Fc epsilon RI Protein

Fc epsilon RI Protein Overview

Fc epsilon RI reagents

The IgE receptor plays a central role in allergic disease, coupling allergen and mast cell to initiate the inflammatory and immediate hypersensitivity responses that are characteristic of disorders such as hay fever and asthma. The allergic response occurs when 2 or more high-affinity IgE receptors are crosslinked via IgE molecules that in turn are bound to an allergen (antigen) molecule. A perturbation occurs that brings about the release of histamine and proteases from the granules in the cytoplasm of the mast cell and leads to the synthesis of prostaglandins and leukotrienes--potent effectors of the hypersensitivity response. The IgE receptor consists of 3 subunits: alpha, beta (147138), and gamma (147139); only the alpha subunit is glycosylated.

Fc epsilon RI protein name

Recommended name
High affinity immunoglobulin epsilon receptor subunit alpha
Short name
FcERI
Aliases
Fc epsilon receptor Ia
Alternative name
Fc-epsilon RI-alpha IgE Fc receptor subunit alpha

Fc epsilon RI Protein Sequence

Species Human Fc epsilon RI protein
Length 257
Mass (Da) 29596
Sequence Human Fc epsilon RI protein sequence
Species Mouse Fc epsilon RI protein
Length 250
Mass (Da) 28657
Sequence Mouse Fc epsilon RI protein sequence
Species Rat Fc epsilon RI protein
Length 245
Mass (Da) 27793
Sequence Rat Fc epsilon RI protein sequence

Fc epsilon RI Protein Molecular Weight & PI

High affinity immunoglobulin epsilon receptor subunit alpha precursor (Fc-epsilon RI-alpha) (FcERI) (IgE Fc receptor subunit alpha) Homo sapiens (Human).

The parameters have been computed for the following feature

FT CHAIN 26-257 High affinity immunoglobulin epsilon

Molecular weight (Da)

27035.73

Theoretical pI

7.10

Fc epsilon RI Protein Structure

HUMAN HIGH AFFINITY FC RECEPTOR FC(EPSILON)RI(ALPHA), TETRAGONAL CRYSTAL FORM 1
Deposited
2001-05-20   Released:  2001-08-29
Deposition Author(s)
Garman, S.C., Sechi, S., Kinet, J.P., Jardetzky, T.S.
Organism(s)
Homo sapiens
Expression System
Cricetulus griseus
Experimental Data Snapshot
Method
X-RAY DIFFRACTION
Resolution
3.2000 Å
R-Value Free
0.310
R-Value Work
0.262
1J88 From PDB

Human Fc epsilon RI protein Secondary structure

Fc epsilon RI Protein Interaction

Recombinant Fc epsilon RI Protein Feature

Fc epsilon RI Protein, Human, Recombinant (His Tag)

High Purity
> 95 % as determined by SDS-PAGE
Low Endotoxin
< 1.0 EU per μg of the protein as determined by the LAL method

Recombinant Fc epsilon RI protein citations

Title
Feasibility of antibody-poly(glutamic Acid) complexes: preparation of high-concentration antibody formulations and their pharmaceutical properties
Year
2015
Author
Izaki, S;Kurinomaru, T;Maruyama, T;Uchida, T;Handa, K;Kimoto, T;Shiraki, K;
Journal
J Pharm Sci

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