Glia-derived nexin Antibodies

Glia-derived nexin (SERPINE2)

Serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin.

Binds heparin. .

Gene Information

Human
Gene Name:	SERPINE2
Uniprot:	P07093
Entrez:	5270

Family

Belongs to:
serpin family

Alternative Names

GDN; GdNPF; GDNserine (or cysteine) proteinase inhibitor, clade E (nexin, plasminogenactivator inhibitor type 1), member 2; glia-derived nexin; glial-derived neurite promoting factor; Peptidase inhibitor 7; PI-7; PI7DKFZp686A13110; PN-1; PN1nexin; PNI; Protease nexin 1; Protease nexin I; Proteinase Nexin 1; Serpin E2; serpin peptidase inhibitor, clade E (nexin, plasminogen activator inhibitortype 1), member 2

Molecular Weight

Mass (kDA):
44.002 kDA

Genomic Context

Human
Location:	2q36.1
Sequence:	2; NC_000002.12 (223975045..224039319, complement)

Subcellular Localizations

Secreted, extracellular space.

Diseases

• Malignant Neoplasms
• Chronic Obstructive Airway Disease
• Neoplasms
• Lung Diseases
• Lung Diseases, Obstructive
• Fibrosis
• Inflammation
• Tissue Adhesions
• Neoplasm Metastasis
• Pulmonary Emphysema
• Nervousness
• Alzheimer's Disease
• Tumor Angiogenesis

• Cell Invasion
• Thrombosis
• Brain Injuries
• Carcinoma
• Atherosclerosis
• Obesity
• Hemorrhage

Interacting Proteins

• FAM9B

Pathways

• Secretion
• Coagulation
• Pathogenesis
• Fibrinolysis
• Localization
• Cell Adhesion
• Angiogenesis
• Cell Migration
• Cell Proliferation
• Proteolysis
• Blood Coagulation
• Rna Interference
• Ovulation

• Plasminogen Activation
• Endocytosis
• Tissue Remodeling
• Regeneration
• Aging
• Protein Secretion
• Inflammatory Response

PTMs

• Phosphorylation
• Cleavage
• Glycosylation
• Methylation

• Demethylation
• Nitrosylation
• Acetylation
• Myristoylation

Research Areas

• Neuroscience

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/SERPINE2

Best Uses of the SERPINE2 Marker

Understanding the SERPINE2 Marker's biological activity is essential in order to fully appreciate its potential uses. We will explore the many ways that it can be used in producing antibodies. We will also discuss the use of RNA interference in order to suppress the SERPINE2 protein. We will also examine the isolation and production of nucleic acids useful for the production of polypeptides.

Biological activity

Molecular analyses of tumors with the SERPINE2 marker revealed a marked difference in the amount and organization of the ECM. SERPINE2-expressing cancers had significantly greater amounts of ECM proteins. These were evident by prominent fibrous bundles. Contrary to this, tumors lacking SERPINE2 had very little ECM fiber formation. For tumor-targeting therapies, the SERPINE2 marker can be important.

SERPINE2-expressing tumors had higher levels of ECM components in xenografts and prominent fibrous bundles. While ECM is traditionally considered a largely inert scaffold, it has recently been found to actively regulate the growth, adhesion, migration, and invasion of cells. SERPINE2 overexpression in pancreatic tumors did not enhance the metastatic potential of the tumors.

The SERPINE2 marker is linked to LRP1 and BAP31 expression in human cells. These proteins are involved for the phosphorylation Erk1/2/p38. The SERPINE2 does not phosphorylate the BAP31 protein, but it is likely to impact the phosphorylation Erk1/2/p38. This is another indication SERPINE2 could be a downstream gene to BAP31.

The SERPINE2 marker provides excellent tools for pancreatic tumor research. SERPINE2 expression can be found in many gastrointestinal tissues. It was found in G1 and G2 gastric carcinomas and C1-C3 colon adenocarcinomas. Normal pancreas tissue does not express SERPINE2 protein.

