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Annexin a1

Manufactured by Abcam
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Annexin A1 is a calcium-dependent phospholipid-binding protein that plays a role in the regulation of cellular processes. It is involved in the anti-inflammatory response, apoptosis, and membrane organization.

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Lab products found in correlation

Peroxidase conjugated secondary antibody, by Agilent Technologies (2 mentions) α tubulin, by Abcam (2 mentions) Raised against human s100a11, by Proteintech (2 mentions) Annexin a2, by BD (2 mentions) Alexa fluor 488 and alexa fluor 546 594 coupled secondary antibodies, by Thermo Fisher Scientific (2 mentions) Rfp trap agarose beads, by Proteintech (2 mentions) Turbo gfp antibody, by OriGene (2 mentions) β actin, by Merck Group (2 mentions) Glial fibrillary acidic protein (gfap), by Abcam (1 mentions) Dxm1200, by Nikon (1 mentions) Granzyme b, by Mabtech (1 mentions) Lcn 2, by Merck Group (1 mentions) Ecl plex goat anti mouse cy5, by GE Healthcare (1 mentions) Anti rab7, by Cell Signaling Technology (1 mentions) Alexafluor donkey anti goat 488, by Thermo Fisher Scientific (1 mentions) Donkey anti rabbit 647, by Thermo Fisher Scientific (1 mentions) Anti gfp, by Abcam (1 mentions)

Close spelling variants of this product

Human Annexin A1 ELISA Kit Anti-annexin A1 α–annexin A1

6 protocols using annexin a1

1

Immunohistochemical Localization of Vulvodynia Proteins

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Immunohistochemistry was performed on multiple samples from vulvodynia and control subjects to determine tissue localization within the vestibule of selected proteins that distinguished vulvodynia patients from controls and as a validation for proteomic results. Paraffin-embedded tissues from vulvodynia patients who had undergone vestibulectomy and control subjects from a previous study were sectioned (4 μm), deparaffinized, rehydrated, and processed by low-temperature antigen retrieval as previously described.14 (link) Sections were blocked with normal horse serum and immunoreacted overnight at room temperature with the primary antibody for annexin A1 (Abcam), S100 A9 (Abcam), and glial fibrillary acidic protein (Abcam) at dilutions from 1:500 to 1:2000. The signals were amplified with Vector Immpress-AP horse antirabbit IgG Polymer Detection Kit and Vector Red used as the chromogen. Control sections were incubated with only the secondary antibody. Images were recorded using a Nikon DXM 1200 digital camera under Nomarski optics and using Nikon ACT1, version 2, software.
MacNeill C., Umstead T., Shearer D., Weisz J., Phelps D.S, & Floros J. (2022). A Pilot Proteomic Study of Vestibular Fluid From Patients With Vulvodynia. Journal of Lower Genital Tract Disease, 26(2), 169-175.
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2

Immunological Analysis of Protein Interactions

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Proteins were separated by SDS-PAGE and transferred to nitrocellulose membranes. Primary antibodies raised against human S100A11 (1:1000 dilution) (ProteinTech Group), Annexin A1 (1:1000 dilution) (Abcam), Annexin A2 (1:1000 dilution) (BD Transduction Laboratories), heat shock cognate 70 kDa protein (1:6000 dilution) (Hsc70; N69, kindly provided by Boris Margulis, Russian Academy of Sciences, St. Petersburg, Russia), α-tubulin (1:5000) (Abcam) and ErbB2 (1:1000) (Fischer Thermo Scientific, MA) was used. This was followed by appropriate peroxidase-conjugated secondary antibodies (DAKO). Immunocytochemistry: cells on coverslips were fixed in paraformaldehyde and stained with indicated primary antibodies (1:300 dilution) including S100A11 and β-actin (Sigma). Samples were incubated with the appropriate Alexa Fluor-488– and Alexa- Fluor-546/594-coupled secondary antibodies (1:1000 dilution) (Molecular Probes) and images taken by confocal microscopy. Immunoprecipitation (IP) was performed on lysates from HeLa or MCF7-ErbB2 cells overexpressing ANXA2-RFP and S100A11-GFP (wild type or mutants) or only S100A11-turbo-GFP. Immuno complexes were captured with RFP-Trap agarose beads (Chromotek) or turbo-GFP antibody (OriGene) coupled to sepharose-G beads and washed 4 times before immunoblot analysis (Extended blots showing Co-IP are presented in Supplementary Figure 4).
Jaiswal J.K., Lauritzen S.P., Scheffer L., Sakaguchi M., Bunkenborg J., Simon S.M., Kallunki T., Jäättelä M, & Nylandsted J. (2014). S100A11 is required for efficient plasma membrane repair and survival of invasive cancer cells. Nature communications, 5, 3795.
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3

