Talk:Antibody

Ozone

An anon deposited this in the article body:

Some immunoglobulins are known to catalyze the formation of ozone from water, presumably to kill pathogenic agents in its vicinity. The catalytic mechanism for this process is unknown.

Does anyone know if this is correct? Google gives some high-ranking results, but I wonder if this isn't too tentative to make it into an encyclopedia. The first reference I can find is from 2003 (PMID 12967665). JFW | T@lk 11:17, 27 Sep 2004 (UTC)

I would have though that would be more about the "reactive oxygen" (superoxide etc) system in endolysosomes within the actual phagocytic cells, not directly from the Ig.--KX36 16:09, 14 February 2007 (UTC)

A science magazine article (http://www.sciencemag.org/cgi/reprint/298/5601/2195.pdf) says the ozone is produced from singlet molecular oxygen (that can be produced by neutrophils) and water. Not from water alone. Narayanese 16:19, 13 May 2007 (UTC)

Difficult to Understand

Hello, as someone who has only an "average" understanding of chemistry and medicine, I found that this article was too technical. While I liked the indepth explanations, I simply could not understand the paragraphs included under "Definition", "Structure of the antibody" and "Isotypes". I hope I did not offend the author(s) of this article -- just keep it safe for the non Ph.D.s and MDs! :)

Nobody said biology was simple. However, if something is not understandable, you can ask questions (be specific) and the authors or me at least will detail it further so the article will gradually become more readable. Anyway, if someone has a clear idea how to make this article more simple while at the same time keeping it accurate and all the facts included, just feel free to do it. --Eleassar777 23:52, 23 Feb 2005 (UTC)

It is difficult to understand, more difficult than it needs to be. This is probably a function of cutting and pasting sentences from other resources like http://www.absoluteastronomy.com/encyclopedia/a/an/antibody.htm. There are also a few contradictions, for example "The monomer is composed of two heavy and two light chains" - an unusual use of the word monomer. When I have some time I'll clean this article up a bit.

You are welcome to do so and thank you for having come here. Yes, perhaps this is an unusual use of the word monomer, however it is generally used in such a context. The other thing I wish to point out is that all the resources I used were offline resources, that are stated below, and some text (from the page you give) was written before I came here.

Also, please use your signature. You create it with three tildes ~~~). Four tildes ~~~~ gives also the time and date you came here. Thanks. --Eleassar777 09:08, 24 Feb 2005 (UTC)

The immune system is a fascinating subject, but IMHO - this article is way too complicated for an encyclopedia. Also, it doesn't seem to link up with other parts of the immune system (unless it's buried and I missed it...) I remember understanding these processes backwards and forwards in college - but when I read this - I'm like, huh? Did something change in the last 3 years? I know there were some advances but this is really hard to absorb. I'd edit it myself but it's over my head at the moment. The immune system can be made much more easy to understand... like any subject. Even nuclear physics can be explained simply...and that involves math!

A summary in laymen's terms at the beginning of the article would really be welcome. Totorotroll (talk) 19:11, 20 February 2012 (UTC)

Number of antibodies

Is there information on how many different antibody molecules humans and other mammals (or even other animals) can express. I've got a text book where it says that mammals can produce 10^6 to 10^8 different antibodies. --EnSamulili 16:24, 11 May 2005 (UTC)

Not very precise, uh? VDJ recombination produces a very large number, but I would avoid "mammals can produce 10^6 to 10^8 different antibodies". I would say: "Estimates differ on the number of possible antibodies that a mammal can produce. Some maintain it is 1,000,000, while others think it may be 100 times as much". JFW | T@lk 20:01, 11 May 2005 (UTC)

Reasonable accurate figures can be calculated, and come out to about 10^16 possible antibodies in total. However the average human has about 10^12 B-cells, so this is the limit of individual antibody production. There is enough information on this to form a section on how antibodies generate diversity. I'll probably get round to this at some point --|Spaully 12:21, 1 February 2006 (UTC)

There was a proof in one of my lectures that the VDJC recombination system can form ">10^8 different hypervariable regious (CDR's)". Some clever chap has worked out that that's a bigger number than the possible number of epitopes.

