Review

polyclonal rabbit anti human fhl1 antibody (Aviva Systems)

Aviva Systems is a verified supplier

Aviva Systems manufactures this product

About

News

Press Release

Team

Advisors

Partners

Contact

Bioz Stars

Bioz vStars

Buy from Supplier

Structured Review

Aviva Systems polyclonal rabbit anti human fhl1 antibody

Top : FHL1A, FHL1B and FHL1C protein structures (resulting from alternative splicing of the wild-type <t>FHL1</t> gene), including the LIM domain architecture and functional domains ( RBP-Jk , recombination signal-binding protein 1 for J-kappa; NLS , nuclear localization signals; NES , nuclear export sequence) are shown for the corresponding variants. Bottom : Protein structures resulting from alternative splicing of the two different mutant FHL1 genes. An arrow in the fourth LIM domain of mutated FHL1A at position 224 (termed FHL1A p.C224W ) indicates the position of the amino acid exchange. The dotted line suggests alterations in the LIM-like architecture (termed MUT1 here). FHL1A p.G168fs is identical to FHL1C protein (termed MUT2 here) (G = glycine, fs = frame shift).

Polyclonal Rabbit Anti Human Fhl1 Antibody, supplied by Aviva Systems, used in various techniques. Bioz Stars score: 93/100, based on 5 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/polyclonal+rabbit+anti+human+fhl1+antibody/FHL1+antibody+-+C-terminal+region+(ARP34378_T100)/pmc03203871-69-32-51
Average 93 stars, based on 5 article reviews

polyclonal rabbit anti human fhl1 antibody - by Bioz Stars, 2026-10

93/100 stars

Images

1) Product Images from "Four and a Half LIM Protein 1C (FHL1C): A Binding Partner for Voltage-Gated Potassium Channel K v1.5"

Article Title: Four and a Half LIM Protein 1C (FHL1C): A Binding Partner for Voltage-Gated Potassium Channel K v1.5

Journal: PLoS ONE

doi: 10.1371/journal.pone.0026524

Top : FHL1A, FHL1B and FHL1C protein structures (resulting from alternative splicing of the wild-type FHL1 gene), including the LIM domain architecture and functional domains ( RBP-Jk , recombination signal-binding protein 1 for J-kappa; NLS , nuclear localization signals; NES , nuclear export sequence) are shown for the corresponding variants. Bottom : Protein structures resulting from alternative splicing of the two different mutant FHL1 genes. An arrow in the fourth LIM domain of mutated FHL1A at position 224 (termed FHL1A p.C224W ) indicates the position of the amino acid exchange. The dotted line suggests alterations in the LIM-like architecture (termed MUT1 here). FHL1A p.G168fs is identical to FHL1C protein (termed MUT2 here) (G = glycine, fs = frame shift).

Figure Legend Snippet: Top : FHL1A, FHL1B and FHL1C protein structures (resulting from alternative splicing of the wild-type FHL1 gene), including the LIM domain architecture and functional domains ( RBP-Jk , recombination signal-binding protein 1 for J-kappa; NLS , nuclear localization signals; NES , nuclear export sequence) are shown for the corresponding variants. Bottom : Protein structures resulting from alternative splicing of the two different mutant FHL1 genes. An arrow in the fourth LIM domain of mutated FHL1A at position 224 (termed FHL1A p.C224W ) indicates the position of the amino acid exchange. The dotted line suggests alterations in the LIM-like architecture (termed MUT1 here). FHL1A p.G168fs is identical to FHL1C protein (termed MUT2 here) (G = glycine, fs = frame shift).