Quantifying Immune Markers in Inflammatory Conditions

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The concentration of human LL-37 (Cusabio), LCN-2 (Sigma), annexin A1 (Abcam), procalcitonin (Abcam), perforin (Mabtech), granzyme B (Mabtech), and granulysin (Boster) were measured by ELISA in each patient’s sera and blister fluids or culture supernatants per the manufacturer’s instructions.
Kinoshita M., Ogawa Y., Hama N., Ujiie I., Hasegawa A., Nakajima S., Nomura T., Adachi J., Sato T., Koizumi S., Shimada S., Fujita Y., Takahashi H., Mizukawa Y., Tomonaga T., Nagao K., Abe R, & Kawamura T. (2021). Neutrophils initiate and exacerbate Stevens–Johnson syndrome and toxic epidermal necrolysis. Science translational medicine, 13(600), eaax2398.
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4

Quantifying DAMP Release in Viral Infection

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To quantify damage-associated molecular patterns (DAMPs), 4 × 105 MC38 cells seeded into six-well plates overnight were infected with JX at MOIs of 0 and 10 in 10% FBS-containing DMEM for 24 hours. Culture supernatants were harvested to measure calreticulin and HMGB1, and cell pellets were lysed to measure annexin A1. Calreticulin (Biomatik, Ontario, California, USA), HMGB1 (Biomatik, Ontario, CA), and annexin A1 (Abcam, Burlingame, California, USA) were quantified using the ELISA kit following the manufacturer’s instructions.
Lee Y.S., Lee W.S., Kim C.W., Lee S.J., Yang H., Kong S.J., Ning J., Yang K.M., Kang B., Kim W.R., Chon H.J, & Kim C. (2020). Oncolytic vaccinia virus reinvigorates peritoneal immunity and cooperates with immune checkpoint inhibitor to suppress peritoneal carcinomatosis in colon cancer. Journal for Immunotherapy of Cancer, 8(2), e000857.
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5

Antibody Characterization and Specificity

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Source of antibodies used in this study are as follows: rabbit polyclonal anti‐GFP, Annexin A1 and CD9 from Abcam (Cambridge, MA,USA); rabbit polyclonal for Nedd4‐2 generated and purified in‐house (Konstas et al., 2002 ); rat monoclonal anti‐HA (3F10) and mouse monoclonal anti‐c‐Myc (9E10) from Roche Diagnostics (Indianapolis, IN, USA); mouse monoclonal anti flag (M2) and goat polyclonal anti‐GFP from Rockland Immuno‐chemicals (Limerick, PA, USA); rabbit polyclonal anti‐Rab7 from Cell Signalling Technology (MA, USA). Secondary antibodies used for this study are as follows: donkey anti‐rabbit horseradish peroxidase and ECL Plex goat anti‐mouse Cy5 from GE Healthcare (Buckinghamshire, UK); goat anti‐mouse Alkaline Phosphatase, goat anti‐rabbit Alkaline Phosphatase and goat anti‐rat Alkaline Phosphatase from Merck Millipore (Billerica, MA, USA). Alexa‐Fluor donkey anti‐goat 488, donkey anti‐mouse 568 and donkey anti‐rabbit 647 were purchased from Thermo Fisher Scientific (Waltham, MA, USA).
Farooq A.U., Gembus K., Sandow J.J., Webb A., Mathivanan S., Manning J.A., Shah S.S., Foot N.J, & Kumar S. (2022). K‐29 linked ubiquitination of Arrdc4 regulates its function in extracellular vesicle biogenesis. Journal of Extracellular Vesicles, 11(2), e12188.
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6

Immunological Analysis of Protein Interactions

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Proteins were separated by SDS-PAGE and transferred to nitrocellulose membranes. Primary antibodies raised against human S100A11 (1:1000 dilution) (ProteinTech Group), Annexin A1 (1:1000 dilution) (Abcam), Annexin A2 (1:1000 dilution) (BD Transduction Laboratories), heat shock cognate 70 kDa protein (1:6000 dilution) (Hsc70; N69, kindly provided by Boris Margulis, Russian Academy of Sciences, St. Petersburg, Russia), α-tubulin (1:5000) (Abcam) and ErbB2 (1:1000) (Fischer Thermo Scientific, MA) was used. This was followed by appropriate peroxidase-conjugated secondary antibodies (DAKO). Immunocytochemistry: cells on coverslips were fixed in paraformaldehyde and stained with indicated primary antibodies (1:300 dilution) including S100A11 and β-actin (Sigma). Samples were incubated with the appropriate Alexa Fluor-488– and Alexa- Fluor-546/594-coupled secondary antibodies (1:1000 dilution) (Molecular Probes) and images taken by confocal microscopy. Immunoprecipitation (IP) was performed on lysates from HeLa or MCF7-ErbB2 cells overexpressing ANXA2-RFP and S100A11-GFP (wild type or mutants) or only S100A11-turbo-GFP. Immuno complexes were captured with RFP-Trap agarose beads (Chromotek) or turbo-GFP antibody (OriGene) coupled to sepharose-G beads and washed 4 times before immunoblot analysis (Extended blots showing Co-IP are presented in Supplementary Figure 4).
Jaiswal J.K., Lauritzen S.P., Scheffer L., Sakaguchi M., Bunkenborg J., Simon S.M., Kallunki T., Jäättelä M, & Nylandsted J. (2014). S100A11 is required for efficient plasma membrane repair and survival of invasive cancer cells. Nature communications, 5, 3795.
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