Product Info

WB 1:3000-1:10000, IF/ICC: 1:200, IP 1:200
*The optimal dilutions should be determined by the end user.

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Monoclonal [T80]
HA-Tag Mouse Monoclonal antibody detects endogenous levels of internal, C-terminal, or N-terminal HA-tagged recombinant proteins.
Cite Format: Affinity Biosciences Cat# T0008, RRID:AB_2839415.
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl,. Store at -20 °C. Stable for 12 months from date of receipt.


ha tag



A synthetic peptide YPYDVPDYA coupled to KLH.



1). Liu T et al. The m6A reader YTHDF1 promotes ovarian cancer progression via augmenting EIF3C translation. NUCLEIC ACIDS RESEARCH 2020 Jan 30 (PubMed: 31996915) [IF=14.9]

Application: WB    Species: Human    Sample: in A2780 or SKOV3 cells

Figure 6. YTHDF1 regulates EIF3C translation in an m6A-dependent manner. (A) Relative RNA level of EIF3C in A2780 and SKOV3 upon YTHDF1 knockdown. (B) Western blot detected the protein level of EIF3C in A2780 and SKOV3 cells upon YTHDF1 knockdown. (C) Gene-specific m6A qPCR validation of m6A levels in A2780 and SKOV3 cells. Primers to m6A negative region of EEF1A as the negative control and primers to m6A postive region of EEF1A as the positive control. (D) YTHDF1 RIP followed by RT-qPCR confirmed the interaction between YTHDF1 and EIF3C mRNA. (E) Schematic representation of wild-type (YTHDF1-wt) and mutant (YTHDF1-mut) YTHDF1 constructs. (F) RIP-derived RNA and protein in A2780 cells were measured by RT-qPCR and western blot, respectively. GAPDH was used as the negative control in western blot assays. (G) Western blot confirmed HAtagged EIF3C expression in A2780 or SKOV3 cells co-transfected with empty vector, wild-type or mutant Flag-tagged YTHDF1 and wild-type or mutant HA-tagged EIF3C. (H) Nascent protein synthesis was detected by HPG incorporation upon YTHDF1 knockdown or EIF3C knockdown in A2780 cells. Scale bar, 100  m. Data are shown as means ± S.D. *P < 0.05, **P < 0.01, ***P < 0.001, NS, not significant.

2). Zou J et al. WWP2 drives the progression of gastric cancer by facilitating the ubiquitination and degradation of LATS1 protein. Cell Communication and Signaling 2023 Feb 17;21(1):38. (PubMed: 36803368) [IF=8.4]

3). Zhang H et al. Oryza sativa POSITIVE REGULATOR OF IRON DEFICIENCY RESPONSE 2 (OsPRI2) and OsPRI3 are involved in the maintenance of Fe homeostasis. PLANT CELL AND ENVIRONMENT 2020 Jan;43(1):261-274 (PubMed: 31674679) [IF=7.3]

Application: WB    Species: yeast    Sample: yeast cells

FIGURE 1| Interaction of OsHRZ1 with OsPRI2 and OsPRI3.(c) CoIP assay. Total proteins from different combinations with OsHRZ1‐GFP and HA‐OsPRI2/HA‐OsPRI3/HA‐GUS were immunoprecipitated with GFP‐Trap followed by immunoblotting with the indicated antibodies. HRZ1‐GFP/HA‐GUS, negative control. Protein molecular weight (in kDa) is indicated.

Application: WB    Species: Plant    Sample: Root

FIGURE 1 Interaction of OsHRZ1 with OsPRI2 and OsPRI3. (a) Yeast two‐hybrid assays. Yeast co‐transformed with different BD and AD plasmid combinations were spotted in parallel in 10‐fold dilution series on synthetic dropout medium lacking Leu/Trp/His/Ade. The C‐terminal truncated OsHRZ1 and full‐length OsPRI2/3 were cloned into pGBKT7 and pGADT7, respectively. OsHRZ1‐C/OsPRI1, positive control. OsHRZ1‐ C/Empty, negative control. (b) Pull‐down assay. OsHRZ1 was fused with the GST tag and OsPRI2/3 were fused with the His tag. Recombinant proteins were expressed in E. coli. Proteins were pulled down by glutathione Sepharose 4B and detected using the anti‐His antibody. Protein molecular weight (in kDa) is indicated. (c) CoIP assay. Total proteins from different combinations with OsHRZ1‐GFP and HA‐OsPRI2/HA‐OsPRI3/ HA‐GUS were immunoprecipitated with GFP‐Trap followed by immunoblotting with the indicated antibodies. HRZ1‐GFP/HA‐GUS, negative control. Protein molecular weight (in kDa) is indicated. (d) Degradation of OsPRI2 or OsPRI3 was carried out by detecting the OsPRI2/3‐GFP protein level in co‐infiltration experiments with increasing amounts of OsHRZ1‐GFP. GFP proteins were used as an internal control. Anti‐GFP antibody was used in western blot. Protein molecular weight (in kDa) is indicated. Stars indicate the non‐specific bands. Numbers indicate the ratio of the concentrations of agrobacteria used in co‐infiltration. Empty vector, a binary vector pOCA30 with a 35S promoter; GFP, 35S:GFP in pOCA30; OsPRI2‐GFP, 35S:OsPRI2‐GFP in pOCA30; OsPRI3‐GFP, 35S:OsPRI3‐GFP in pOCA30; OsHRZ1‐GFP, 35S:OsHRZ1‐GFP in pOCA30. (e) Cell‐free degradation. Ten‐day‐old roots grown in Fe‐sufficient solution were harvested and used for protein extraction. Incubation with or without MG132 was performed over the indicated time course

