HEK293 human embryonic kidney cell line transfected with either (A) HA-tagged proteins (filled histogram) or (B) irrelevant transfectants (open histogram) was stained with Mouse Anti-HA Tag Alexa Fluor® ...read more
SARS-CoV-2 VLPs with N-glycan mutations display reduced viral entry.(A) Plasmids encoding for the four structural proteins containing distinct tags or EGFP reporters were either transfected alone or pooled and ...read more
SARS-CoV-2 VLPs with N-glycan mutations display reduced viral entry.(A) Plasmids encoding for the four structural proteins containing distinct tags or EGFP reporters were either transfected alone or pooled and ...read more
12 months from date of receipt, 2 to 8 °C as supplied.
Buffer
Supplied in a saline solution containing BSA and Sodium Azide.
Reconstitution Instructions
Notes
This product is provided under an agreement between Life Technologies Corporation and R&D Systems, Inc, and the manufacture, use, sale or import of this product is subject to one or more US patents and corresponding non-US equivalents, owned by Life Technologies Corporation and its affiliates. The purchase of this product conveys to the buyer the non-transferable right to use the purchased amount of the product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components (1) in manufacturing; (2) to provide a service, information, or data to an unaffiliated third party for payment; (3) for therapeutic, diagnostic or prophylactic purposes; (4) to resell, sell, or otherwise transfer this product or its components to any third party, or for any other commercial purpose. Life Technologies Corporation will not assert a claim against the buyer of the infringement of the above patents based on the manufacture, use or sale of a commercial product developed in research by the buyer in which this product or its components was employed, provided that neither this product nor any of its components was used in the manufacture of such product. For information on purchasing a license to this product for purposes other than research, contact Life Technologies Corporation, Cell Analysis Business Unit, Business Development, 29851 Willow Creek Road, Eugene, OR 97402, Tel: (541) 465-8300. Fax: (541) 335-0354.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for HA Tag Antibody (912426) [Alexa Fluor® 488]
HA Epitope Tag
HA Tag
HA
Hemagglutinin
Background
Consecutive histidine residues (usually 6 to 10 in length) are often inserted into the amino acid sequences of recombinant proteins. The resulting His-tagged proteins can be detected or purified by using anti-polyHis antibodies.
Limitations
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
Publications for HA Tag Antibody (IC6875G)(4)
We have publications tested in 4 confirmed species: Human, Chinese Hamster, Hamster, Spodoptera frugiperda.
We have publications tested in 3 applications: Bioassay, Flow Cytometry, Immunocytochemistry.
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FAQs for HA Tag Antibody (IC6875G). (Showing 1 - 1 of 1 FAQs).
We are looking for a NON-RABBIT polyclonal anti-HA (hemagglutinin - YPYDVPDYA ) antibody for immunohistochemistry that works in 4% paraformaldehyde-fixed tissue. We have a transgenic mouse expressing an HA-tagged protein and want to perform double-labeling with another antibody made in rabbit. We have had no luck using mouse or rat monoclonal anti-HA antibodies. The non-rabbit polyclonal antibody would preferably be made in goat, although if you have other species let us know. It could be unconjugated or conjugated (eg fluorochrome or HRP). However, we are only interested in a product with demonstrated effectiveness for IHC in a published paper. Do you have any such products?
We do have other host species for this target and some that have been mentioned in publications. Unfortunately for our goat antibodies against this tag none of them have been validated in IHC-P, and for two we have shown they do not work. Please see this link to our goat anti-HA Epitope Tag antibodies. Since they work in ICC/IF I would assume as long as the tag is expressed in your tissues that you should still pick it up. In this case we have an Innovators Reward Program you can take advantage of for testing a new application to save some money. Here are the chicken anti-HA Epitope Tag antibodies. None of them have been tested in IHC-P as before, or that would be indicated with a positive result and the application on the datasheet or a negative results with the (-) beside the application. Another option for you as well would be going with a Rabbit polyclonal that we have available that has been well publicized and reviewed by customers (cat# NB600-363). I know you plan on double staining, but one way around this would be to use your other antibody and incubate with the secondary for detection first. After doing that you could have this one directly conjugated to your preferred detection probe and then pick up both of their signals since you would already have bound secondary to your first rabbit primary, there would not be any non-specific binding.