Light chain has 1C, 35V, 5J; 3 different ways V and J join, 2 different light chains; makes 1050 combinations.

Heavy chain has 1C, 45V, 6J, 20D, 3 different ways V and D join, 3 different ways D and J join; makes 48600 combinations.

Now here's the dodgey bit. Making the assumption that all light chains can pair with all heavy chains, which isn't true, there's 51,030,000 combinations. Affinity maturation (somatic mutation) is estimated to roughly double this value to 10^8.

I don't know how you got values of 10^16 antibodies and 10^12 B cells.--KX36 17:06, 14 February 2007 (UTC)

Antibodies vs immunoglobulins

Are there any antibodies that are not immunoglobulins? --Eleassar777 12:41, 18 May 2005 (UTC)

Not as far as I'm aware. JFW | T@lk 20:45, 3 January 2006 (UTC)

Antibody and Immunoglobulin are synonyms, they are literally the same thing. Philmcl 11:58, July 11 2006 (EST)

According to Stedman's Medical Dictionary vol 27 (immunoglobulin), there are some pathologically-produced immunoglobulins that do not function as antibodies, but I'm not sure how significant this fact is. Drangscleaner 18:23, 17 July 2006 (UTC)

Very interesting. For reference, here's the link: 1528225, Stedman's Online Medical Dictionary at Lippincott Williams and Wilkins. And here's the key sentence: "Antibodies are Ig's, and all Ig's probably function as antibodies. However, Ig refers not only to the usual antibodies, but also to a great number of pathological proteins classified as myeloma proteins, which appear in multiple myeloma along with Bence Jones proteins, myeloma globulins, and Ig fragments." --Arcadian 18:57, 17 July 2006 (UTC)

Don't worry - all Ig's ("immunoglobulins") are antibodies and vice versa. All are produced by B-cells. --GeHa 21:42, 21 July 2006 (GMT)

Immunoglobulins are also produced by Plasma Cells (which in turn are the progeny of activated B-cells). I recently read a textbook (Basic Immunology, Abbas et al) that stated that more than half of the antibody present in the human body are produced by plasma cells. However, the experts seem to disagree on this point. Andbir (talk) 09:50, 20 May 2008 (UTC)

Ahhh, but as you say, plasma cells are still B cells that have become huge due to their large scale production of antibody - they need all the space to make and process the protein! As for the confusion over Ig's above, immunoglobulin was a name given to describe an antibody when it was first characterized many years ago (based on its biochemical properties). Other proteins can be referred to Ig-like proteins or immunoglobulin superfamily (IgSF) proteins, since the have the same structural features (Ig-domains) as antibodies (the first known Igs), but they are not true "immunoglobulins" stricto senso. These other IgSF proteins are produced by cells other than B cells. ~ Ciar ~ _{(Talk to me!)} 15:36, 20 May 2008 (UTC)

Some cancers are derived from B-cells ("myeloma"), and as these cells expand far beyond the usual for a normal B-cell (as cancers do), these may produce the one Ig that B-cell coded for in immense amounts. Normally, any individual Ig is only produced in large amounts when it has particular relevance - say, an anti-viral antibody during an active infection. However, as the continued growth of the B-cell "gone wild" is not being being driven by a productive immune response, the massive amounts of the immunoglobulin it is pouring out may or may not be binding anything known/useful. Perhaps this lead to the statement you quoted above. Antibodies reacting to self proteins are called autoantibodies and are thought to be driving certain diseases (Multiple sclerosis, rheumatoid arthritis, lupus...). These contribute to disease activity and are thus considered pathogenic/harmful. The immunoglobulins produced by the myelomas referred to here probably don't do anything harmful in their own right, but are secundary to the actual problem (i.e. cancer). Thus, they should not be considered pathological in the sense that they cause disease - they are merely symptoms of the underlying disease --GeHa 21:42, 21 July 2006 (GMT)

The immunoglobulins produced by myelomas are very harmful for the patient mainly causing serious damage to the kidneys leading to renal insufficiency in late stages. Kischel 23:07, 22 September 2007 (UTC)