4). Duan et al. Mutation of Basic Residues R283, R286, and K288 in the Matrix Protein of Newcastle Disease Virus Attenuates Viral Replication and Pathogenicity. International Journal of Molecular Sciences 2023 Jan 4;24(2):980. (PubMed: 36674496) [IF=5.6]

5). Yin X et al. The Nuclear-Localized RxLR Effector PvAvh74 From Plasmopara viticola Induces Cell Death and Immunity Responses in Nicotiana benthamiana. Frontiers in Microbiology 2019 Jul 10;10:1531 (PubMed: 31354650) [IF=5.2]

6). Duan et al. Chicken bromodomain-containing protein 2 interacts with the Newcastle disease virus matrix protein and promotes viral replication. Veterinary Research 2020 Sep 22;51(1):120. (PubMed: 32962745) [IF=4.4]

Application: WB    Species: Chicken    Sample: DF-1 cells

Figure 1| Identifcation of the interaction between the NDV M protein and chBRD2 protein.B Identifcation of the interaction between the M protein and chBRD2 protein by co-IP assay. The indicated plasmids were co-transfected into DF-1 cells, and reciprocal co-IP assays were performed to identify the interaction between HA-M and Myc-chBRD2 in DF-1 cells at 36 hpt.

7). Hu Y et al. Schizosaccharomyces pombe MAP kinase Sty1 promotes survival of Δppr10 cells with defective mitochondrial protein synthesis. The international journal of biochemistry & cell biology 2022 Sep 26;152:106308. (PubMed: 36174923) [IF=4.0]

8). Chen F et al. Assessment of SENP3-interacting proteins in hepatocytes treated with diethylnitrosamine by BioID assay. ACTA BIOCHIMICA ET BIOPHYSICA SINICA 2021 Aug 31;53(9):1237-1246. (PubMed: 34312671) [IF=3.7]

Application: WB    Species: Human    Sample: LO2 cells

Figure 3. Identification and verification of SENP3-interacting proteins with SENP3–BirA (A) Silver staining of precipitations by BioID. LO2 cells were stably transfected with pCDH–SENP3–BirA (named LO2–SENP3–BirA). LO2–SENP3–BirA cells were untreated or treated with DEN. (B) A pie chart showing the number of proteins identified by MS. (C) The interaction of SENP3 with TKT, NPM1, and ATP5F1A was verified by co-IP. LO2 cells were transfected with pCDH–SENP3–BirA and treated with DEN. (D) The in vitro interaction of SENP3 with TKT was validated by GST pull-down assay. Flag-SENP3 was transfected into HEK293T cells, and SENP3 was purified from cell lysates with anti-Flag M2 gels after 24 h of transfection. GST–TKT was obtained from prokaryotic expression system. (E) The physical interaction of SENP3 with TKT or ATP5F1A was measured by FRET with acceptor photobleaching method. After treatment with DEN for 2 h, LO2 cells were fixed and stained with primary antibodies and fluorescence-conjugated secondary antibodies. Scale bar: 10 μm. The efficiency of FRET from 10 cells are shown. (F) Transient SUMOylated proteins that interact with SENP3 were evaluated. co-IP was performed in HEK293T cells transfected with HA–SENP3.

9). Sun L et al. Proteasome inhibition promotes mono-ubiquitination and nuclear translocation of mature (52 kDa) PINK1. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 2019 Sep 17;517(2):376-382 (PubMed: 31362890) [IF=3.1]

10). Li C et al. Porcine TRIM35 positively regulate TRAF3-mediated IFN-β production and inhibit Japanese encephalitis virus replication. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 2022 Feb;127:104290. (PubMed: 34626690) [IF=2.9]

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