Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | P01857 |
express system | HEK293 |
product tag | No Tag |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
background | IgG1 is most abundant in serum among the four IgG subclasses (IgG1, 2, 3 and 4) and binds to Fc receptors (FcγR) on phagocytic cells with high affinity. Fc fragment is demonstrated to mediate phagocytosis, trigger inflammation, and target Ig to particular tissues.IgG1 Fc was reported has a novel role as a potential anti-inflammatory drug for treatment of human autoimmune diseases. |
molecular weight | The protein has a predicted MW of 25.5 kDa. Due to glycosylation, the protein migrates to 31-33 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human IgG1 Fc Protein 4674
$75.00 – $250.00
Summary
- Expression: HEK293
- Binding assay: Yes (SPR)
- Amino Acid Range: Asp104-Lys330
Human IgG1 Fc Protein 4674
protein |
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Size and concentration 100, 500µg and lyophilized |
Form Lyophilized |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped at ambient temperature. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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IgG1 is most abundant in serum among the four IgG subclasses (IgG1, 2, 3 and 4) and binds to Fc receptors (FcγR) on phagocytic cells with high affinity. Fc fragment is demonstrated to mediate phagocytosis, trigger inflammation, and target Ig to particular tissues.IgG1 Fc was reported has a novel role as a potential anti-inflammatory drug for treatment of human autoimmune diseases. |
Protein names Immunoglobulin heavy constant gamma 1 (Ig gamma-1 chain C region) (Ig gamma-1 chain C region EU) (Ig gamma-1 chain C region KOL) (Ig gamma-1 chain C region NIE) |
Gene names IGHG1,IGHG1 |
Mass 9606Da |
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). Mediates IgG effector functions on monocytes triggering ADCC of virus-infected cells. |
Subellular location [Isoform 1]: Secreted .; [Isoform 2]: Cell membrane ; Single-pass membrane protein . |
Structure Immunoglobulins are composed of two identical heavy chains and two identical light chains; disulfide-linked (PubMed:20176268). Interacts with FCGR1A; this interaction mediates IgG effector functions on monocytes. Interacts with FCGR2A and FCGR3A (PubMed:11711607). |
Post-translational modification Glycosylation on Asn-180 is required for interaction with Fc receptors and ability to activate the complement pathway.; (Microbial infection) Deglycosylation on Asn-180 by S.pyogenes EndoS or Endos2 endoglucosidases prevents interaction between immunoglobulin-gamma (IgG) and Fc receptors, impairing ability to activate the complement pathway. |
Target Relevance information above includes information from UniProt accession: P01857 |
The UniProt Consortium |
Data
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 |
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Protocols
relevant to this product |
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Documents
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