"Antibody" is a functional definition, something that binds antigens. "immunoglobulin" is a structural one. It could probably be said that T-cell receptors and MHC's are antibodies and although they contain immunoglobulin domains (as do many proteins), are not themselves immunoglobulins. I would also agree that an immunoglobulin without activity on an antigen is not an antibody--KX36 17:21, 14 February 2007 (UTC)

T-cell receptors and MHC's do interact with peptides while antibodies interact with molecular structures which are considerably larger. Antibodies also belong to a different section of the immune system with its own effector mechanisms. I would therefore strongly suggest not to use the term antibody for T-cell receptors or MHC molecules. Kischel 23:07, 22 September 2007 (UTC)

It was through myeloma cells that enough monoclonal antibodies were first isolated for study.86.134.236.70 (talk) 23:28, 20 February 2009 (UTC)

IgM hexamer formation?

Does IgM ever adopt the hexemeric form under normal, non-disease process conditions? In know it can occur in some lymphomas, but thought the pentemer form was by far the most common. MarcoTolo 03:55, 4 February 2006 (UTC)

IgM can only form hexamers without a J chain. Janeway ('05) describes the formation as 'occasional'. Will edit. Tricky 15:35, 10 March 2006 (UTC)

Why "Y" shaped

Just quick question - why are antibodies "Y" shaped. From a layman's perspective, it seems to me that only one half of the Y is need for an antibody to work.

That is, it seems to me that only one receptor on one of the arms is needed to binding to the antigen.

Does two arms result in a simple doubling the number of binding sites, so as to double the number of "capture site" per molecule, or is there something more subtle to it all?

Thanks -- Quantockgoblin 17:11, 16 March 2007 (UTC)

There's two quick answers, which I'm unclear how pertinent they'd be to the article, since they're essentially teleologic.

1) Binding of bivalent immunoglobulins of multiple epitope specificities allows for the formation of immune complexes

2) Activation of Fc receptors on effector cells (B cells, macrophages, etc.) may require cross-linking Jbarin 00:42, 7 May 2007 (UTC)

-> A third comment should be added to the question: Working with single-chain antibodies – a form of antibodies modified by biotechnological means, which possess only one binding domain - one does observe a significant reduction in the strength of binding of the single-chain antibody to its antigen ias compared with the original antibody having two binding sites - This observation strongly suggests that the two binding sites are also needed to improve the strength of binding. Kischel 22:45, 22 September 2007 (UTC)

GA nomination

H'mmm, I'm thinking this article is a little bit weak on the refs. I'll try and add some in when I can....anyone else able to help push this up to standard?? Thanks, Ciar 23:46, 30 March 2007 (UTC)

I'd be happy to help out, let me know if you need anything special. First on my list will be to find some GOOD external links, hopefully to discourage some of the spamming.--DO11.10 00:00, 31 March 2007 (UTC)

As far as references go, this article is pretty good, for GA standard. III don't know how much you've done since 31 March, but it seems to be up to scratch. The only thing I am a little concerned about is the use of jargon in this article, however, as most of the jargon is blue-linked, that is OK for GA. The structure is consistent and well ordered. The lead section, while a little complex, does provide a suitable overview for the article.

As for stability, I can see there have been a lot of vandalism on this page in the past few hours, but otherwise the page is pretty stable, so I'm happy with that. Obviously, some school somewhere is using Wikipedia as a resource.

GA review (see here for criteria)

1. It is reasonably well written.

   a (prose): b (MoS):

2. It is factually accurate and verifiable.

   a (references): b (citations to reliable sources): c (OR):

3. It is broad in its coverage.

   a (major aspects): b (focused):

4. It follows the neutral point of view policy.

   a (fair representation): b (all significant views):

5. It is stable.

   

6. It contains images, where possible, to illustrate the topic.

   a (tagged and captioned): b lack of images (does not in itself exclude GA): c (non-free images have fair use rationales):

7. Overall:

   a Pass/Fail:

So, as you can see, I am happy to pass this article to GA. It contains a good amount of well-structured, reliably sourced information that would be useful to many users.

If you want to take this article further, I would recommend trying to cut down on the amount of jargon used in the article and using simpler prose, for example "similar" instead of "analogous", to make it easier to understand. Don't go overboard though. Also, the lead section could do with some restructuring, perhaps to find a more suitable place for that second paragraph.

