Fab fragments

Manufactured by Jackson ImmunoResearch

Sourced in United States

Fab fragments are a type of antibody fragment consisting of the antigen-binding region of an antibody. They are produced by enzymatic cleavage of the full-length antibody molecule. Fab fragments retain the specific antigen-binding capability of the original antibody.

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Lab products found in correlation

Alexa fluor 488, by Thermo Fisher Scientific (3 mentions) Alexa fluor 555, by Thermo Fisher Scientific (2 mentions) Anti strep tag, by Merck Group (1 mentions) Dylight 594, by Jackson ImmunoResearch (1 mentions) Giantin, by Abcam (1 mentions) Anti tgn46, by Abcam (1 mentions) Gm130, by Abcam (1 mentions) Dylight 488, by Jackson ImmunoResearch (1 mentions) Calnexin, by Abcam (1 mentions) Horseradish peroxidase, by Jackson ImmunoResearch (1 mentions) Axioobserver z1, by Thermo Fisher Scientific (1 mentions) 4 6 diamidino 2 phenylindole (dapi), by Thermo Fisher Scientific (1 mentions) Zen 3.5 blue edition software, by Zeiss (1 mentions) Fluoromount g, by Southern Biotech (1 mentions)

Close spelling variants of this product

AffiniPure Fab Fragment Goat Anti-Mouse IgG (H+L) (16 citations) Donkey Fab fragments (6 citations) Goat-anti mouse Fab fragment (6 citations) FAB fragment anti-mouse IgG (5 citations) AffiniPure Fab fragment (5 citations) Fab fragments of anti-Fcγ antibody (4 citations) AffiniPure Fab Fragment Goat Anti-Mouse IgG (4 citations) Fab Fragment Goat Anti-Mouse IgG (4 citations) Fab fragment goat anti-mouse IgG (H+L) (3 citations) Anti-mouse Fab fragments (2 citations)

6 protocols using fab fragments

Antibody Immunostaining of SARS-CoV-2 Proteins

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Anti-SARS-CoV-2 Spike antibody, anti-nucleocapsid antibody, and anti-nucleoprotein antibody were from ProSci, Inc. (Poway, CA, USA). Anti-SARS-CoV-2 anti-Membrane (M) glycoprotein antibody was a custom synthesized rabbit polyclonal antibody to the peptide: KLNDTHSSSSDNIALLVQ (Thermo Fisher Scientific/Invitrogen, Waltham, MA, USA). Anti-TGN46, giantin, GM130, and calnexin were from Abcam (Cambridge, UK). Anti-TGN46 from Thermo Fisher Scientific/Invitrogen, Waltham, MA, USA was used in some experiments. Anti-Strep tag was from Sigma. Monoclonal antibody SCICONS J2 to dsRNA was from English and Scientific Consulting, Kft, Hungary. Secondary antibodies, anti-mouse Ig or anti-rabbit Ig, were Fab’-fragments conjugated to DyLight₄₈₈ or DyLight₅₉₄ or horseradish peroxidase (Jackson ImmunoResearch, West Grove, PA, USA). All primary antibodies and fluorescent secondary antibodies were used at a dilution of 1:200. Anti-horseradish peroxidase secondary antibody was used at 1:100.
Helix pomatia agglutinin (HPA) lectin conjugated to AlexaFluor 488 was from Invitrogen and used at a final concentration of 5 μg/mL. Vital staining with C6-NBD-ceramide (Thermo Fisher Scientific/ Invitrogen, Waltham, MA, USA) was performed as previously described [15 (link)].

Hackstadt T., Chiramel A.I., Hoyt F.H., Williamson B.N., Dooley C.A., Beare P.A., de Wit E., Best S.M, & Fischer E.R. (2021). Disruption of the Golgi Apparatus and Contribution of the Endoplasmic Reticulum to the SARS-CoV-2 Replication Complex. Viruses, 13(9), 1798.

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Iterative Immunostaining of SHIELD Tissue

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SHIELD-processed coronal slices obtained from H-line mice at 100 μm thickness were stained with primary antibodies (5 μg/antibody) pre-incubated with dye-conjugated Fab fragments (3:1 molar ratio between the Fab fragment and the primary antibody, Jackson Immunoresearch) for 12 hr at 4°C in 1X PBST. Following imaging, the slices were incubated in the destaining buffer (7 mM SDS, 0.5 M Tris-HCl, 1% (w/v) 2-mercaptoethanol, pH 6.8) for 18 hr at 37°C to remove bound antibodies. Subsequent rounds of immunostaining were performed similarly.

Park Y.G., Sohn C.H., Chen R., McCue M., Yun D.H., Drummond G.T., Ku T., Evans N.B., Oak H.C., Trieu W., Choi H., Jin X., Lilascharoen V., Wang J., Truttmann M.C., Qi H.W., Ploegh H.L., Golub T.R., Chen S.C., Frosch M.P., Kulik H.J., Lim B.K, & Chung K. (2018). Simultaneous protection of tissue physicochemical properties using polyfunctional crosslinkers. Nature biotechnology.

