{"id":11189,"date":"2025-05-07T06:08:26","date_gmt":"2025-05-07T10:08:26","guid":{"rendered":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/?p=11189"},"modified":"2026-01-05T10:54:49","modified_gmt":"2026-01-05T15:54:49","slug":"why-use-a-particular-antibody-format","status":"publish","type":"post","link":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/immuno-techniques\/why-use-a-particular-antibody-format\/","title":{"rendered":"Why use a particular Antibody format?"},"content":{"rendered":"\n\n\n\t<div class=\"dkpdf-button-container\" style=\" text-align:right \">\n\n\t\t<a class=\"dkpdf-button\" href=\"\/secondary-antibody-resource\/wp-json\/wp\/v2\/posts\/11189?pdf=11189\" target=\"_blank\"><span class=\"dkpdf-button-icon\"><i class=\"fa fa-file-pdf-o\"><\/i><\/span> Download PDF<\/a>\n\n\t<\/div>\n\n\n\n\n\n<style>.entry p, .entry ol{font-size: 1rem;}.entry h3{color:#009fe3;margin-top:0}.entry h4{color:#009453;margin-top:1.5rem}.entry h5{color: #003a5c; font-size: 1.05rem;margin-top:1.5rem;}.entry figure{margin:32px auto;border:1px solid #ccc}.entry figure img{width:100%;display:block;margin:0 auto}.entry figcaption{font-size:.875rem;line-height:1.35rem;padding:10px;color:#222}.entry .blog-tbl{margin:1rem auto;caption-side:bottom}.entry .blog-tbl td,.entry .blog-tbl th{padding:10px 9px;border:1px solid #00172b;text-align:left}.entry .blog-tbl td{border-color:#003a5c}.entry .blog-tbl th{background-color:#00172b;color:#fff;border-left-color:#fff;border-right-color:#fff}.entry .blog-tbl th p{color:#fff}.entry .blog-tbl th:first-of-type{border-left-color:#00172b}.entry .blog-tbl th:last-of-type{border-right-color:#00172b}.entry .blog-tbl p{text-align:left;margin:0}.entry .box-note{border:2px solid #009453;padding:12px;margin:1rem 0}.entry .box-note p{margin:0;padding:0}.entry .styled-list{list-style-type:none}.entry .styled-list li{margin-top:1rem;line-height:22px;font-size:1rem;}.entry .styled-list li::before{font-family:\"Font Awesome 5 Pro\";display:inline-block;content:\"\\f3c5\";-webkit-transform:rotate(-90deg);transform:rotate(-90deg);margin-left:-20px;margin-right:11px;font-size:.75rem;color:#ed7004;font-weight:600}.entry .styled-list ol li::before{display:none}.entry .styled-list li>ul li::before{font-weight:200}.entry .overview{width:-webkit-fit-content;width:-moz-fit-content;width:fit-content;padding:16px;margin:1rem auto;border:1px solid #eee}.entry .overview hr{margin-top:14px}.entry .overview-text{text-align:center;font-size:1rem;margin:0}.entry .btn-sq{color:#fff;font-size:.9rem;font-weight:600;border:2px solid rgb(237, 112, 4);padding:7px 13px;background:rgb(237, 112, 4);cursor:pointer;text-align:center;line-height:1.5rem;margin:0 auto;}.entry .btn-sq:hover{text-decoration:none;color:rgb(237, 112, 4);background:#fff;}.entry .btn-container{display:flex;width:100%;margin:1.3rem 0;}.entry .btn-container .fa-solid, .entry .btn-container .fa-duotone{margin-right:10px;}@media(max-width: 768px){.entry .btn-sq{font-size:1.05rem;}}<\/style>\n<style>.entry h4{margin-top: 2rem;}.entry ol li{line-height: 1.6rem;margin-top:1rem;}<\/style>\n<p><script src=\"https:\/\/kit.fontawesome.com\/904923013f.js\" crossorigin=\"anonymous\"><\/script><\/p>\n<div class=\"entry\">\n<h2>Here, we discuss the differences between the different antibody formats available, including H+L, F(ab\u2032)<sub>2<\/sub>, Fab, and VHH fragment antibodies. We will address how they can offer solutions to your experimental setup, help you improve specificity and resolution, and circumvent limitations.