I would strongly suggest you get a peer review of this article and try and get as many editors as you can to comment, so as you can see where to go from here, before making any major changes. Otherwise, well done! Smomo 14:44, 3 April 2007 (UTC)

For safe-keeping: papain and pepsin

Just trying to tidy up article following peer review so going to add/remove/move around stuff trying to get a good overall "big picture". Not sure the info below adds useful info to the antibody article so took it out for now...but didn't want to completely delete is....gonna pop it here for now if someone prefers it goes back in!

In an experimental setting, enzymes can be used to cleave the antibody into Fc and Fab fragments.

Enzyme	Location of cleavage	First fragment	Second fragment
papain	at hinge region	two Fab fragments	Fc fragment
pepsin	below hinge region	one F(ab')2 fragment	Fc fragment

The variable regions of the heavy and light chains can be fused together to form a single chain variable fragment (scFv), which is only half the size of the Fab fragment yet retains the original specificity of the parent immunoglobulin.

References

External link suggestion

Dear writers, I would like to suggest a link to the article on antibody generation on openwetware. The article in question is a technical description of how a biologist would go about generating a new antibody. It may be of interest to the public to see how antibodies are not just a natural phenomena but also a technique in the lab. To researchers this would be an interesting link with a lot of added information. Please consider it. Best, --Jakob Suckale (talk) 14:03, 24 April 2008 (UTC)

Antibodies vs immunoglobulins 2

In #Antibodies va immunoglobulins it was discussed whether all antibodies are immunoglobulins. What remains uncler to me, is if all multicellular species immunoglobulins as antibodies. Do all species in the kingdom Animalia use immunoglobulins and nothing else, in internal defence. Samulili (talk) 12:19, 7 August 2008 (UTC)

We commonly do not describe it as 'antibody' if it is not immunoglobulin, even though it would belong to immunoglobulin super family, have selective bindig ability or contribute to host defence. This review (Marchalonis and Schluter. Scand. J. Immunol. 1990; 32: 13–20.) may help you understand. Thanks. --Y tambe (talk) 03:00, 8 August 2008 (UTC)

At the beginning of article: Antibodies (also known as immunoglobulins[1], abbreviated Ig) are gamma globulin proteins that are found in blood or other bodily fluids of vertebrates. I thought gamma globulins were IgG only. 86.134.236.70 (talk) 23:32, 20 February 2009 (UTC)

If you check the link under gamma globulin, you will see the definition of this type of protein. All antibodies are gamma globulins. Gamma globulins belong to a large family of proteins found in the serum of blood -- this family contains other types (e.g. alpha and beta) of globulins. The gamma labeling of globulins refers to the grouping given to members of this protein family, based on their size/property differences.

IgG is a type of gamma globulin (or immunoglobulin) that contains a "gamma" type heavy chain -- the gamma in this case refers to the gene coding for the heavy chain and is not the same as the "gamma" in gamma globulins. In other words, under the long naming system, IgG could be called "gamma globulin gamma", whereas IgA could be called "gamma globulin alpha" and so on. Hope this helps! ~ Ciar ~ _{(Talk to me!)} 00:27, 21 February 2009 (UTC)

Intrabody therapy - should it be in this article?

Wandering if intrabody should be a redirect to this article - it seems an emerging term for intracellular antibody and used in the context intrabody therapy as in this following review article, amongst others. If so is intrabody therapy covered or in the scope of this article? LeeVJ (talk) 22:42, 21 September 2008 (UTC)

Messer A, McLear J (2006). "The therapeutic potential of intrabodies in neurologic disorders: focus on Huntington and Parkinson diseases". BioDrugs. 20 (6): 327–33. PMID 17176119. {{cite journal}}: |access-date= requires |url= (help)

Hi Lee, I think a sentence or two could be added about this in the disease therapy section of the antibody article, but a more detailed stand alone article could be made to cover this novel type of antibody/antibody fragment, and its applications to science and medicine, which could be linked to/from this article. With more than 100 papers about these things available on pubmed, I'm sure it would be considered notable enough!! Best, ~ Ciar ~ _{(Talk to me!)} 23:13, 21 September 2008 (UTC)

Structure prediction

I moved the section structure prediction to follow medical applications and research applications, since the content makes more sense if those sections are read first. ~ Ciar ~ _{(Talk to me!)} 23:28, 24 December 2008 (UTC)

How long until antibodies leave body?

