MS4A2 Protein Overview: Sequence, Structure, Function and Protein Interaction

MS4A2 Protein Overview

The high affinity IgE receptor is responsible for initiating the allergic response. Binding of allergen to receptor-bound IgE leads to cell activation and the release of mediators (such as histamine) responsible for the manifestations of allergy. The receptor is a tetrameric complex composed of an alpha chain (147140), a beta chain, and 2 disulfide-linked gamma chains (147139). It is found on the surface of mast cells and basophils. The alpha and beta subunits have not been detected in other hematopoietic cells, although the gamma chains are found in macrophages, natural killer (NK) cells, and T cells where they associate with the low affinity receptor for IgG or with the T-cell antigen receptor. The molecular cloning of subunits permitted the reconstitution of surface-expressed receptor complexes by transfection. Cotransfection of all 3 chains--alpha, beta, and gamma--was required for efficient surface expression of the rat or mouse receptor. By contrast, surface expression of the human alpha-gamma complex was achieved by cotransfecting alpha and gamma alone, suggesting that beta is not necessary. To study the expression of the beta gene, Kuster et al. (1992) isolated and characterized the gene and its cDNA. Analysis of the surface expression of transfected receptors indicated that human alpha-gamma and alpha-beta-gamma complexes are expressed with comparable efficiency. Donnadieu et al. (2003) noted that the FCER1 tetrameric complex is expressed on mast cells and basophils, whereas the FCER1 trimeric complex lacking the beta subunit is expressed on Langerhan cells, dendritic cells, and monocytes. Thus, beta chain expression correlates with allergy mediator release, while the trimeric FCER1 form is associated with antigen presentation. The presence of the beta chain amplifies FCER1 surface expression and signaling capacity, and the beta chain acts as a chaperone for transporting the FCER1 complex to the cell surface. By RT-PCR of basophil RNA, Donnadieu et al. (2003) cloned an FCER1B splice variant that retains intron 5 and encodes a truncated protein, designated beta(T). The fourth transmembrane domain and the C-terminal tail of the full-length beta form are deleted and replaced with 16 novel amino acids in beta(T). The beta(T) variant was also present in cord blood mast cells, but not in a monocyte cell line. Immunoprecipitation and Western blot analyses showed that beta(T) was expressed as a 21-kD protein, whereas the full-length form was 28 kD. Using RT-PCR, Cruse et al. (2010) cloned an MS4A2 splice variant lacking exon 3, which they termed MS4A2-trunc, from primary human lung mast cells and the slowly dividing mast cell line LAD-2. The variant was not expressed in the rapidly growing mast cell line HMC-1. The deduced MS4A2-trunc protein retains the cytoplasmic N and C termini of full-length MS4A2, including the noncanonical ITAM, but it lacks the first 2 transmembrane domains. Unlike full-length MS4A2, the truncated variant did not traffic to the cytoplasmic membrane, but instead to the nuclear membrane, in human mast cells. Cruse et al. (2010) found that the MS4A2-trunc isoform was negatively regulated by SCF (KITLG; 184745) in human mast cells. Overexpression of MS4A2-trunc induced lung mast cell death and inhibited HMC-1 cell proliferation by inducing G2-phase cell-cycle arrest and apoptosis. Flow cytometric analysis demonstrated that MS4A2-trunc expression had no impact on FCER1A surface expression. Cruse et al. (2010) concluded that MS4A2 has roles, extending beyond the regulation of acute allergic responses. They proposed that induction of MS4A2 in mast cells may lead to better treatments for asthma and mastocytosis. Cruse et al. (2013) determined that MS4A2-trunc, which they called t-FCER1B, propagated Ca(2+) signals and was critical for microtubule formation in human mast cells. Mutation analysis suggested that Ca(2+) signaling required calmodulin (CALM1; 114180) binding to t-FCER1B in the presence of Ca(2+). Silencing of t-FCER1B attenuated microtubule formation, degranulation, and IL8 (146930) production. Cruse et al. (2013) concluded that t-FCER1B plays an important role in mast cell degranulation.

MS4A2 protein family

Belongs to the MS4A family.

MS4A2 protein name

Recommended name
High affinity immunoglobulin epsilon receptor subunit beta
Aliases
Fc fragment of IgE, high affinity I, receptor for; beta polypeptide, MS4A1

MS4A2 Gene family protein

Membrane spanning 4-domains
Approved symbol Common name
MS4A1 CD20 protein, recombinant

MS4A2 Protein Molecular Weight & PI

The parameters have been computed for the following feature

FT CHAIN 1-244 High affinity immunoglobulin epsilon

Molecular weight (Da)

26533.69

Theoretical pI

5.05

Bulk Order of Recombinant MS4A2 Protein

Please Leave Us a Message if you have any questions regarding bulk price quote of our products on the website, our customer specialist will get back to you in 24 hours by email.

Custom Recombinant Protein Production Service Features

  • Over 10 years' experience for 6000+ recombinant proteins production.
  • One-stop service from gene synthesis and vector construction to protein expression and purification.
  • Multiple protein expression systems: bacterial, yeast, baculovirus-insect and mammalian expression system.
  • Multiple purification systems (30+) to choose.
  • High R & D ability with over 1000 new proteins per year and quick problem-solving ability.
  • Close to 100 bioreactors with various volume between 2-1000 L to guarantee high-throughput and large-scale production.

Custom Recombinant Protein Production Service Advantages

  • High-efficiency expression vectors
  • High cell density culturing
  • Proprietary medium formulation
  • >6000 proteins expression and purification experience
  • High-efficiency expression vectors
  • High cell density culturing

Recombinant Protein Production Service Description

We offer one-stop services for recombinant protein production using our advanced protein expression platform technologies. Our full services include protein gene synthesis, protein codon optimization, protein expression vector design, large scale cell culture and fermentation, protein purification, and protein quality control testing. We offer significant cost saving advantages and record speed in protein expression and bulk production. We also have extensive experiences and expertise in handling various types of recombinant protein purification projects, with or without purification tags.