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![SARS-CoV-2 VLPs with N-glycan mutations display reduced viral entry.(A) Plasmids encoding for the four structural proteins containing distinct tags or EGFP reporters were either transfected alone or pooled and transfected together into 293Ts. (B) Confocal micrographs show the intracellular colocalization of M, N, E, and Spike in perinuclear compartments that likely includes the ERGIC (arrowhead). (C) Flow cytometry analysis performed with live and “fixed-permeabilized cells” demonstrate cell surface expression of Spike and M proteins. N and E were intracellular. Here, the structural proteins were either expressed alone or altogether: “+” and “−” indicate presence/absence of indicated proteins. (D) All proteins were expressed in VLPs (detected using epitope-tag Abs), but Spike carrying N61Q and N801Q mutations displayed somewhat reduced expression. (E) Luc-VLPs containing firefly luciferase reporter were produced by cotransfecting 293T cells with plasmids encoding for N (R203M mutant), M-IRES-E, Luc-PS9, and Spike constructs. Luc-VLP viral entry into 293T/ACE2 cells was reduced upon implementing many of the N-to-Q glycosylation mutations. “No-spike” VLPs were made using all plasmids except Spike. Mock infection did not contain VLP. Data were normalized to parent-VLP luminescence in each run [both for (E) and (F)]. (F) Luc-VLP with parent-Spike, produced using 293T cells, was deglycosylated using either Endo H or peptide N-glycosidase (PNGase) F. PNGase F reduced viral entry into 293T/ACE2 and Calu-3 cells, with a smaller effect being observed for Endo H. Data are means ± SD for n ≥ 3. *P < 0.05 with respect to all other treatments and †P < 0.05 with respect to parent. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/36149962), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/ic6875g_ha-tag-alexa-fluor-488-antibody-clone-912426-western-blot-121220259231624.jpg "SARS-CoV-2 VLPs with N-glycan mutations display reduced viral entry.(A) Plasmids encoding for the four structural proteins containing distinct tags or EGFP reporters were either transfected alone or pooled and transfected together into 293Ts. (B) Confocal micrographs show the intracellular colocalization of M, N, E, and Spike in perinuclear compartments that likely includes the ERGIC (arrowhead). (C) Flow cytometry analysis performed with live and “fixed-permeabilized cells” demonstrate cell surface expression of Spike and M proteins. N and E were intracellular. Here, the structural proteins were either expressed alone or altogether: “+” and “−” indicate presence/absence of indicated proteins. (D) All proteins were expressed in VLPs (detected using epitope-tag Abs), but Spike carrying N61Q and N801Q mutations displayed somewhat reduced expression. (E) Luc-VLPs containing firefly luciferase reporter were produced by cotransfecting 293T cells with plasmids encoding for N (R203M mutant), M-IRES-E, Luc-PS9, and Spike constructs. Luc-VLP viral entry into 293T/ACE2 cells was reduced upon implementing many of the N-to-Q glycosylation mutations. “No-spike” VLPs were made using all plasmids except Spike. Mock infection did not contain VLP. Data were normalized to parent-VLP luminescence in each run [both for (E) and (F)]. (F) Luc-VLP with parent-Spike, produced using 293T cells, was deglycosylated using either Endo H or peptide N-glycosidase (PNGase) F. PNGase F reduced viral entry into 293T/ACE2 and Calu-3 cells, with a smaller effect being observed for Endo H. Data are means ± SD for n ≥ 3. *P < 0.05 with respect to all other treatments and †P < 0.05 with respect to parent. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/36149962), licensed under a CC-BY license. Not internally tested by R&D Systems.")
![SARS-CoV-2 VLPs with N-glycan mutations display reduced viral entry.(A) Plasmids encoding for the four structural proteins containing distinct tags or EGFP reporters were either transfected alone or pooled and transfected together into 293Ts. (B) Confocal micrographs show the intracellular colocalization of M, N, E, and Spike in perinuclear compartments that likely includes the ERGIC (arrowhead). (C) Flow cytometry analysis performed with live and “fixed-permeabilized cells” demonstrate cell surface expression of Spike and M proteins. N and E were intracellular. Here, the structural proteins were either expressed alone or altogether: “+” and “−” indicate presence/absence of indicated proteins. (D) All proteins were expressed in VLPs (detected using epitope-tag Abs), but Spike carrying N61Q and N801Q mutations displayed somewhat reduced expression. (E) Luc-VLPs containing firefly luciferase reporter were produced by cotransfecting 293T cells with plasmids encoding for N (R203M mutant), M-IRES-E, Luc-PS9, and Spike constructs. Luc-VLP viral entry into 293T/ACE2 cells was reduced upon implementing many of the N-to-Q glycosylation mutations. “No-spike” VLPs were made using all plasmids except Spike. Mock infection did not contain VLP. Data were normalized to parent-VLP luminescence in each run [both for (E) and (F)]. (F) Luc-VLP with parent-Spike, produced using 293T cells, was deglycosylated using either Endo H or peptide N-glycosidase (PNGase) F. PNGase F reduced viral entry into 293T/ACE2 and Calu-3 cells, with a smaller effect being observed for Endo H. Data are means ± SD for n ≥ 3. *P < 0.05 with respect to all other treatments and †P < 0.05 with respect to parent. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/36149962), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/ic6875g_ha-tag-alexa-fluor-488-antibody-clone-912426-western-blot-12122025974220.jpg "SARS-CoV-2 VLPs with N-glycan mutations display reduced viral entry.(A) Plasmids encoding for the four structural proteins containing distinct tags or EGFP reporters were either transfected alone or pooled and transfected together into 293Ts. (B) Confocal micrographs show the intracellular colocalization of M, N, E, and Spike in perinuclear compartments that likely includes the ERGIC (arrowhead). (C) Flow cytometry analysis performed with live and “fixed-permeabilized cells” demonstrate cell surface expression of Spike and M proteins. N and E were intracellular. Here, the structural proteins were either expressed alone or altogether: “+” and “−” indicate presence/absence of indicated proteins. (D) All proteins were expressed in VLPs (detected using epitope-tag Abs), but Spike carrying N61Q and N801Q mutations displayed somewhat reduced expression. (E) Luc-VLPs containing firefly luciferase reporter were produced by cotransfecting 293T cells with plasmids encoding for N (R203M mutant), M-IRES-E, Luc-PS9, and Spike constructs. Luc-VLP viral entry into 293T/ACE2 cells was reduced upon implementing many of the N-to-Q glycosylation mutations. “No-spike” VLPs were made using all plasmids except Spike. Mock infection did not contain VLP. Data were normalized to parent-VLP luminescence in each run [both for (E) and (F)]. (F) Luc-VLP with parent-Spike, produced using 293T cells, was deglycosylated using either Endo H or peptide N-glycosidase (PNGase) F. PNGase F reduced viral entry into 293T/ACE2 and Calu-3 cells, with a smaller effect being observed for Endo H. Data are means ± SD for n ≥ 3. *P < 0.05 with respect to all other treatments and †P < 0.05 with respect to parent. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/36149962), licensed under a CC-BY license. Not internally tested by R&D Systems.")