Myocardial fibrblasts and mastmyocardial cells make up the majority of the heart. SerpinE2 can be expressed by both fibroblasts or myocardial fibroblasts in varying amounts. This marker is present in both the cytosol, the extracellular spaces, and is expressed at higher levels by the myocardialfibroblast. UniProtKB/SwissProt database identified its subcellular location. The protein is mainly secreted from the cytosol and extracellular space.

Antibodies that inhibit SERPINE2 function

Recent studies have shown SERPINE2 is differentially expressed by different types of tumors. Contrary to normal tissues SERPINE2 is expressed in high levels in tumors. These include the breast, thyroid, as well as testis. While low levels are possible, most tumors are benign. SERPINE2 expression levels are also elevated in many types, including glioma.

Complex mechanisms govern SERPINE2's function. It regulates the expression of MMP-9 and uPA, which are involved in cell migration and invasion. It is also implicated with MEK-induced and BRAF-induced tumorigenesis. It has also been shown that it can increase the production ECM in pancreatic carcinoma. As a result, blocking SERPINE2 function may inhibit the growth of tumors, promote their metastasis, and lead to increased patient survival.

Normal pancreas expression of SERPINE2 is low. It is high in pancreatic tumors, which promotes drug resistant genes. SERPINE2 plays a complex role in tumor development. This may be due to its tissue specificity and individual genetic differences as well as varying levels of expression. Its role in tumor development depends on the type of tumor and type of the tumor cells.

Studies have shown that SERPINE2/PN-1 contributes to airway remodeling. Anti-SERPINE2 antibodies were blocked by a monoclonal antibody that inhibited SERPINE2. This reduced asthmatic mice's airway remodeling. Inhibition may involve the activation of the ERK pathway as well as downregulation MMP-9, TIMP-1. These effects may lead to clinical trials of antiSERPINE2 therapies.

SERPINE2 expression is suppressed by RNA interference

RNA interference is a form of post-transcriptional gene silencing. It is a form RNA interference that results in the degradation of RNA through a sequence specific and sequence-independent process. RNA interference is a powerful technique to repress SERPINE2 expression. It is not like a conventional method of silencing genetics. Here, we will look at its basic mechanism.

The RNA interfering technology works by delivering small molecules of RNA to knock down a particular gene. The field of RNA interference is growing rapidly in research laboratories all over the world. It offers several advantages over traditional methods of gene silence. This new technique could revolutionize key areas in medical research. Although RNAi has been around for many years, it has only recently started to have a significant impact on the field.

Isolated nucleic Acids are useful in the production polypeptides

Molecular biology is primarily concerned in the isolation of nucleic Acids, which are essential to downstream processes, analytical purpose, and preparative purposes. This process was labor-intensive and required long processes. It was also limited in terms of throughput. Today, however, several specialized protocols have been developed for the extraction of pure biomolecules. A solution-based protocol is one such method.

The self-replication mechanism behind IDA relies on mathematical equations to explain concentrations. For dynamical properties of the peptides, chain length and sequence are essential. Only certain chain combinations are suitable for catalysis. Turing instabilities can also occur in the configuration space. This is why peptides from different families are chosen because of their high relative amounts.

Recent studies have shown that PNAs with a backbone of phosphate are required for sequence-selective recognition. Mischiati C., and Nielsen PE. showed that PNAs mimic the binding sites of NFKappaB. These findings were published by Biochemistry, 37: 1917-1925. Additionally, PNAs possess antisense as well as antigene properties.

DNA is composed of three components: a nitrogenous base and a five-carbon sugar. The sugar molecule sits in the center, while the base phosphate and phosphate groups attach to the carbon. The phosphate group is responsible for the acidic nature of the nucleic acid. These three parts can then be used to synthesize peptides.

Polypeptides which retain biological activity

New cancer therapies can use peptides' unique properties to target tumors and retain their biological activity. The novel peptidetherapeutics approach is to develop a plasma stable peptide and pharmacokinetic properties. Boster Bio has created a new peptide therapeutics approach using crystallographic evidence. This will eliminate the long and difficult hunt for a small-molecule replica.