Hi All,

I sincerely appreciate all of your invaluable feedback and suggestions.

Your insights have greatly enhanced my understanding, allowing me to make a
well-informed decision regarding the selection of cells.

Thank you for your support. I will keep you all posted as I move forward
and may ask more questions.

Regards,
Anamika

On Thu, 12 Feb 2026 at 04:33, David Briggs <
[email protected]> wrote:

> Following up on Tom's comment with "*that one weird trick that
> extracellular crystallographers don't want you to know**"
>
> Let's assume you're working on a human protein.
> Make a big old sequence alignment of that protein from at least 10-20
> different mammalian species.
> Looks at conservation of the N linked glycan sequons (N-X-S/T, where
> X≠Pro).
>
> Conserved = probably needed for fold or function - keep it in.
> Not conserved = probably just decoration. Get rid of it, either N>Q or the
> most common homologue residue (if human has an N but every other species
> you look at has an S at that position, go with S).
>
> This reduces complexity, makes your life easier and in my hands generally
> gives a well-behaved protein with comparable (sometimes better) expression
> than the wild type sequence.
>
> Combine this with GntI- cells or kifunensine ± Endoglycosidase H**
> treatment and you're probably close to the minimal viable glycosylated
> protein.
> Note when using kifunensine: pre-treat your cells for 24hr ahead of
> transfection, and keep it in the media throughout your expression.
>
> HTH,
>
> Dave
>
> *caveat emptor, of course.
>
> **Pngase F is commonly used, but - is sometimes sterically blocked from
> some glycan sites, and so doesn't give efficient or complete cleavage in
> native conditions. Also remember that Pngase actually cleaves the bond
> between CG and ND2, and replaces the ND2 with an oxygen, so it turns your
> Ns into Ds.
>
> --
>
> *Dr David C. Briggs CSci MRSB **(he/him)*
>
> Principal Laboratory Research Scientist, and
>
> *Co-chair, Crick Staff Consultative forum*
>
> Signalling and Structural Biology Lab
>
> The Francis Crick Institute
>
> London, UK
>
> *Working hours Mon-Fri 0900-1700*
>
> ==
> about.me/david_briggs | OrcID <https://orcid.org/0000-0002-9793-7339> | Google
> Scholar <https://scholar.google.co.uk/citations?user=DRKG5wAAAAJ>
> ==
> "Would it not be better if one could really 'see' whether molecules...were
> just as experiments suggested?"
> – Dorothy Hodgkin
> ------------------------------
> *From:* Tom Peat <[email protected]>
> *Sent:* Thursday, February 12, 2026 8:43:46 AM
> *To:* [email protected] <[email protected]>; David Briggs <
> [email protected]>
> *Subject:* Re: [ccp4bb] Guidance Needed for Secreted Protein Expression
>
>
> *External Sender:* Use caution.
>
> Hello Anamika,
>
> To add to what others have said- if you are producing the protein for
> crystallographic work, you may want to consider the question of
> glycosylation. There are specialised strains (e.g Lec8) that reduce the
> amount of glycosylation on the protein being produced. One can also add a
> specific inhibitor (e.g. kifunensine) to the cells to limit the amount of
> glycosylation.
> Best of luck, Tom
> ------------------------------
> *From:* CCP4 bulletin board <[email protected]> on behalf of David
> Briggs <[email protected]>
> *Sent:* Thursday, February 12, 2026 7:27 PM
> *To:* [email protected] <[email protected]>
> *Subject:* Re: [ccp4bb] Guidance Needed for Secreted Protein Expression
>
> You don't often get email from
> [email protected]. Learn why this is important
> <https://aka.ms/LearnAboutSenderIdentification>
> Hi Anamika,
>
> I just want to echo much of what Kevin said:
>
> Please don't think you are locked into specific media and cell types
> offered by a particular company, or their (normally outrageously expensive)
> proprietary transfection mixes. Good old fashion PEI-based transfection can
> still allow you to crank out mgs of your favourite protein, if you think
> about things carefully.
>
> Also, we routinely use Expi293 cells in Freestyle293 media. Expi media is
> 3x the cost of Freestyle media, but we rarely see 3x the yield. So why
> bother?
>
> In addition to your choice of Signal Peptide (there are some good papers
> talking about optimisation of SP for recombinant protein production) you
> want to think about whether you want a stable cell line (good for your
> wild-type "parent" construct, but can be slow to generate initially) or
> transients (allow you to be quick on your feet and move rapidly from mutant
> construct > protein, but you'll spend more money on plasmid prep kits).
>
> When screening SPs, I normally trial the native SP (it might be there for
> a reason!) alongside favorites like BM40 and IL2.
>
> You can also use adherent HEK293s (strongly recommend expanding up to
> gas-permeable hyperflasks for the final expression run) for semi-stable
> transfection.
> Reagents and media are cheaper and you don't require a shaking CO2
> incubator, but time from construct > protein is typically 6-8 weeks, not
> days.
>
> Good luck!
>
> Dave
>
>
> --
>
> *Dr David C. Briggs CSci MRSB **(he/him)*
>
> Principal Laboratory Research Scientist (Signalling and Structural
> Biology Lab)
>
> *and Co-chair, Crick Staff Consultative Forum*
>
> The Francis Crick Institute
>
> London, UK
>
> *Working hours: Mon-Fri 0900-1700*
>
> ==
>
> about.me/david_briggs | OrcID <https://orcid.org/0000-0002-9793-7339> | Google
> Scholar  <https://scholar.google.co.uk/citations?user=DRKG5KwAAAAJ>
>
> ==
>
> "Would it not be better if one could really 'see' whether molecules...were
> just as experiments suggested?"
>
> – Dorothy Hodgkin
> ------------------------------
> *From:* CCP4 bulletin board <[email protected]> on behalf of Anamika
> Singh <[email protected]>
> *Sent:* 11 February 2026 15:07
> *To:* [email protected] <[email protected]>
> *Subject:* [ccp4bb] Guidance Needed for Secreted Protein Expression
>
>
> *External Sender:* Use caution.
>
>
> Hello Everyone,
>
> I am seeking advice on selecting the appropriate cell lines for the
> expression of a secreted protein that is over 180 kDa in size. I am
> particularly interested in conducting expression experiments using
> mammalian cells. I have come across several research papers that mention
> the use of HEK-derived cell lines, such as HEK293 GnTI-, Expi293, and
> FreeStyle 293F.
>
> I would greatly appreciate your insights on how to choose the best cell
> line to achieve a high protein expression yield, as this specific protein
> has shown suboptimal expression in other systems.
>
> Thank you for your help.
>
>
> I look forward to your response.
>
> Regards,
> --
> Anamika Singh, Ph.D.
> Research Associate
>
>
> ------------------------------
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-- 
Anamika Singh, Ph.D.
Post-Doctoral Scholar

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