQVNKPLE HHHHHH.

Product Science Overview

Gene and Protein Structure

PAI-2 is encoded by the SERPINB2 gene. In mice, this gene is located on chromosome 1 . The protein exists in two forms: a 60-kDa extracellular glycosylated form and a 43-kDa intracellular form . Structurally, like other serpins, PAI-2 has three beta sheets (A, B, C) and nine alpha helices (hA-hI) .

Biological Functions

PAI-2 is primarily known for its role in inhibiting uPA, which is involved in the plasminogen activation system. This system plays a crucial role in fibrinolysis, the process of breaking down blood clots . However, PAI-2 has a number of other functions:

  1. Immunomodulatory Activities: PAI-2 has been shown to have immunomodulatory effects, influencing both innate and adaptive immunity .
  2. Cytoprotective and Anti-inflammatory Activities: It has cytoprotective properties, helping cells survive under stress conditions, and also exhibits anti-inflammatory activities .
  3. Cell Differentiation and Autophagy: PAI-2 is involved in cell differentiation and autophagy, processes essential for maintaining cellular homeostasis .
Expression and Regulation

PAI-2 is expressed in various tissues, with high levels found in monocytes and macrophages . Its expression is upregulated in response to stress and inflammatory signals . Interestingly, PAI-2 is present in detectable quantities in blood only during pregnancy, as it is produced by the placenta .

Clinical Relevance

Due to its role in inhibiting uPA, PAI-2 has been studied for its potential in cancer therapy. Overexpression of uPA at the surface of cancer cells is linked to malignancy, and targeting uPA with recombinant PAI-2 has been proposed as a potential therapeutic strategy .

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