<\/h2>\n<p><img decoding=\"async\" loading=\"lazy\" class=\"aligncenter wp-image-11038 size-full\" src=\"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/anti-gfp-hero.jpg\" alt=\"\" width=\"700\" height=\"169\" srcset=\"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/anti-gfp-hero.jpg 700w, https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/anti-gfp-hero-300x72.jpg 300w\" sizes=\"(max-width: 700px) 100vw, 700px\" \/><\/p>\n<h4>Antibody Formats &#8211; not just the heavy and light chain<\/h4>\n<p>Jackson ImmunoResearch offers Affinity-Purified secondary antibodies in four different formats. Select from <a href=\"\/technical\/products\/groups\/whole-igg\">Whole IgG<\/a>, <a href=\"\/technical\/products\/groups\/fab2\">F(ab&#8217;)<sub>2<\/sub> fragment<\/a>, <a href=\"\/technical\/products\/groups\/fab\">Fab fragment<\/a>, and <a href=\"\/technical\/products\/AffiniPure-VHH-secondary-antibodies\">VHH fragment antibodies<\/a>. The optimal format for your experiment depends largely on the intended application and expectations. Whole molecule antibodies, comprised of both heavy and light chains, making up the Fab and Fc domains, are suitable for most immunodetection procedures. However, the specialist formats of F(ab&#8217;)<sub>2<\/sub>, Fab, and VHH antibodies can offer advantages to users with specific assay requirements.<\/p>\n<figure style=\"max-width: 500px;\"><img decoding=\"async\" loading=\"lazy\" width=\"500\" height=\"400\" class=\"aligncenter wp-image-2574 size-full\" style=\"width: 95%; margin-top: 1rem; margin-left: 0;\" src=\"\/secondary-antibody-resource\/wp-content\/uploads\/digest.jpg\" alt=\"\" srcset=\"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/digest.jpg 500w, https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/digest-300x240.jpg 300w\" sizes=\"(max-width: 500px) 100vw, 500px\" \/><figcaption><strong>Figure 1:<\/strong> The digestion of IgG (approximate MW = 160 kDa) yields several different fragments. Papain digestion generates two monovalent Fab fragments and an Fc fragment, each about 50 kDa. Pepsin digestion degrades the Fc domain, leaving a divalent F(ab&#8217;)<sub>2<\/sub> fragment with an approximate MW of 110 kDa.<\/figcaption><\/figure>\n<h4>Whole-molecule antibodies<\/h4>\n<p>Canonical or conventionally shaped immunoglobulins are antibodies with heavy and light chains that make up the easily recognizable Y shape. The Y shape is a monomeric subunit of the immunoglobulin, even if both chain species aren\u2019t present (see camelid antibodies below). The antibody may exist as a Y monomer in the immunoglobulin classes D, E, and G. Whereas Ig class A exists as both a monomer and a dimer, and IgM as a pentamer or hexamer.<\/p>\n<p>The arms of the Y consist of two antigen-binding regions called a Fab (Fragment antigen binding) fragment. The Fab arms are joined together by disulfide bonds (Figure 1). With the exception of many engineered antibodies (learn more), the two arms are typically specific (bind) to the same epitope, making the antibody divalent.<\/p>\n<p>The trunk of the antibody is made up of the Fc (fragment crystallizable) region or domain. This Fc domain confers the antibody\u2019s functionality in its biological setting. Specific receptors bind to it, activating downstream pathways.<\/p>\n<p>The whole Ig molecule is a commonly used antibody format suitable for most immunoassays and immunodetection applications. IgG is roughly 160 kDa, and the other classes vary slightly in their monomeric subunit.<\/p>\n<div class=\"btn-container\"><a class=\"btn-sq\" href=\"\/technical\/products\/groups\/whole-igg\"><i class=\"fa-duotone fa-book-open-reader\"><\/i>Read more about whole IgG format secondary antibodies<\/a><\/div>\n<h4>F(ab&#8217;)<sub>2<\/sub> Fragment antibodies<\/h4>\n<p>Another format that antibodies can be found in is as an F(ab\u2019)<sub>2<\/sub> fragment antibody. These comprise the two Fab arms linked by part of the antibody hinge. The F(ab\u2019)<sub>2<\/sub> is generated by limited proteolysis using pepsin digestion of whole IgG antibodies. The digestion removes most of the Fc region whilst leaving some of the hinge region intact. Consequently, the two Fab arms\/fragments are linked to create the F(ab\u2019)<sub>2<\/sub> fragments, making them divalent. Their average molecular weight is about 110 kDa.