Techniques Used: Alternative Splicing, Functional Assay, Binding Assay, Sequencing, Mutagenesis

(A) RNA was isolated from myoblasts from controls (WT1, WT2) and XMPMA patients (MUT1, MUT2) and the corresponding K v1.5 and FHL1 regions were amplified by RT-PCR. Primers, spanning from exon 1 to 2 (termed FHL1) amplify the mRNA stretch coding for the common N-terminus of FHL1 in all three FHL1 isoforms (FHL1A, FHL1B and FHL1C), while primers termed FHL1A or FHL1C specifically amplify mRNAs encoding FHL1A or FHL1C, respectively. (P = positive control: human fetal brain marathon cDNA). To ensure equal gel loading, RT-PCR for human HPRT1 was performed. One representative experiment out of three is shown. See for the primer sequences used. (B) Protein lysates from myoblasts from controls (WT1, WT2) and XMPMA patients (MUT1, MUT2) were subjected to SDS-PAGE. Proteins were transferred to nitrocellulose membranes and immunoreactive bands were detected with anti-K v1.5 or anti-FHL1A as primary antibodies. After stripping, the membranes were incubated with anti-β-actin antibody. (K v1.5 = 68 kDa; FHL1A = 32 kDa; β-actin = 45 kDa). One representative experiment out of three is shown.

Figure Legend Snippet: (A) RNA was isolated from myoblasts from controls (WT1, WT2) and XMPMA patients (MUT1, MUT2) and the corresponding K v1.5 and FHL1 regions were amplified by RT-PCR. Primers, spanning from exon 1 to 2 (termed FHL1) amplify the mRNA stretch coding for the common N-terminus of FHL1 in all three FHL1 isoforms (FHL1A, FHL1B and FHL1C), while primers termed FHL1A or FHL1C specifically amplify mRNAs encoding FHL1A or FHL1C, respectively. (P = positive control: human fetal brain marathon cDNA). To ensure equal gel loading, RT-PCR for human HPRT1 was performed. One representative experiment out of three is shown. See for the primer sequences used. (B) Protein lysates from myoblasts from controls (WT1, WT2) and XMPMA patients (MUT1, MUT2) were subjected to SDS-PAGE. Proteins were transferred to nitrocellulose membranes and immunoreactive bands were detected with anti-K v1.5 or anti-FHL1A as primary antibodies. After stripping, the membranes were incubated with anti-β-actin antibody. (K v1.5 = 68 kDa; FHL1A = 32 kDa; β-actin = 45 kDa). One representative experiment out of three is shown.

Techniques Used: Isolation, Amplification, Reverse Transcription Polymerase Chain Reaction, Positive Control, SDS Page, Stripping Membranes, Incubation

Incubation:

Article Title: Four and a Half LIM Protein 1C (FHL1C): A Binding Partner for Voltage-Gated Potassium Channel K v1.5
Article Snippet: After boiling for 5 min at 95°C, protein samples were subjected to electrophoresis at 4–12% NuPage® gradient SDS-PAGE gels and transferred (90 min, 200 mA) to nitrocellulose membranes (0.45 μm, Schleicher and Schuell, Dassel, Germany, ). .. The membranes were blocked (30 min) with TBST (10 mM Tris-HCl [pH 7.4], 140 mM NaCl, 0.1% [v/v] Tween-20) containing 3% (w/v) non-fat dry milk followed by incubation overnight at 4°C with polyclonal rabbit anti-human FHL1 antibody (1∶1000, cross-reacting with the fourth LIM domain [coded for by exon 4–6] of FHL1A, AVIVA Systems Biology, San Diego, CA, USA) or polyclonal goat anti-human K v1.5 (1∶200, Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA) as primary antibodies (diluted in 3% (w/v) BSA). ..

Image Search Results

Figure 1. FHL1 inhibits anchorage‑dependent growth of tongue cancer cells. (A and B) Anchorage‑dependent growth assays in (A) Tca8113 and (B) SCC6 cells stably transfected with control siRNA or FHL1 siRNAs. Cell viability was determined at the indicated time points. Western blot analysis demonstrated the siRNA knockdown effects of anti‑FHL1. GAPDH was used as a loading control. *P<0.05 vs. control siRNA on day 5. (C and D) Anchorage‑dependent growth assays in (C) Tca8113 and (D) SCC6 cells stably transfected with FLAG‑tagged FHL1 or an empty vector (FLAG). The transfected cells were analyzed as in (A and B). *P<0.05 vs. empty vector on day 5. FHL1, four and a half LIM protein 1; siRNA, small‑interfering RNA.

