图片区自拍区 亚洲欧美-欧美精东天美夜夜嗨牛牛-亚洲av制服一区二区三区-丝袜高跟鞋ol中文字幕

Immunoglobulin G (IgG), is one of the most abundant proteins in serum with normal levels between 8-17 mg/mL in adult blood. IgG is important for our defence against microorganisms and the molecules are produced by B lymphocytes as a part of our adaptive immune response. The IgG molecule has two separate functions; to bind to the pathogen that elicited the response and to recruit other cells and molecules to destroy the antigen. The variability of the IgG pool is generated by somatic recombin

Immunoglobulin G (IgG), is one of the most abundant proteins in serum with normal levels between 8-17 mg/mL in adult blood. IgG is important for our defence against microorganisms and the molecules are produced by B lymphocytes as a part of our adaptive immune response. The IgG molecule has two separate functions; to bind to the pathogen that elicited the response and to recruit other cells and molecules to destroy the antigen. The variability of the IgG pool is generated by somatic recombin

Immunoglobulin G (IgG), is one of the most abundant proteins in serum with normal levels between 8-17 mg/mL in adult blood. IgG is important for our defence against microorganisms and the molecules are produced by B lymphocytes as a part of our adaptive immune response. The IgG molecule has two separate functions; to bind to the pathogen that elicited the response and to recruit other cells and molecules to destroy the antigen. The variability of the IgG pool is generated by somatic recombin

IgM normally constitutes about 10% of serum immunoglobulins. IgM antibody is prominent in early immune responses to most antigens and is largely confined to plasma due to it's large size. Monomeric IgM is expressed as a membrane bound antibody on the surface of B cells and as a pentamer when secreted by plasma cells. Due to it's high valency IgM is more efficient than other isotypes is binding antigens with repeating epitopes (virus particles and red blood cells) and is more efficient tha

The biological function of avidin is not known. It is a homotetrameric glycoprotein found in chicken egg white, and forms a strong non covalent specific complex with biotin (one molecule of biotin per subunit of avidin).$n$n

IgM normally constitutes about 10% of serum immunoglobulins. IgM antibody is prominent in early immune responses to most antigens and is largely confined to plasma due to it's large size. Monomeric IgM is expressed as a membrane bound antibody on the surface of B cells and as a pentamer when secreted by plasma cells. Due to it's high valency IgM is more efficient than other isotypes is binding antigens with repeating epitopes (virus particles and red blood cells) and is more efficient tha