<\/p>\n<p>F(ab\u2019)<sub>2<\/sub> antibodies are generally used for specific applications due to the absence of the Fc domain. One application is when it is necessary to avoid the secondary antibody binding to live cells via their Fc receptors. Consequently, they are popular in flow cytometry or FACS (fluorescence-activated cell sorting) experiments where avoiding internalization or stimulation of various cell types is desirable. F(ab\u2019)<sub>2<\/sub> antibodies can offer the same specificity, cross adsorption, and conjugate options as whole molecule antibodies, but because the F(ab\u2019)<sub>2<\/sub> format is popular for flow cytometry applications, they are often available conjugated to fluorescent proteins such as PerCP, APC, and R-PE. These large fluorescent proteins are ideal for surface staining and can provide excellent signal. F(ab\u2019)<sub>2<\/sub> antibodies can also be useful to avoid binding Protein A or G.<\/p>\n<div class=\"btn-container\"><a class=\"btn-sq\" href=\"\/technical\/products\/groups\/fab2\"><i class=\"fa-duotone fa-book-open-reader\"><\/i>Read more about F(ab\u2019)<sub>2<\/sub> fragment secondary antibodies<\/a><\/div>\n<div class=\"box-note\">\n<p>Caution: Primary antibodies can still bind to Fc receptors expressed on the sample cells\u2019 surface if the primary antibodies are whole IgG format antibodies. This binding can generate background signal\/ non-specific signal regardless of the format of the secondary antibody.<\/p>\n<\/div>\n<p>To avoid Fc receptor binding, generating background blocking is necessary. Simply incubate cells in buffer solution containing 5% normal serum from the host species of the labeled secondary antibody.<\/p>\n<p>To prevent endocytosis (called capping) and the regeneration of Fc receptors on living cells, incubate cells at 4\u00b0C in buffer containing 5% normal serum and sodium azide added to inhibit metabolism.<\/p>\n<div class=\"btn-container\"><a class=\"btn-sq\" href=\"\/secondary-antibody-resource\/technical-tips\/controls-diluents-blocking\/\"><i class=\"fa-solid fa-graduation-cap\"><\/i>Learn more about how to avoid background<\/a><\/div>\n<h4>Fab Fragment antibodies<\/h4>\n<p>As we learned above, a Fab fragment antibody is a single binding arm of the whole immunoglobulin molecule. Fab fragments are also generated with limited proteolysis, but the enzyme used is papain. Digestion of whole IgG antibodies with papain removes the entire Fc domain, including the hinge region (Figure 1). Consequently, Fab fragment antibodies are monovalent, with a molecular weight of about 50 kDa.<\/p>\n<p>Fab fragments can be very useful tools in addition to standard primary and secondary antibodies. One use is to block endogenous immunoglobulins on cells, tissues, or other surfaces in which the primary antibody is the same species as the tissue. Blocking with Fab fragments helps prevent non-specific signals and promotes the specific detection of the primary antibody by the secondary antibody. In multiple labeling experiments, Fab fragments can facilitate the success of experiments using two primary antibodies generated in the same host species.<\/p>\n<div class=\"btn-container\"><a class=\"btn-sq\" href=\"\/technical\/products\/groups\/fab\"><i class=\"fa-duotone fa-book-open-reader\"><\/i>Read more about Fab fragment secondary antibodies.