I couldn't find the answer to this in the article, if you HIV, you have HIV antibodies, your cured of HIV, how long until HIV antibodies leave the body, if ever? (obviously it would be the same for any virus, right?) If the answer is in the article, can someone please tell me where? If not, can someone please tell me what happens in the above example, once you are cured? And the reason I want to know is because I'm researching HIV, and there seems to be no way to tell if someone is cured, regardless whether or not there is a cure, it seems while a protocol for diagnosis exists there is no protocol for determining a cure. And anyway, if the virus was no longer in someone previously infected (like in my above example) what would happen to the antibodies?Jason1170 (talk) 16:55, 11 February 2009 (UTC)

Serum antibodies will decay slowly, but the memory cells that can produce them will remain indefinitely. In the case of HIV, see PMID 16791025, which basically says that once you have the virus it is impossible (with present treatments) to totally eradicate it from the body. This reservoir problem is reviewed in PMID 11818490 Tim Vickers (talk) 17:23, 11 February 2009 (UTC)

Actually, Jason1170, you don't need that information, because you wouldn't support a claim of HIV eradication on the absence of anti-gp120 antibodies anyway. WhatamIdoing (talk) 03:39, 12 February 2009 (UTC)

You guys are crazy. Anything living can be killed, including some virus. As you likely know with HIV, the tests they use to confirm someone is positive are antibody tests. However, they say it usually takes 2-3 months for the body to produce antibodies. So, does it work vise versa? Does it take 2-3 months for the antibodies to disappear if the virus is totally killed? What would you estimate? Do you think that you should put the simple information that you gave to answer my question in the article? I don't understand how someone can say you can't be confirmed cured by antibody tests since you are officially diagnosed by testing positive for antibodies. And Tim, it doesn't matter what treatments can do, these idiots with millions can't find a cure, then they should be establishing a protocol to determine if someone is cured - like do something they're capable of. Jason1170 (talk) 16:37, 12 February 2009 (UTC)

Testing uses both antibodies and RT-PCR, which detects viral RNA. Since the virus integrates into the genome of its host cells, it becomes part of these cells - so it will remain in the body for as long as these cells and their descendants do. This is called a "viral reservoir". If you look at the first paper I linked to it contrasts HIV, which can't be cured, with hepatitis C. Treatment of HIV does not lead to loss of antibodies, while treatment of hepatitis C does remove the antibodies. This is since hepatitis is curable and AIDS is not. Tim Vickers (talk) 17:45, 12 February 2009 (UTC)

Comments on the first paragraph of the article

1. Since the isotype of antibodies is not only determined by the different heavy chains but also by the different light chains (see Isotype (immunology)) - IgG, IgA, IgM, IgE and IgD should rather be referred to as classes, this would require changes not only in the first paragraph but also in the rest of the article. For the sake of clarity this should be done though.
2. Both references for the first paragraph (references 1 and 2) concern VDJ recombination and genomic structure of immunoglobulin loci - they do not support and provide information about the structure of antibodies as described in the first paragraph. Although the information in the first paragraph is correct to my knowledge, other references need to be given to support it.
--Teddy73 15:17, 19 August 2009 (UTC)

Comment on the IgE section of the table

"Binds to allergens and triggers histamine release from mast cells and basophils, and is involved in allergy. Also protects against parasitic worms.[6]"

"Binds to allergens" mixes up cause and effect. Antigens binding to IgE trigger physiologic reactions, which in some cases cause the symptoms of an allergic disorder...

"protects against parasitic worms" remains for the time being a theory, which still remains to be proven (see: [1]). It should be marked as such.
--Teddy73 15:33, 19 August 2009 (UTC) --Teddy73 15:37, 19 August 2009 (UTC)

Antibodies are not Gammaglobulins

In the body article it states at the top in the primary definition that "antibodies are gammaglobulins". This is an absolute statement, it is incorrect. Some Ig's are gamma globulins but others fration in electrophoresis to be alpha or beta globulins. Re-read the definition of a gamma globulin and what i say will become apparent. Although i dont have a refrence for this im sure one is out there.