Journal: Molecular medicine reports

Article Title: FHL1 inhibits the growth of tongue squamous cell carcinoma cells via G1/S cell cycle arrest.

doi: 10.3892/mmr.2015.3844

Figure Lengend Snippet: Figure 1. FHL1 inhibits anchorage‑dependent growth of tongue cancer cells. (A and B) Anchorage‑dependent growth assays in (A) Tca8113 and (B) SCC6 cells stably transfected with control siRNA or FHL1 siRNAs. Cell viability was determined at the indicated time points. Western blot analysis demonstrated the siRNA knockdown effects of anti‑FHL1. GAPDH was used as a loading control. *P<0.05 vs. control siRNA on day 5. (C and D) Anchorage‑dependent growth assays in (C) Tca8113 and (D) SCC6 cells stably transfected with FLAG‑tagged FHL1 or an empty vector (FLAG). The transfected cells were analyzed as in (A and B). *P<0.05 vs. empty vector on day 5. FHL1, four and a half LIM protein 1; siRNA, small‑interfering RNA.

Article Snippet: The antibodies used in the present study were as follows: Rabbit polyclonal anti-human FHL1 (1:200; cat. no. sc-28691; Santa Cruz Biotechnology, Inc. Dallas, TX, USA), rabbit polyclonal anti-human GAPDH (1:5,000; cat. no. sc-25778; Santa Cruz Biotechnology, Inc.), rabbit monoclonal anti-human cyclin D (1:1,000; cat. no. ab134175; Abcam, Cambridge, UK), rabbit polyclonal anti-human cyclin E (1:500; cat. no. ab101324; Abcam), and horseradish peroxidase-conjugated goat anti-rabbit immunoglobulin G secondary antibody (1:10,000; cat. no. sc-2004; Santa Cruz Biotechnology, Inc.).

Techniques: Stable Transfection, Transfection, Control, Western Blot, Knockdown, Plasmid Preparation, Small Interfering RNA

Figure 3. FHL1 induces cell cycle arrest at the G1 phase. (A) Tca8113 and (B) SCC6 cells stably transfected with control siRNA and FHL1 siRNA‑1 were ana lyzed by flow cytometry. The experiments were repeated three times with similar results. FHL1, four and a half LIM protein 1; siRNA, small‑interfering RNA.

Journal: Molecular medicine reports

Article Title: FHL1 inhibits the growth of tongue squamous cell carcinoma cells via G1/S cell cycle arrest.

doi: 10.3892/mmr.2015.3844

Figure Lengend Snippet: Figure 3. FHL1 induces cell cycle arrest at the G1 phase. (A) Tca8113 and (B) SCC6 cells stably transfected with control siRNA and FHL1 siRNA‑1 were ana lyzed by flow cytometry. The experiments were repeated three times with similar results. FHL1, four and a half LIM protein 1; siRNA, small‑interfering RNA.

Techniques: Stable Transfection, Transfection, Control, Flow Cytometry, Small Interfering RNA

Figure 2. FHL1 inhibits anchorage‑independent growth of tongue cancer cells. (A) Tca8113 and (B) SCC6 cells stably transfected with FHL1 siRNA‑1 were plated in soft agar and analyzed. Scale bar=50 mm. *P<0.05 vs. control siRNA. (C and D) FHL1 does not affect Tca8113 cell migration and invasion. Wound healing assays were performed in Tca8113 cells stably transfected with control siRNA or FHL1 siRNA‑1. (C) Images were captured at the indicated time points. Cell invasion ability was evaluated using a Matrigel invasion chamber. (D) Invasive cells were fixed and stained with crystal violet. Scale bar=100 mm. FHL1, four and a half LIM protein 1; siRNA, small‑interfering RNA.

