Weight | 1 lbs |
---|---|
Dimensions | 9 × 5 × 2 in |
host | mouse |
isotype | IgG |
clonality | monoclonal |
concentration | concentrate, predilute |
applications | IHC |
reactivity | human |
available size | 0.1 mL, 0.5 mL, 1 mL concentrated, 7 mL prediluted |
rabbit anti-IgA monoclonal antibody (ZR291) 6221
$160.00 – $528.00
Antibody summary
- Rabbit monoclonal to IgA
- Suitable for: Immunohistochemistry (formalin-fixed, paraffin-embedded tissues)
- Reacts with: Human
- Isotype:IgG
- Control: Lymph node
- Visualization: Cytoplasmic, cell surface
- 0.1, 0.5, 1.0 mL concentrated, 7 mL prediluted
rabbit anti-IgA monoclonal antibody ZR291 6221
target relevance |
---|
Protein names Immunoglobulin heavy constant alpha 1 (Ig alpha-1 chain C region) (Ig alpha-1 chain C region BUR) (Ig alpha-1 chain C region TRO) |
Mass 42849Da |
Function Constant region of immunoglobulin heavy chains. 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:17576170, PubMed:20176268). Ig alpha is the major immunoglobulin class in body secretions (PubMed:2241915). . |
Subellular location [Isoform 1]: Secreted .; [Isoform 2]: Cell membrane ; Single-pass type I membrane protein . |
Structure Immunoglobulins are composed of two identical heavy chains and two identical light chains; disulfide-linked (PubMed:20176268). Monomeric or polymeric (PubMed:2241915). Part of the secretory IgA (sIgA) complex that consists of two, four or five IgA monomers, and two additional non-Ig polypeptides, namely the JCHAIN and the secretory component (the proteolytic product of PIGR). . |
Post-translational modification PTM: [Isoform 1]: 3-Hydroxykynurenine, an oxidized tryptophan metabolite that is common in biological fluids, reacts with alpha-1-microglobulin to form heterogeneous polycyclic chromophores including hydroxanthommatin. The chromophore reacts with accessible cysteines forming non-reducible thioether cross-links with Ig alpha-1 chain C region Cys-352. .; PTM: N- and O-glycosylated. N-glycan at Asn-144: Hex5HexNAc4. . |
Domain DOMAIN 6..98; /note="Ig-like 1"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"; DOMAIN 125..220; |
Involvement in disease Note=A chromosomal aberration involving IGHA1 is found in multiple myeloma (MM) cell lines. Translocation t(1;14)(q21;q32) that forms a FCRL4-IGHA1 fusion protein. . |
Target Relevance information above includes information from UniProt accession: P01876 |
The UniProt Consortium |
Data
Formalin-fixed, paraffin-embedded human tonsil stained with anti-IgA antibody using peroxidase-conjugate and DAB chromogen. Note cytoplasmic staining of plasma cells |
Publications
Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.pmid | title | authors | citation |
---|
Protocols
relevant to this product |
---|
IHC |
Documents
# | |||
---|---|---|---|
Please enter your product and batch number here to retrieve - product datasheet, SDS, and QC information. |
Only logged in customers who have purchased this product may leave a review.
Reviews
There are no reviews yet.