Flag and ha

Manufactured by Merck Group

Sourced in United States

FLAG and HA are laboratory reagents used for protein detection and purification. FLAG is a short amino acid sequence used as an affinity tag to facilitate the identification and isolation of recombinant proteins. HA is a similar affinity tag derived from the hemagglutinin protein of the influenza virus. These reagents are commonly used in various biochemical and molecular biology applications.

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Lab products found in correlation

Bl21 de3 ripl cells, by Agilent Technologies (1 mentions) P yap, by Cell Signaling Technology (1 mentions) Calreticulin, by Abcam (1 mentions) P mob1 t35, by Cell Signaling Technology (1 mentions) Cleaved caspase 3, by Cell Signaling Technology (1 mentions) Fbxw7, by Abcam (1 mentions)

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Anti-FLAG and anti-HA antibodies (7 citations) Anti-FLAG M2 and anti-HA antibodies (3 citations) Flag (A8592) and HA (H 6908) (2 citations) Antibodies against HA and Flag (2 citations) Anti-HA and anti-Flag (2 citations)

3 protocols using flag and ha

Protein Expression and Antibody Validation

Cited 2 times

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Myc-Hpo, FLAG-Sav (Wu et al., 2003 (link)); FLAG-Cka, FLAG-Slmap, FLAG-Fgop2, FLAG-Strip, FLAG-Mob4 (Liu et al., 2016 (link)); FLAG-MST2, FLAG-MST2^D164A (Chan et al., 2005 (link)); Flag-Hpo, and GST-Mats (Ni et al., 2015 (link)) expression constructs have been described previously. HA-Slmap was made from Flag-Slmap. FLAG-PP2A-A (LD10247) and FLAG-Mts (LD26077) expression constructs were generated from cDNA clones obtained from Drosophila Genomics Resource Center. V5-SLMAP was made from the cDNA clone BC115701.1. Site-directed mutagenesis was used to generate mutants of linker autophosphorylation sites of Hpo/MST2. A flexible linker GGSG was fused to the N-terminus of Slmap FHA domain (C205-Q343) and the DNA sequence was inserted into pGEX6p-1 to produce GST-FHA proteins in BL21(DE3)-RIPL cells (Agilent).
The following antibodies were used in this study: FLAG and HA (Sigma-Aldrich); Myc (Calbiochem); V5 (Invitrogen); Hpo (Wu et al., 2003 (link)); Diap1 (Gift from B. Hay); β-galactosidase (Developmental Biology Hybridoma Bank); YAP (Novus; for immunostaining); GFP, YAP (for Western blotting), p-YAP(S127), p-YAP(S381), p-MST1/2(T181/T180; also used to detect p-Hpo), MOB1, and p-MOB1(T35) (Cell Signaling); Calreticulin (Abcam).

Zheng Y., Liu B., Wang L., Lei H., Prieto K.D, & Pan D. (2017). Homeostatic control of Hpo/MST kinase activity through autophosphorylation-dependent recruitment of the STRIPAK PP2A phosphatase complex. Cell reports, 21(12), 3612-3623.

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Drosophila Transcription Factor Constructs

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FLAG-Nerfin-1 construct was generated from cDNA clone LD18634 obtained from Drosophila Genomics Resource Center (DGRC). INSM1 expressing construct was generated from ORF clone (OHu02156) purchased from Genscript. Nerfin-1 zinc finger domain mutant constructs were generated by mutating following residues using site-directed mutagenesis: C252 and C255 were mutated to alanine in ZF1CA; C280 and C283 were mutated to alanine in ZF2CA; C336 and C339 were mutated to alanine in ZF3CA. Sd mutant constructs Y108F, D120N/E121N, L130G, Q153A and R157A were generated by site-directed mutagenesis. The following luciferase reporter constructs have been described previously: diap1 HRE-luciferase (Wu et al., 2008 (link)), 8xGTIIC-luciferase (Dupont et al., 2011 (link)), and CTGF-luciferase (Zhao et al., 2008 (link)).
Primary antibodies used in this study include the following: FLAG and HA (Sigma); Myc (Calbiochem); Diap1 (gift from Bruce Hay); Expanded and Merlin (gift from Richard Fehon); β-galactosidase and Cut (Developmental Studies Hybridoma Bank).

Guo P., Lee C.H., Lei H., Zheng Y., Pulgar Prieto K.D, & Pan D. (2019). Nerfin-1 represses transcriptional output of Hippo signaling in cell competition. eLife, 8, e38843.

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Leukemic Cell Lysis and Western Blot

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Leukemic cells were lysed in radioimmunoprecipitation (RIPA) buffer containing 50 mM Tris-HCl, 150 mM NaCl, 5 mM MgCl2, 2 mM EDTA, 1 mM NaF, 1% NP-40, and 0.1% sodium dodecyl sulfate. Western blots were performed using antibodies against FBXW7 and FBXL2 (Abcam, Cambridge, USA), Flag and HA (Sigma), cleaved caspase-3, Aurora B and USP14 (cell signaling, Beverly, MA), and β-actin (Calbiochem, Darmstadt, Germany).

Song C., Ma R., Yang X, & Pang S. (2017). The Deubiquitinating Enzyme USP14 Regulates Leukemic Chemotherapy Drugs-Induced Cell Apoptosis by Suppressing Ubiquitination of Aurora Kinase B. Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology, 42(3).

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