<\/a><\/div>\n<h5>FabuLight\u2122<\/h5>\n<p>FabuLight\u2122 antibodies are Fab fragment antibodies specific to the Fc region of IgG or IgM primary antibodies available conjugated to a range of reporter molecules. FabuLight antibodies enable primary antibodies to be labeled before incubation with cells or tissue. This avoids the active site of the primary antibody being compromised and can make the protocol more efficient by removing an incubation and wash step. FabuLights are ideal for flow cytometry experiments where it is desirable to avoid Fc receptor binding. The Fc domain is absent from the FabuLight, enabling labeling of cell surface immunoglobulins without risk of stimulation\/activation of cells.<\/p>\n<div class=\"btn-container\"><a class=\"btn-sq\" href=\"\/technical\/products\/groups\/fab\/fabulight\"><i class=\"fa-duotone fa-book-open-reader\"><\/i>Read more about FabuLight\u2122<\/a><\/div>\n<h4>Camelid antibodies and VHH antibodies (NANOBODIES\u00ae)<\/h4>\n<p>Camelid species such as Alpacas and Llamas produce a unique class of antibodies composed only of heavy chains (Figure 2b). Light chains are absent from IgG2 and 3 antibodies of camelid species. The immunological function of these unconventional-format antibodies is still being investigated. A consequence of the lack of light chains is that the antigen-binding fragments (Fab), also termed Variable heavy-chain-only fragment antibodies (VHH Fragments), or NANOBODIES\u00ae (Figure 2a), have some tractable characteristics for life science applications.<\/p>\n<p>One of the advantages of the absence of the light chain is that VHH fragments are very small. Another happy accident is that they are extremely stable as both a cleaved native protein and as a recombinant construct. So easily produced recombinantly, the VHH format antibody is fast becoming a popular framework for therapeutic mAbs and ADC (antibody-drug conjugates). As a primary or secondary antibody, the VHH antibodies are an exciting, novel antibody format with outstanding specificity and penetration, and offer a fantastic solution for high-quality and high-resolution imaging.<\/p>\n<figure><img decoding=\"async\" loading=\"lazy\" width=\"1024\" height=\"397\" class=\"aligncenter wp-image-11190 size-large\" style=\"width: 95%; margin: 1rem auto 0;\" src=\"\/secondary-antibody-resource\/wp-content\/uploads\/Artwork86-copy-vhh-cartoon-1024x397.jpg\" alt=\"\" srcset=\"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/Artwork86-copy-vhh-cartoon-1024x397.jpg 1024w, https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/Artwork86-copy-vhh-cartoon-300x116.jpg 300w, https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/Artwork86-copy-vhh-cartoon-1536x595.jpg 1536w, https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/Artwork86-copy-vhh-cartoon-2048x793.jpg 2048w\" sizes=\"(max-width: 1024px) 100vw, 1024px\" \/><figcaption><strong>Figure 2:<\/strong> Comparison of conventional IgG with VHH alongside canonical Immunoglobulins. Camelids such as Alpacas make heavy chain-only IgGs. The antigen-binding domain (Fab fragment) of IgG2 and 3 do not contain the heavy chain\u2019s CH1 domain, and the light chains are also absent. These heavy-chain-only Fab fragments are called VHH fragments or NANOBODIES\u00ae.<\/figcaption><\/figure>\n<div class=\"btn-container\"><a class=\"btn-sq\" href=\"\/technical\/products\/VHH-Discovery\"><i class=\"fa-solid fa-graduation-cap\"><\/i>Learn more about VHH antibodies<\/a><\/div>\n<h5>AffiniPure-VHH\u00ae Secondary Antibodies<\/h5>\n<p>Jackson ImmunoResearch AffiniPure-VHH\u00ae Secondary Antibodies are polyclonal VHH Fragment antibodies (NANOBODIES\u00ae) produced in Alpacas. They are available with specificity to Human, Rabbit or Mouse, and are cross-adsorbed against other commonly used species. They are 10x smaller than conventional whole IgG antibodies, and are available conjugated to reporter enzymes and a range of fluorescent dyes, including Alexa Fluor\u00ae. They provide scope for high-resolution Immunohistochemistry and Immunofluorescence by reducing linkage error between the target antigen and signal-producing dye.