Hi, 114. This is a common point of confusion, and has already been addressed on this page. Take a look at this exchange from last year. – ClockworkSoul 14:21, 13 April 2010 (UTC)

Need more on the attached sugars

The Structure sections says some of the amino acids have attached sugar chains but does not give any details or explain the significance. Is it these sugars that allow the body to recognise the antibodies as foreign ? Are some of these sugars asialated (whatever that means) ?Rod57 (talk) 15:10, 15 June 2010 (UTC)

I have expertise in antibody glycosylation (sugars attached to different parts of the antibodies), and have started reviewing the page with this in mind. Hoping to start editing in a couple of weeks! Mattiascollin (talk) 08:59, 3 September 2019 (UTC)

Simplify lead

A concern has been raised here that this article is not as clear as it could be. Please note that the first paragraph in the lead needs to be kept dead simple so that anyone can understand it. Looking back to a previous version at the time it was promoted to good article status, the first paragraph is in my opinion significantly clearer. Would anyone object if I try to restore some of the language of the previous version of the lead? In addition, I suggest that some of the more detailed description concerning antibody structure that is currently in the first paragraph of the lead could be split out into a new paragraph. Boghog (talk) 11:05, 6 February 2011 (UTC)

Since no one has commented, I was bold and went ahead and edited the lead so that it now hopefully clearer. Boghog (talk) 20:39, 10 February 2011 (UTC)

I think it's an improvement. Thanks for doing that. WhatamIdoing (talk) 18:09, 15 February 2011 (UTC)

Section Antibody mimetic

In this section, I cannot parse the sentence "Nucleic acids and small molecules are sometimes considered antibody mimetics, but not artificial antibodies, antibody fragments and fusion proteins are composed from these" What does "these" refer to? Is every item listed after "not" to be regarded as being refer to by it, or is this supposed to be two sentences, with the second sentence starting with "Antibody fragments"? Having a full second sentence content attached to the first half with no clear conjunction makes the whole ambiguous. Could someone who knows what is being said, fix this? 173.180.151.49 (talk) 05:56, 22 January 2017 (UTC)

Definition and Citation of Immature/Naive B cells and Application

A few comments and clarifications:

1. A citation for the last sentence in paragraph 3 in the overview is needed, in which the article states, "The allergen-IgE-FcRε interaction mediates allergic signal transduction to induce conditions such as asthma." Induction of asthma is a complex and still not completely understood process, so I think a citation that demonstrates the connection between the antibody interaction and the pathways that lead to asthma or allergic response would be very valuable here. If the citation could also address the previous two sentences as well, that would be even better. I would suggest

2. Under the Subsection Isotypes, in the second paragraph, the article states, "Immature B cells, which have never been exposed to an antigen, express only the IgM isotype in a cell surface bound form. The B lymphocyte, in this ready-to-respond form, is known as a "naive B lymphocyte"." As it reads, it seems to imply that naive B lymphocytes are also immature B cells, which is false. While immature B cells and naive B lymphocytes have not been exposed to antigens, naive B lymphocytes are mature B lymphocytes, as they have undergone positive selection. I would recommend rewording this so that it isn't as ambiguous and difficult to understand. SamBerry (talk) 15:56, 6 April 2017 (UTC)

References

Would it make sense to have a separate article for “constant region” as this was mention in the article eight times

How about the dictionary definition as a start where experts in the field can elaborate? "Subregions of antibody molecules that are identical. They combine with variable regions to create billions of types of antibodies with unique structures.” ----Bernburgerin (talk) 09:37, 2 November 2018 (UTC)

antibodies and immunoglobulins 3

Maybe after a decade or so people are wiser now. Please note that MeSH has antibodies as a subset of IGs:

