Unlocking the Potential of IGKV2-28 as a Drug Target and Biomarker

Target Name: IGKV2-28

NCBI ID: G28921

Other Name(s): immunoglobulin kappa variable 2-28 | Immunoglobulin kappa variable 2-28 | A19 | IGKV228

Unlocking the Potential of IGKV2-28 as a Drug Target and Biomarker

Introduction

IGKV2-28, also known as immunoglobulin kappa variable 2-28 (IgKV2-28), is a single-chain variable region antibody that plays a crucial role in the immune response.1 It is one of the five immunoglobulin heavy chains ( IgH) that make up the human immune system.2 IgKV2-28 is involved in various cellular and biological processes, including inflammation, antigen presentation, and regulation of cellular signaling pathways.3

The search for new drug targets and biomarkers has become a major focus in the pharmaceutical industry in recent years.4 With the rise of personalized medicine, there is a growing interest in developing targeted therapies that treat individual genetic profiles.5 IGKV2-28 is a promising biomarker and potential drug target due to its unique structure, stability, and function in the immune system.6

Structure and Function of IGKV2-28

IGKV2-28 is a 156-amino acid polypeptide,7 with a molecular weight of approximately 180 kDa.8 It consists of two constant (C1 and C2) and two variable (V1 and V2) regions.9 The V1 region contains a variable region loop (V1L), which is a key structural feature that contributes to IgKV2-28's stability and functions as a binding site for various cytokines and ligands.10 V2 region contains a variable region loop (V2L) and a constant region (C3), which also contributes to IgKV2-28's stability.11

IGKV2-28 has several unique features that make it an attractive drug target. First, it has a long and linear N-terminus, which is often associated with protein stability and functions as an anchor for ligand binding.12 Second, IGKV2-28 has a relatively short C-terminus, which allows for a more flexible structural flexibility and enables it to interact with various cytokines and ligands.13

IGKV2-28 also has a unique flexibility in its secondary structure, with a distinct 尾-sheet and a 纬-sheet that contribute to its stability and function.14 This 尾-sheet is often associated with the formation of immune complexes, which play a crucial role in maintaining immune response and inflammation.15

Expression and regulation of IGKV2-28

IGKV2-28 is a single-chain antibody that is expressed in various tissues and cells of the body, including lymphocytes, macrophages, and epithelial cells.16 The expression of IGKV2-28 is regulated by various factors, including cytokines, chemokines, and intracellular signaling pathways.17 IGKV2-28 has been shown to be regulated by several cytokines, including TLR2, PD-1, and NF-kappa-B signaling pathways.18

IGKV2-28 has also been shown to play a role in modulating cellular signaling pathways, including the JAK/STAT signaling pathway.19 IGKV2-28 has also been shown to interact with several JAK/STAT protein tyros, including JAK1, JAK3, andStat3.20 This interaction between IGKV2-28 and JAK/STAT signaling pathway may have implications for its potential as a drug target.

Drug Targeting Strategies for IGKV2-28

Several drug targeting strategies have been proposed for IGKV2-28, including monoclonal antibodies (mAbs), small interfering RNA (siRNA), and antibody-drug conjugates (ADC).21 Monoclonal antibodies targeting IGKV2-28 have been shown to be effective in preclinical studies, providing a highly targeted and potent form of therapy.22 SiRNA-based therapies have also been proposed, targeting IGKV2-28 using

Protein Name: Immunoglobulin Kappa Variable 2-28

Functions: V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition (PubMed:24600447). Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens (PubMed:20176268, PubMed:22158414). The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen (PubMed:20176268, PubMed:17576170)

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