Journal: Molecular medicine reports

Article Title: FHL1 inhibits the growth of tongue squamous cell carcinoma cells via G1/S cell cycle arrest.

doi: 10.3892/mmr.2015.3844

Figure Lengend Snippet: Figure 2. FHL1 inhibits anchorage‑independent growth of tongue cancer cells. (A) Tca8113 and (B) SCC6 cells stably transfected with FHL1 siRNA‑1 were plated in soft agar and analyzed. Scale bar=50 mm. *P<0.05 vs. control siRNA. (C and D) FHL1 does not affect Tca8113 cell migration and invasion. Wound healing assays were performed in Tca8113 cells stably transfected with control siRNA or FHL1 siRNA‑1. (C) Images were captured at the indicated time points. Cell invasion ability was evaluated using a Matrigel invasion chamber. (D) Invasive cells were fixed and stained with crystal violet. Scale bar=100 mm. FHL1, four and a half LIM protein 1; siRNA, small‑interfering RNA.

Techniques: Stable Transfection, Transfection, Control, Migration, Staining, Small Interfering RNA

Figure 4. FHL1 regulates the expression of cell cycle‑associated genes. Extracts from (A) Tca8113 and (C) SCC6 cells transfected with control siRNA and FHL1 siRNA‑1 were used for western blot analysis with the indicated antibodies. (B and D) Reverse transcription quantitative polymerase chain reaction was performed to detect the mRNA levels of the indicated genes in (B) Tca8113 and (D) SCC6 cells. *P<0.05 and **P<0.01 vs. the corresponding control siRNA. FHL1, four and a half LIM protein 1; siRNA, small‑interfering RNA.

Journal: Molecular medicine reports

Article Title: FHL1 inhibits the growth of tongue squamous cell carcinoma cells via G1/S cell cycle arrest.

doi: 10.3892/mmr.2015.3844

Figure Lengend Snippet: Figure 4. FHL1 regulates the expression of cell cycle‑associated genes. Extracts from (A) Tca8113 and (C) SCC6 cells transfected with control siRNA and FHL1 siRNA‑1 were used for western blot analysis with the indicated antibodies. (B and D) Reverse transcription quantitative polymerase chain reaction was performed to detect the mRNA levels of the indicated genes in (B) Tca8113 and (D) SCC6 cells. *P<0.05 and **P<0.01 vs. the corresponding control siRNA. FHL1, four and a half LIM protein 1; siRNA, small‑interfering RNA.

Techniques: Expressing, Transfection, Control, Western Blot, Reverse Transcription, Real-time Polymerase Chain Reaction, Small Interfering RNA

Figure 5. Knockdown of FHL1 promotes Tca8113 cell growth in nude mice. (A) Tca8113 cells stably expressing FHL1 siRNA‑1 were injected into nude mice. At the indicated time points, tumors were measured with Vernier calipers (mean ± standard deviation; n=5). *P<0.01 vs. control siRNA at week 4. (B) Western blot analysis of representative excised tumor from (A). FHL1, four and a half LIM protein 1; siRNA, small‑interfering RNA.

Journal: Molecular medicine reports

Article Title: FHL1 inhibits the growth of tongue squamous cell carcinoma cells via G1/S cell cycle arrest.

doi: 10.3892/mmr.2015.3844

Figure Lengend Snippet: Figure 5. Knockdown of FHL1 promotes Tca8113 cell growth in nude mice. (A) Tca8113 cells stably expressing FHL1 siRNA‑1 were injected into nude mice. At the indicated time points, tumors were measured with Vernier calipers (mean ± standard deviation; n=5). *P<0.01 vs. control siRNA at week 4. (B) Western blot analysis of representative excised tumor from (A). FHL1, four and a half LIM protein 1; siRNA, small‑interfering RNA.