<\/p>\n<div class=\"btn-container\"><a class=\"btn-sq\" href=\"\/technical\/products\/AffiniPure-VHH-secondary-antibodies\"><i class=\"fa-solid fa-graduation-cap\"><\/i>Learn more about AffiniPure-VHH\u00ae Secondaries<\/a><\/div>\n<p><a href=\"\/technical\/products\/groups\/anti-gfp\"><img decoding=\"async\" loading=\"lazy\" width=\"729\" height=\"91\" class=\"aligncenter wp-image-11094 size-full\" style=\"width: 100%;\" src=\"\/secondary-antibody-resource\/wp-content\/uploads\/24-Q2-GFP-Ads-728x90-B.jpg\" alt=\"\" srcset=\"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/24-Q2-GFP-Ads-728x90-B.jpg 729w, https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-content\/uploads\/24-Q2-GFP-Ads-728x90-B-300x37.jpg 300w\" sizes=\"(max-width: 729px) 100vw, 729px\" \/><\/a><\/p>\n<h4>References<\/h4>\n<ol>\n<li>Shimomura O, Johnson FH, Saiga Y. Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. <em>J Cell Comp Physiol.<\/em> 1962;59:223-239. doi:10.1002\/jcp.1030590302 <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/13911999\/\">https:\/\/pubmed.ncbi.nlm.nih.gov\/13911999\/<\/a><\/li>\n<li>Heim R, Cubitt AB, Tsien RY. Improved green fluorescence. <em>Nature<\/em>. 1995;373(6516):663-664. doi:10.1038\/373663b0 <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/7854443\/\">https:\/\/pubmed.ncbi.nlm.nih.gov\/7854443\/<\/a><\/li>\n<li>Heim R, Prasher DC, Tsien RY. Wavelength mutations and posttranslational autoxidation of green fluorescent protein. <em>Proc Natl Acad Sci USA<\/em>. 1994;91(26):12501-12504. doi:10.1073\/pnas.91.26.12501 <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/7809066\/\">https:\/\/pubmed.ncbi.nlm.nih.gov\/7809066\/<\/a><\/li>\n<li>Cormack BP, Valdivia RH, Falkow S. FACS-optimized mutants of the green fluorescent protein (GFP). <em>Gene<\/em>. 1996;173(1 Spec No):33-38. doi:10.1016\/0378-1119(95)00685-0 <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/8707053\/\">https:\/\/pubmed.ncbi.nlm.nih.gov\/8707053\/<\/a><\/li>\n<li>Romei MG, Boxer SG. Split Green Fluorescent Proteins: Scope, Limitations, and Outlook. <em>Annu Rev Biophys<\/em>. 2019;48:19-44. doi:10.1146\/annurev-biophys-051013-022846 <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/30786230\/\">https:\/\/pubmed.ncbi.nlm.nih.gov\/30786230\/<\/a><\/li>\n<li>Kodama Y, Hu CD. Bimolecular fluorescence complementation (BiFC): a 5-year update and future perspectives. <em>Biotechniques<\/em>. 2012;53(5):285-298. doi:10.2144\/000113943 <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/23148879\/\">https:\/\/pubmed.ncbi.nlm.nih.gov\/23148879\/<\/a><\/li>\n<li>Ghosh I, Hamilton AD, Regan L. Antiparallel Leucine Zipper-Directed Protein Reassembly: Application to the Green Fluorescent Protein. <em>J Am Chem Soc. <\/em>2000;122:5658-5659. DOI:10.1021\/JA994421W <a href=\"https:\/\/www.semanticscholar.org\/paper\/Antiparallel-Leucine-Zipper-Directed-Protein-to-the-Ghosh-Hamilton\/84e65b5eb57f93deadee8983bd67315c1a980561\">https:\/\/www.semanticscholar.org\/paper\/Antiparallel-Leucine-Zipper-Directed-Protein-to-the-Ghosh-Hamilton\/84e65b5eb57f93deadee8983bd67315c1a980561<\/a><\/li>\n<li>Cabantous S, Nguyen HB, Pedelacq JD, <em>et al<\/em>. A new protein-protein interaction sensor based on tripartite split-GFP association. <em>Sci Rep<\/em>. 