Human varicella zoster virus gE protein antibody

All products of our company are for scientific experiments only and are not intended for use outside of scientific experiments!

Don't Name;GE_VZVO; Envelope glycoprotein E; gE; Human Varicella zoster virus; membrane glycoprotein E; 68; Glycoprotein E;

The first antibody is commonly referred to as an antibody, which can specifically bind to antigens.

The second antibody is an antibody that can bind to antibodies, that is, antibodies. Mainly used to detect the presence of antibodies.

The primary antibody is an antibody against an antigen, and the secondary antibody is an antibody against the primary antibody. Antibodies can also act as antigens to stimulate the body to produce antibodies. That is to say, antigens entering the body stimulate the immune response, and B cells can produce special proteins that specifically bind to the corresponding antigens.

Both primary and secondary antibodies are functional groups that can specifically bind to other substances, and primary antibodies can bind to at least two other functional groups (substrates and secondary antibodies).

Primary antibody: It can specifically bind to substrates, which is to recognize what we want to detect. Whether the primary antibody binds to the substrate or not

It cannot be seen with the naked eye.

Secondary antibody: can bind to primary antibody and carry detectable markers (such as fluorescent, radioactive, chemiluminescence, or chromogenic groups), with the function of detecting primary antibody. If the primary antibody carries detectable markers (such as fluorescent, radioactive, chemiluminescent, or chromogenic groups), there is no need for a secondary antibody. But this is costly because a single antibody only recognizes one substrate. So nowadays, the design usually involves adding detectable markers to the secondary antibody before testing the primary antibody. And the primary antibody recognizes substrates. In this way, when the primary antibody binds to the substrate, it can be detected by the secondary antibody.

Research field; Bacteria and viruses

Source of antibodies;Rabbit

Clone type;Polyclonal

Product application;ELISA=1:5000-10000

not yet tested in other applications.

optimal dilutions/concentrations should be determined by the end user.

Theoretical molecular weight;65kDa

Cell localization; cytoplasm cell membrane

sex State;Liquid

thick Degree;1mg/ml

exempt epidemic Original;KLH conjugated synthetic peptide derived from VZV Envelope glycoprotein E: 521-623/623

Asia Type;IgG

Purification method;affinity purified by Protein A

slow rush Liquid;0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.

Preservation conditions;Shipped at 4℃. Store at -20 °C for one year. Avoid repeated freeze/thaw cycles.

matters needing attention;This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.

Varicella Zoster Virus (VZV), a member of the human herpes virus family, causes two distinct clinical manifestations: childhood chickenpox(Varicella) and shingles (zoster). Varicella is the outcome of the primary infection with VZV

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Through X-ray crystal diffraction analysis, it was found that Ig is composed of four polypeptide chains, which are connected by varying numbers of interchain disulfide bonds. Ig can form a "Y" - shaped structure, called an Ig monomer, which is the basic unit that constitutes antibodies.

Natural Ig molecules contain four heterologous polypeptide chains, among which the two chains with larger molecular weight are called heavy chains (H), while the two chains with smaller molecular weight are called light chains (L). The amino acid composition of two H chains and two L chains in the same Ig molecule is the same. The heavy chain has a molecular weight of 50KD to 75KD and is composed of 450 to 550 amino acid residues. Due to the different composition and arrangement of amino acids in the constant region of heavy chains, as well as the number and position of disulfide bonds, the antigenicity of Ig varies. Ig can be divided into five classes: IgM, IgD, IgG, IgA, and IgE, with corresponding heavy chains being μ chain, δ chain, γ chain, α chain, and ε chain. The molecular weight of the light chain is approximately 25KD, consisting of 214 amino acid residues. Light chains can be divided into two types, namely kappa (κ) chains and lambda (λ) chains. Therefore, lg can be divided into two types, namely kappa type and lambda type. The kappa: lambda ratio of normal human serum Ig is approximately 2:1.

By comparing and analyzing the amino acid sequences of different Ig heavy and light chains, it was found that the amino terminal (N-terminal) amino acid sequence had significant changes, known as the variable region (V), which accounted for 1/4 and 1/2 of the heavy and light chains, respectively; The region where the amino acid sequence at the C-terminus is relatively stable is called the constant region (C), which accounts for 3/4 and 1/2 of the heavy and light chains, respectively.

The V regions of heavy and light chains are called VH and VL, respectively. VH and VL each contain three highly variable regions of amino acid composition and arrangement, known as hypervariable regions (HVR) or complementarity determining regions (CDRs), including HVR1 (CDR1), HVR2 (CDR2), and HVR3 (CDR3), with HVR3 (CDR3) showing a higher degree of variation. The three hypervariable regions of VH are located at amino acids 29-31, 49-58, and 95-102, respectively, while the three hypervariable regions of VL are located at amino acids 28-35, 49-56, and 91-98, respectively. The three CDRs of VH and VL together form the antigen binding site of Ig, which determines the specificity of the antibody and is the site where the antibody recognizes and binds to the antigen. In the V region, the amino acid composition and arrangement order outside the CDR region are relatively conserved, known as the backbone region (FR). VH or VL each have four skeletal regions, represented by FR1, FR2, FR3, and FR4, respectively.

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