Techniques: Knockdown, Stable Transfection, Expressing, Injection, Standard Deviation, Control, Western Blot, Small Interfering RNA

Journal: PLoS ONE

Article Title: Four and a Half LIM Protein 1C (FHL1C): A Binding Partner for Voltage-Gated Potassium Channel K v1.5

doi: 10.1371/journal.pone.0026524

Figure Lengend Snippet: Top : FHL1A, FHL1B and FHL1C protein structures (resulting from alternative splicing of the wild-type FHL1 gene), including the LIM domain architecture and functional domains ( RBP-Jk , recombination signal-binding protein 1 for J-kappa; NLS , nuclear localization signals; NES , nuclear export sequence) are shown for the corresponding variants. Bottom : Protein structures resulting from alternative splicing of the two different mutant FHL1 genes. An arrow in the fourth LIM domain of mutated FHL1A at position 224 (termed FHL1A p.C224W ) indicates the position of the amino acid exchange. The dotted line suggests alterations in the LIM-like architecture (termed MUT1 here). FHL1A p.G168fs is identical to FHL1C protein (termed MUT2 here) (G = glycine, fs = frame shift).

Article Snippet: The membranes were blocked (30 min) with TBST (10 mM Tris-HCl [pH 7.4], 140 mM NaCl, 0.1% [v/v] Tween-20) containing 3% (w/v) non-fat dry milk followed by incubation overnight at 4°C with polyclonal rabbit anti-human FHL1 antibody (1∶1000, cross-reacting with the fourth LIM domain [coded for by exon 4–6] of FHL1A, AVIVA Systems Biology, San Diego, CA, USA) or polyclonal goat anti-human K v1.5 (1∶200, Santa Cruz Biotechnology, Inc., Santa Cruz, CA, USA) as primary antibodies (diluted in 3% (w/v) BSA).

Techniques: Alternative Splicing, Functional Assay, Binding Assay, Sequencing, Mutagenesis

Journal: PLoS ONE

Article Title: Four and a Half LIM Protein 1C (FHL1C): A Binding Partner for Voltage-Gated Potassium Channel K v1.5

doi: 10.1371/journal.pone.0026524

Figure Lengend Snippet: (A) RNA was isolated from myoblasts from controls (WT1, WT2) and XMPMA patients (MUT1, MUT2) and the corresponding K v1.5 and FHL1 regions were amplified by RT-PCR. Primers, spanning from exon 1 to 2 (termed FHL1) amplify the mRNA stretch coding for the common N-terminus of FHL1 in all three FHL1 isoforms (FHL1A, FHL1B and FHL1C), while primers termed FHL1A or FHL1C specifically amplify mRNAs encoding FHL1A or FHL1C, respectively. (P = positive control: human fetal brain marathon cDNA). To ensure equal gel loading, RT-PCR for human HPRT1 was performed. One representative experiment out of three is shown. See for the primer sequences used. (B) Protein lysates from myoblasts from controls (WT1, WT2) and XMPMA patients (MUT1, MUT2) were subjected to SDS-PAGE. Proteins were transferred to nitrocellulose membranes and immunoreactive bands were detected with anti-K v1.5 or anti-FHL1A as primary antibodies. After stripping, the membranes were incubated with anti-β-actin antibody. (K v1.5 = 68 kDa; FHL1A = 32 kDa; β-actin = 45 kDa). One representative experiment out of three is shown.

Techniques: Isolation, Amplification, Reverse Transcription Polymerase Chain Reaction, Positive Control, SDS Page, Stripping Membranes, Incubation

Review

polyclonal rabbit anti human fhl1 antibody (Aviva Systems)

Structured Review

Images

1) Product Images from "Four and a Half LIM Protein 1C (FHL1C): A Binding Partner for Voltage-Gated Potassium Channel K v1.5"

Related Articles

Incubation:

Similar Products

Image Search Results