文献支持Anti-HA Tag Antibody [HA.C5] - Identical to Abcam (ab18181) and Thermo (MA5-27543) (A85278)

免疫原 ：YPYDVPDYA (HA) synthetic peptide conjugated to KLH.

亚型 ：IgG3

保存条件 ：Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.

克隆性 ：Monoclonal

标记物 ：Unconjugated

宿主 ：Mouse

应用范围 ：Dot, ELISA, IP, IS, WB

靶点 ：HA Tag

抗体英文名 ：Anti-HA Tag Antibody [HA.C5] - Identical to Abcam (ab18181) and Thermo (MA5-27543) (A85278)

抗体名 ：HA.C5

规格 ：100µg/200µg

Mouse monoclonal (HA.C5) antibody to HA Tag for Dot, ELISA, IP, IS and WB.

Figure 1: Western Blot - Anti-HA Tag Antibody [HA.C5] (A85278)
1:1000 (1µg/mL) Ab dilution probed against HEK293 cells transfected with HA-tagged protein vector; untransfected (1) and transfected (2).

Citations:
[1]

Construction and representative in vitro expression of BoNT/Hc/A, BoNT/Hc/B, and BoNT/Hc/EDNA vaccine constructs. (A) Schematic of BoNT/Hc/A, B, or E genes cloned into the pVAX1 mammalian expression vector. The CMV promoter, BoNT Hc gene(s), BGH poly A signal, kanamycin resistance gene, and pUC origin are shown. (B) Representative in vitro expression of the hemagglutinin-tagged BoNT Hc plasmids. Expression was confirmed using transfected RD cells and a HA-tagged antibody. An empty vector (pVAX) was used as a negative control. Results were analyzed with confocal imaging. Scale bar = 100 μm.

[2]

The impaired invasion of Salmonella Paratyphi A at fever temperature occurs in a type III secretion system 1–independent manner. A, The ratio between the expression of the Salmonella pathogenicity island (SPI) 1 genes hilD, hilC, hilA, invF, invA, spaO, prgJ, sipB and sopB in S. Paratyphi A and Salmonella Typhimurium at 42°C was determined by quantitative reverse-transcription polymerase chain reaction (qRT-PCR). Total RNA was harvested from S. Paratyphi A 45157 and S. Typhimurium SL1344 cultures grown in Lennox Luria-Bertani broth to the late logarithmic phase and gene expression was normalized using the housekeeping gene rpoD. Values represent the mean and standard error of the mean (SEM) for 3 independent qRT-PCR analyses based on 3 independent RNA extractions. B, Western blot analysis of bacterial cell lysate from S. Typhimurium and S. Paratyphi A expressing SipB-2HA, SopB-2HA, and PrgJ-2HA. Protein fractions were probed using anti–hemagglutinin antibody and anti-DnaK as a control. C, D, S. Typhimurium SL1344 and its hilA, invA, and invG null mutant strains were grown at 37°C (C) or 42°C (D) and used to infect Caco-2 cells (multiplicity of infection, 20:1), using the gentamicin protection assay. *P < .05; ^†P < .001. E, F, S. Paratyphi A 45157 and its hilA, invA, and invG null mutant strains were grown at 37°C (E) or 42°C (F). The invasion of SPI-1 mutants in panels C–F is shown relative to the wild-type (WT) parental strain. Values represent the mean and SEM for ≥3 independent infections in 1 of 3 representative experiments. Analysis of variance with Dunnett multiple-comparison test was used to determine differences between data sets; Abbreviation: NS, not significant.

The flagella-chemotaxis regulon in Salmonella Paratyphi A is down-regulated at fever temperature. A, Total RNA was harvested from Salmonella Typhimurium SL1344 and S. Paratyphi A 45157 cultures grown at 37°C and 42°C to the late logarithmic phase and was subjected to quantitative reverse-transcription polymerase chain reaction (qRT-PCR). The fold change in the abundance of the transcripts (normalized to rpoD) in S. Typhimurium (open bars) or S. Paratyphi A (gray bars) grown at 42°C relative to their expression at 37°C is shown. Values represent mean and standard error of the mean (SEM) for 3 independent qRT-PCR experiments. B, Abundance of flhD, fliZ, flgM, cheA, and fliC transcript in S. Typhimurium SL1344 (open bars) or in S. Paratyphi A 45 157 (gray bars), grown at 42°C relative to 37°C. The qRT-PCR results show the mean and the SEM for 3 independent experiments. C, Western blot analysis of bacterial cell lysate from S. Typhimurium and S. Paratyphi A expressing FliC-2HA grown at 37°C or 42°C. Protein fractions were probed using anti-hemagglutinin antibody and anti-DnaK as a control.