• Ig: "Multi-subunit proteins which function in IMMUNITY. They are produced by B LYMPHOCYTES from the IMMUNOGLOBULIN GENES. They are comprised of two heavy (IMMUNOGLOBULIN HEAVY CHAINS) and two light chains (IMMUNOGLOBULIN LIGHT CHAINS) with additional ancillary" Ref.: https://meshb.nlm.nih.gov/#/record/ui?ui=D007136
• Ab: "Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS)." Ref.: https://meshb.nlm.nih.gov/#/record/ui?ui=D000906

This is why we now have two different items in Wikidata. --SCIdude (talk) 17:13, 8 February 2020 (UTC)

Rewrite of first few sections

I'm working on improving the article at User:Tokenzero/Antibody (since I wanted to rearrange and rewrite quite a few parts). Changes include:

• made the lead shorter and less technical.
• rearranged the first few sections, moved "history" later.
• moved the discussion of the most common terminology (the domains and the Fab, Fc regions) as early as possible, simplifying it and clarifying some details.
• clarified what classes are (also it seems to me most modern textbooks prefer class to isotype).
• clarified the main way in which usage varies for antibody vs immunoglobulin; also explained the confusing gammaglobulin term.
• updated illustrations in Structure to make them easier to read, and using consistent colors.

So far I haven't worked on any of the later sections, starting from "Function". Please tell me if there's any change you don't like (or needs a ref). Otherwise I'll move that version to mainspace.

In the future I think it would be beneficial to split out a separate article: Applications of antibodies containing the last few sections. So they would only be discussed shortly here (some mention should be added to the lead in particular) and the last section here would be History. Thoughts? Tokenzero (talk) 17:16, 7 November 2020 (UTC)

"Binding antibody unit" listed at Redirects for discussion

An editor has identified a potential problem with the redirect Binding antibody unit and has thus listed it for discussion. This discussion will occur at Wikipedia:Redirects for discussion/Log/2022 February 14#Binding antibody unit until a consensus is reached, and readers of this page are welcome to contribute to the discussion. Pseudomonas_(talk) 16:27, 14 February 2022 (UTC)

GA Reassessment

Antibody

The following discussion is closed. Please do not modify it. Subsequent comments should be made on the appropriate discussion page. No further edits should be made to this discussion.

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Article (edit | visual edit | history) · Article talk (edit | history) · Watch • Watch article reassessment page • GAN review not found

Result: No significant improvement, even giving the extra allotted time. Delisted. ~~ AirshipJungleman29 (talk) 22:10, 2 March 2023 (UTC)

 Because of an overload of chemistry articles at GAR, if delisting, do not close before 2 March.

There's lots of uncited material including

• "In the framework of the immune network theory, CDRs are also called idiotypes. According to immune network theory, the adaptive immune system is regulated by interactions between idiotypes."
• The protein structure section
• Antibodies also form complexes by binding to antigen: this is called an antigen-antibody complex or immune complex. Small antigens can cross-link two antibodies, also leading to the formation of antibody dimers, trimers, tetramers, etc. Multivalent antigens (e.g., cells with multiple epitopes) can form larger complexes with antibodies. An extreme example is the clumping, or agglutination, of red blood cells with antibodies in the Coombs test to determine blood groups: the large clumps become insoluble, leading to visually apparent precipitation.
• Each antibody contains two identical light chains: both κ or both λ. Proportions of κ and λ types vary by species and can be used to detect abnormal proliferation of B cell clones. Other types of light chains, such as the iota (ι) chain, are found in other vertebrates like sharks (Chondrichthyes) and bony fishes (Teleostei).
• The entire Antibody–antigen interactions section.
• Being able to control the combinational design of the sequence and three-dimensional space could transcend the natural design and allow for the attachment of different combinations of drugs to the arms. Heterodimeric antibodies have a greater range in shapes they can take and the drugs that are attached to the arms don't have to be the same on each arm, allowing for different combinations of drugs to be used in cancer treatment. Pharmaceuticals are able to produce highly functional bispecific, and even multispecific, antibodies. The degree to which they can function is impressive given that such a change of shape from the natural form should lead to decreased functionality.

And more. These will all need to be cited. Onegreatjoke (talk) 21:08, 9 February 2023 (UTC)

The discussion above is closed. Please do not modify it. Subsequent comments should be made on the appropriate discussion page. No further edits should be made to this discussion.