2013;3:2854. doi:10.1038\/srep02854 <a href=\"https:\/\/pubmed.ncbi.nlm.nih.gov\/24092409\/\">https:\/\/pubmed.ncbi.nlm.nih.gov\/24092409\/<\/a><\/li>\n<li>Pham, TD, Poletti, C, Tientcheu, TMN <em>et al<\/em>. FAST, a method based on split-GFP for the detection in solution of proteins synthesized in cell-free expression systems. <em>Sci Rep. <\/em>2024;14:8042. <a href=\"https:\/\/doi.org\/10.1038\/s41598-024-58588-5\">https:\/\/doi.org\/10.1038\/s41598-024-58588-5<\/a><\/li>\n<\/ol>\n<\/div>\n<table class=\"table blogLinks\">\n<thead>\n<tr>\n<th class=\"span6\">Learn more:<\/th>\n<th class=\"span6\">Do more:<\/th>\n<\/tr>\n<\/thead>\n<tbody>\n<tr>\n<td class=\"span6\"><a href=\"\/secondary-antibody-resource\/immuno-techniques\/directandindirectwesternblotting\/\">Indirect and direct Western blotting<\/a><\/td>\n<td class=\"span6\"><a href=\"https:\/\/jacksonimmuno.com\/home\/exhibitions\">Exhibition Schedule<\/a><\/td>\n<\/tr>\n<tr>\n<td class=\"span6\"><a href=\"\/secondary-antibody-resource\/immuno-techniques\/chemiluminescent-western-blotting\/\">Chemiluminescence western blotting<\/a><\/td>\n<td class=\"span6\"><a href=\"\/secondary-antibody-resource\/immuno-techniques\/western-blotting-guide\/\">Western blotting guide<\/a><\/td>\n<\/tr>\n<tr>\n<td class=\"span6\"><a class=\"row-title\" href=\"\/secondary-antibody-resource\/technical-tips\/expansionmicroscopy\/\">An Introduction to Expansion Microscopy<\/a><\/td>\n<td class=\"span6\"><a href=\"\/secondary-antibody-resource\/immuno-techniques\/elisa-guide\/\">ELISA guide<\/a><\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n<!-- AddThis Advanced Settings generic via filter on the_content --><!-- AddThis Share Buttons generic via filter on the_content --><!-- AddThis Related Posts generic via filter on the_content -->","protected":false},"excerpt":{"rendered":"<p>Download PDF Here, we discuss the differences between the different antibody formats available, including H+L, F(ab\u2032)2, Fab, and VHH fragment antibodies. We will address how they can offer solutions to your experimental setup, help you improve specificity and resolution, and circumvent limitations. Antibody Formats &#8211; not just the heavy and light chain Jackson ImmunoResearch offers [&hellip;]<!-- AddThis Advanced Settings generic via filter on get_the_excerpt --><!-- AddThis Share Buttons generic via filter on get_the_excerpt --><!-- AddThis Related Posts generic via filter on get_the_excerpt --><\/p>\n","protected":false},"author":3,"featured_media":11033,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"content-type":""},"categories":[3,16],"tags":[],"acf":[],"_links":{"self":[{"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/posts\/11189"}],"collection":[{"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/posts"}],"about":[{"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/types\/post"}],"author":[{"embeddable":true,"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/users\/3"}],"replies":[{"embeddable":true,"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/comments?post=11189"}],"version-history":[{"count":11,"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/posts\/11189\/revisions"}],"predecessor-version":[{"id":11504,"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/posts\/11189\/revisions\/11504"}],"wp:featuredmedia":[{"embeddable":true,"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/media\/11033"}],"wp:attachment":[{"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/media?parent=11189"}],"wp:term":[{"taxonomy":"category","embeddable":true,"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/categories?post=11189"},{"taxonomy":"post_tag","embeddable":true,"href":"https:\/\/www.jacksonimmuno.com\/secondary-antibody-resource\/wp-json\/wp\/v2\/tags?post=11189"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}