Product Info

Source:
Mouse
Application:
WB: 1:3000-1:10000, IHC: 1:50-1:200, IF/ICC: 1:100-1:500, IP 1:100-1:500
*The optimal dilutions should be determined by the end user.
Reactivity:
All
Clonality:
Monoclonal [5F67]
Specificity:
GFP-Tag Mouse Monoclonal antibody detects endogenous levels of C-terminal, internal, and N-terminal GFP-tagged proteins.
RRID:
AB_2839413
Cite Format: Affinity Biosciences Cat# T0005, RRID:AB_2839413.
Purification:
Affinity-chromatography.
Storage:
Mouse IgG1 in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.

Immunogens

Immunogen:

Full-length GFP protein.

Description:
N/A

References

1). Zhou X et al. Splicing factor SRSF1 promotes gliomagenesis via oncogenic splice-switching of MYO1B. J Clin Invest 2018 Nov 27 (PubMed: 30481162) [IF=11.864]

Application: WB    Species: human    Sample: U87MG and U251 cells

Figure 10.| SRSF1-guided MYO1B splicing determines cell fate through the PDK1/AKT and PAK/LIMK pathways. (D) Co-IP confirmation of the interaction between EGFP-fused MYO1B proteins (MYO1B-fl and MYO1B-t) and endogenous p85 PI3K in U87MG and U251 cells.

2). 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 Environ 2020 Jan;43(1):261-274 (PubMed: 31674679) [IF=6.362]

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

3). Liang L et al. Identification and functional analysis of two new de novo KCNMA1 variants associated with Liang–Wang syndrome. Acta Physiol (Oxf) 2022 Feb 13;e13800. (PubMed: 35156297) [IF=5.542]

4). Zhou Y et al. Orf virus ORF120 protein positively regulates the NF-κB pathway by interacting with G3BP1. J Virol 2021 Jul 21;JVI0015321. (PubMed: 34287041) [IF=4.501]

5). Duan Z et al. Chicken bromodomain-containing protein 2 interacts with the Newcastle disease virus matrix protein and promotes viral replication. Vet Res 2020 Sep 22;51(1):120. (PubMed: 32962745) [IF=3.357]

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

Figure 5 |siRNA-mediated knockdown of chBRD2 promotes NDV replication in DF-1 cells.F The expression levels of the M and GFP proteins in chBRD2 siRNA#2- or control siRNA-treated cells were examined by western blot at 6, 12 and 24 hpi, respectively. The relative expression levels of the M and GFP proteins compared to control GAPDH expression levels were determined by densitometry using ImageJ software version 1.8.0. Error bars represent standard deviations(mean±SD) (*P<0.05; **P<0.01 compared to the value of the control siRNA group).

6). Xu Z et al. Mutated SASH1 promotes Mitf expression in a heterozygous mutated SASH1 knock‑in mouse model. Int J Mol Med 2020 Jun 19. (PubMed: 32582980) [IF=3.098]

7). Sun L et al. Proteasome inhibition promotes mono-ubiquitination and nuclear translocation of mature (52 kDa) PINK1. Biochem Biophys Res Commun 2019 Sep 17;517(2):376-382 (PubMed: 31362890)

8). Ben-Chang Li et al. Plasmalemma localisation of DOUBLE HYBRID PROLINE-RICH PROTEIN 1 and its function in systemic acquired resistance of Arabidopsis thaliana. Functional Plant Biology 2014;41(7):768.

9). A Novel SASH1-IQGAP1-E-Cadherin Signal Cascade Mediates Breast Cancer Metastasis.

Restrictive clause

 

Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.

For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.