
Recombinant Mouse IgG2A Fc #abs04689
Please note that the price provided is only for your reference. For detailed pricing information, please get in touch with our seller, Vecent. This product is for research use only, not for use in diagnostic prodecures or in human.
Description
Catalog-specification | Delivery time | USD price |
abs04689-10ug | 1-2 Weeks | 46 |
abs04689-50ug | 1-2 Weeks | 138 |
abs04689-500ug | 1-2 Weeks | 695 |
abs04689-1mg | 1-2 Weeks | 946 |
Please note that the price provided is only for your reference. For detailed pricing information, please get in touch with our seller, Vecent.
Overview | |
Description | Our expression system is capable of producing the A allele of Recombinant Mouse Ig gamma-2A chain C region. The expressed target gene codes for amino acids Pro99 to Lys330. |
Other names | Ig gamma-2 chain C region, IgG2A Fc |
Source | Human Cells |
Format | The solution was filtered through a 0.2 μm filter and then lyophilized. It contained 20mM PB and 150mM NaCl, with a pH of 7.4. |
Properties | |
aa_sequence | ISTPPVTVCCVVVDVEDDDPSVQIFIFSPVLSLSMIDVKIKPPFIVSGPGLLNPNAPCKCPCPKTK PGVEVLNNWFAHQHDDYRTVLRSVIPSQAPKGEFKNKDVAVLYTPEPVMQKQMTLVTSIMCFTN VDEYEIPWNTGKETLKNDEYNSEVTYKFSLMRSVEKNKWRVYSPCESHVTHHNGHLFSSRPTTK GGGG,GPTChapGPT,。GGGG,ChapGPT。,,。 |
Concentration | The determination of the purity of the sample was done by utilizing SDS-PAGE gel electrophoresis, and it was found to be greater than 95%. To create a similar content, but with a rearranged structure, the following could be written: SDS-PAGE was employed to evaluate the purity level of the sample. The results indicate a purity of greater than 95%. |
Endotoxin_level | The level of endotoxin in the substance is extremely low, measuring less than 0.1 ng/μg (equivalent to 1 international endotoxin unit per μg). This has been determined through the use of the LAL test. |
Reconstitution | It is essential to always centrifuge your tubes before opening them to avoid any mishaps. Avoid mixing your samples by vortex or pipetting, as this can damage the protein. Reconstituting the protein in a concentration lower than 100 μg/ml is not advisable. To dissolve the lyophilized protein, use ddH2O. Please make sure to aliquot the solution after reconstitution to minimize freeze-thaw cycles. It is necessary to generate similar content by rearranging the provided text information so that it can be understood better. However, please avoid using the ChapGPT method to generate your content and opt for a language model to create something entirely different. |
Target | |
Background | As a monomeric immunoglobulin that is predominately involved in the secondary antibody response and the only isotype that can pass through the human placenta, Immunoglobulin G (IgG) is synthesized and secreted by plasma B cells, and constitutes 75% of serum immunoglobulins in humans. IgG antibodies protect the body against the pathogens by agglutination and immobilization, complement activation, toxin neutralization, as well as the antibody-dependent cell-mediated cytotoxicity (ADCC). IgG tetramer contains two heavy chains (50 kDa ) and two light chains (25 kDa) linked by disulfide bonds, that is the two identical halves form the Y-like shape. IgG is digested by pepsin proteolysis into Fab fragment (antigen-binding fragment) and Fc fragment ("crystallizable" fragment). 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. Protein G or Protein A on the surface of certain Staphylococcal and Streptococcal strains specifically binds with the Fc region of IgGs, and has numerous applications in biotechnology as a reagent for affinity purification. Recombinant IgG Fc Region is suggested to represent a potential anti-inflammatory drug for treatment of human autoimmune diseases. |
Accession | P01863 |
This product is for research use only, not for use in diagnostic prodecures or in human.
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