Code | CSB-NP005801m |
Product Type | Native Protein |
Size | $3008 |
Relevance | The fragment crystallizable region (Fc region) is the tail region of an antibody that interacts with cell surface receptors called Fc receptors and some proteins of the complement system. This property allows antibodies to activate the immune system. InIgG, IgA and IgD antibody isotypes, the Fc region is composed of two identical protein fragments, derived from the second and third constant domains of the antibody's two heavy chains; IgM and IgE Fc regions contain three heavy chain constant domains (CH domains 2–4) in each polypeptide chain. The Fc regions of IgGs bear a highly conserved N-glycosylation site. Glycosylation of the Fc fragment is essential for Fc receptor-mediated activity. The N-glycans attached to this site are predominantly core-fucosylated diantennary structures of the complex type. In addition, small amounts of these N-glycans also bear bisecting GlcNAc and α-2, 6 linked sialic acid residues. The other part of an antibody, called the Fab region, contains variable sections that define the specific target that the antibody can bind. By contrast, the Fc region of all antibodies in a class are the same for each species; they are constant rather than variable. The Fc region is, therefore, sometimes incorrectly termed the "fragment constant region". |
Image | |
Description | Mouse IgG Fc fragment is a native protein with full length. This protein is purified from mouse serum IgG digested with papain. Its purity was determined by SDS-PAGE and reached up to 95%. It is presented the mass molecule around 30 kDa visualized on the gel. It has been validated in ELISA, WB and SDS-PAGE applications. The fragment crystallizable region (Fc region) is the tail region of an antibody that interacts with cell surface receptors known as Fc receptors and some proteins of the complement system. This property allows antibodies to activate the immune system. The Fc regions of IgG bear a highly conserved N-glycosylation site. Glycosylation of the Fc fragment is essential for Fc receptor-mediated activity. The N-glycans attached to this site are predominantly core-fucosylated diantennary structures of the complex type. |
Tested Applications | ELISA, WB, SDS-PAGE |
Form | Liquid |
Storage Buffer | PBS, pH 7.4 |
Alias | Fragment crystallizable region |
Biological_Activity | Not test |
Purity | >95% (SDS-PAGE) |
Sequence | Full length protein |
Research Area | Immunology |
Source | Mouse serum IgG digested with papain |
Protein Names | Mouse IgG Fc fragment |
Storage | Aliquot and store at -20°C or -80°C. Avoid repeated freeze/thaw cycles. |
References |
|
Still Have Questions? | Leave a Message or Start an on-line Chat |
I am wondering if I can know the molecular weight and amino acid sequence of mouse IgG Fc fragment.
It is stated as native protein in the information sheet sorry I mixed peptide and protein. Do you mean you don't have the information on its amino acid sequence? If that's the case, do you have any suggestion on data bank that I can search since I am not a protein person?
Recombinant Human interleukin-16 protein(IL16) (Active)
Express system: E.coli
Species: Homo sapiens (Human)
Recombinant Human interleukin-16 proein(IL16) (Active)
Express system: E.coli
Species: Homo sapiens (Human)
Recombinant Human Interleukin-17B protein(IL17B) (Active)
Express system: E.Coli
Species: Homo sapiens (Human)
Recombinant Human Interleukin-1 alpha protein(IL1A) (Active)
Express system: E.coli
Species: Homo sapiens (Human)
Recombinant Human Interleukin-1 beta protein(IL1B) (Active)
Express system: E.coli
Species: Homo sapiens (Human)
Recombinant Human Interleukin-1 receptor antagonist protein(IL1RN) (Active)
Express system: E.coli
Species: Homo sapiens (Human)
Recombinant Human Interleukin-2 protein(IL2) (Active)
Express system: E.coli
Species: Homo sapiens (Human)
Recombinant Human Interleukin-3 protein(IL3) (Active)
Express system: E.coli
Species: Homo sapiens (Human)