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Iterative Immunostaining of SHIELD Tissue

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Immunofluorescence Staining of GBM Tissues

Cited 2 times

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Cryostat sections of GBM tissues and glass cover slips of differentially treated cells were prepared as described previously [19 (link), 32 (link)]. Cells were incubated overnight with the primary antibodies at 4 °C, followed by the secondary antibodies for 1 h at 37 °C. The nuclei were counterstained with 4′,6-diamidino-2-phenylindole, and the embedded slides were analyzed using light and fluorescence microscopy (AxioObserver.Z1; Carl Zeiss) with equal exposure times in relation to controls using the ZEN2 software. Used primary antibodies are listed in Supplementary Table 4. If primary antibodies were derived from the same species, non-specific binding was blocked by F(ab) fragments derived from that species (1:1000, from Jackson ImmunoResearch, West Grove, PA, USA). Primary antibodies were omitted for negative controls. For secondary antibody controls, IgG mouse (MAB002; R&D Systems, Minneapolis, MN, USA) or IgG rabbit (AB-105-C; R&D Systems) control antibodies were used at the same concentrations as the replaced primary antibodies. Donkey anti-mouse or anti-rabbit IgGs labeled with Alexa Fluor 488 or Alexa Fluor 555 (1:1,000; Thermo Fisher Scientific) served as secondary antibodies.

Adamski V., Hattermann K., Kubelt C., Cohrs G., Lucius R., Synowitz M., Sebens S, & Held-Feindt J. (2020). Entry and exit of chemotherapeutically-promoted cellular dormancy in glioblastoma cells is differentially affected by the chemokines CXCL12, CXCL16, and CX3CL1. Oncogene, 39(22), 4421-4435.

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Immunofluorescence Staining of GBM Tissues

Cited 1 time

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Cryostat sections of GBM ex vivo tissues were prepared as previously described [3 (link)]. Cells were incubated overnight with the primary antibodies at 4 °C, followed by the secondary antibodies for 1 h at 37 °C. The nuclei were counterstained with 4′,6-diamidino-2-phenylindole (Thermo Fisher Scientific; 1:30,000, 30 min, room temperature) and the embedded slides were analyzed by fluorescence microscopy (AxioObserver.Z1; Carl Zeiss AG, Oberkochen, Germany) using the ZEN 3.5 (blue edition) software (Carl Zeiss AG). Used primary antibodies are listed in Supplementary Table S2. If primary antibodies were derived from the same species, non-specific binding was blocked by F(ab) fragments derived from that species (1:1000, from Jackson ImmunoResearch, West Grove, PA, USA). Primary antibodies were omitted for negative controls. Donkey anti-mouse or anti-rabbit IgGs labeled with Alexa Fluor 488 or Alexa Fluor 555 (1:1000; Thermo Fisher Scientific) served as secondary antibodies.

Kubelt C., Hellmold D., Esser D., Ahmeti H., Synowitz M, & Held-Feindt J. (2023). Insights into Gene Regulation under Temozolomide-Promoted Cellular Dormancy and Its Connection to Stemness in Human Glioblastoma. Cells, 12(11), 1491.

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Immunohistochemistry of Neurotransmitter Receptors

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Once the brainstem was sliced into roughly 10–20 sections/animal, free-floating slices were blocked in antibody media (AB media: 0.1 M phosphate buffer (PB: 50 mM KH₂PO₄, 150 mM Na₂HPO₄), 150 mM NaCL, 3 mM Triton-X, 1% bovine serum albumin (BSA)) and 5% NGS for one hour. In some animals Fab fragments (Jackson Immunoresearch, Westgrove, PA) were used in this step to increase the specificity of mouse on mouse primary antibody. However, there was no difference seen between sections within genotype containing Fab fragments versus those without and therefore Fab fragment use was discontinued. Following blocking, slices were incubated with primary antibody for GAD67, GlyT2, and VGLUT2 (Table 1, antibody characterization below) diluted in AB media and 1% NGS overnight at 4°C. Slices were then washed (3 × 10 min) in PBS followed by secondary antibody (Table 2, Thermo-Fisher, Waltham, MA) diluted in AB media and 1% NGS incubated for 1 hour at room temperature. Slices were then washed in PB and mounted on glass slides using Fluoromount-G (SouthernBiotech, Cat.-No.: 0100-01, Birmingham, AL) and coverslipped.

McCullagh E.A., Salcedo E., Huntsman M.M, & Klug A. (2017). Tonotopic alterations in inhibitory input to the medial nucleus of the trapezoid body in a mouse model of Fragile X syndrome. The Journal of comparative neurology, 525(16), 3543-3562.

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