Target Name: LRFN2
NCBI ID: G57497
Review Report on LRFN2 Target / Biomarker Content of Review Report on LRFN2 Target / Biomarker
LRFN2
Other Name(s): Fibronectin type III, immunoglobulin and leucine rich repeat domains 2 | Leucine-rich repeat and fibronectin type-III domain-containing protein 2 | KIAA1246 | LRFN2_HUMAN | SALM1 | leucine rich repeat and fibronectin type III domain containing 2 | Synaptic adhesion-like molecule 1 | FIGLER2 | OTTHUMP00000016361 | synaptic adhesion-like molecule 1 | RP11-535K1.2 | Leucine rich repeat and fibronectin type III domain containing 2 | fibronectin type III, immunoglobulin and leucine rich repeat domains 2

LRFN2: A Protein Involved in Cell Adhesion, Migration and Invasion

LRFN2 (Leucine Rich Repeat Domain 2) is a protein that is expressed in a variety of tissues throughout the body, including connective tissue, skin, and organs. It is a member of the immunoglobulin (Ig) family and contains several unique domains, including an N-terminal fibronectin type III domain, a central 尾-sheet, and a C-terminal leucine rich repeat (LRR) domain. LRFN2 has been shown to play a role in several cellular processes, including cell adhesion, migration, and invasion.

The LRFN2 gene was identified and sequenced in the human genome, and it has been shown to encode a protein that contains several unique domains. The N-terminal domain of LRFN2 is a fibronectin type III domain, which is a type of extracellular matrix (ECM ) protein that is involved in cell-cell adhesion and tissue remodeling. The central 尾-sheet is a region of the protein that contains several conserved secondary structure elements, such as a long alpha-helices and a 尾-sheet. The C- Terminal domain is a leucine rich repeat (LRR) domain, which is a type of protein domain that is characterized by a repeated sequence of leucine amino acids.

LRFN2 has been shown to play a role in several cellular processes, including cell adhesion, migration, and invasion. For example, LRFN2 has been shown to be involved in the process of cell adhesion, as it has been shown to interact with several ECM proteins , including E-cadherin and N-cadherin. LRFN2 has also been shown to be involved in the process of cell migration, as it has been shown to promote the migration of cancer cells. In addition, LRFN2 has been shown to be involved in the process of cell invasion, as it has been shown to promote the invasion of cancer cells into surrounding tissue.

LRFN2 has also been shown to contain several unique biological processes. For example, LRFN2 has been shown to play a role in the regulation of cell signaling pathways, as it has been shown to interact with several signaling proteins, including TGF-β and NF-kappa-B. LRFN2 has also been shown to play a role in the regulation of cell growth, as it has been shown to regulate the growth of cancer cells in several ways, including through the inhibition of the cell cycle and the inhibition of the angiogenesis.

In conclusion, LRFN2 is a protein that is expressed in a variety of tissues throughout the body and is involved in several cellular processes, including cell adhesion, migration, and invasion. It is a member of the immunoglobulin family and contains several unique domains, including an N-terminal fibronectin type III domain, a central 尾-sheet, and a C-terminal LRR domain. LRFN2 is a potential drug target or biomarker, and further research is needed to fully understand its role in cellular processes and its potential as a therapeutic agent.

Protein Name: Leucine Rich Repeat And Fibronectin Type III Domain Containing 2

Functions: Promotes neurite outgrowth in hippocampal neurons. Enhances the cell surface expression of 2 NMDA receptor subunits GRIN1 and GRIN2A. May play a role in redistributing DLG4 to the cell periphery (By similarity)

The "LRFN2 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about LRFN2 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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LRFN3 | LRFN4 | LRFN5 | LRG1 | LRGUK | LRIF1 | LRIG1 | LRIG2 | LRIG2-DT | LRIG3 | LRIG3-DT | LRIT1 | LRIT2 | LRIT3 | LRMDA | LRP1 | LRP10 | LRP11 | LRP12 | LRP1B | LRP2 | LRP2BP | LRP3 | LRP4 | LRP4-AS1 | LRP5 | LRP5L | LRP6 | LRP8 | LRPAP1 | LRPPRC | LRR1 | LRRC1 | LRRC10 | LRRC10B | LRRC14 | LRRC14B | LRRC15 | LRRC17 | LRRC18 | LRRC19 | LRRC2 | LRRC2-AS1 | LRRC20 | LRRC23 | LRRC24 | LRRC25 | LRRC26 | LRRC27 | LRRC28 | LRRC3 | LRRC30 | LRRC31 | LRRC32 | LRRC34 | LRRC36 | LRRC37A | LRRC37A11P | LRRC37A14P | LRRC37A15P | LRRC37A16P | LRRC37A17P | LRRC37A2 | LRRC37A3 | LRRC37A4P | LRRC37A5P | LRRC37A6P | LRRC37A7P | LRRC37A9P | LRRC37B | LRRC37BP1 | LRRC38 | LRRC39 | LRRC3B | LRRC3C | LRRC4 | LRRC40 | LRRC41 | LRRC42 | LRRC43 | LRRC45 | LRRC46 | LRRC47 | LRRC49 | LRRC4B | LRRC4C | LRRC52 | LRRC52-AS1 | LRRC53 | LRRC55 | LRRC56 | LRRC57 | LRRC58 | LRRC59 | LRRC61 | LRRC63 | LRRC66 | LRRC69 | LRRC7 | LRRC70