SNAIL Antibody - #AF6032

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Product: SNAIL Antibody
Catalog: AF6032
Source: Rabbit
Application: WB, IHC, IF/ICC
Reactivity: Human, Mouse, Rat
Prediction: Pig, Bovine, Horse, Rabbit, Dog, Chicken, Xenopus
Mol.Wt.: 29kDa; 29kD(Calculated).
Uniprot: O95863
RRID: AB_2834965

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MSDS
Data Sheet
COA
Protocols
WB Handbook
IHC Protocol
IF/ICC Protocol

Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

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.

Reactivity:
Human,Mouse,Rat
Prediction:
Pig(86%), Bovine(86%), Horse(100%), Rabbit(100%), Dog(86%), Chicken(86%), Xenopus(86%)
Clonality:
Polyclonal
Specificity:
SNAIL Antibody detects endogenous levels of total SNAIL.
RRID:
AB_2834965
Cite Format: Affinity Biosciences Cat# AF6032, RRID:AB_2834965.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

dJ710H13.1; Protein sna; Protein snail homolog 1; Protein snail homolog; SLUGH2; SNA; Sna protein; SNAH; SNAI; snai1; SNAI1_HUMAN; Snail 1 homolog; Snail 1 zinc finger protein; SNAIL; Snail homolog 1 (Drosophila); SNAIL, Drosophila, homolog of, 1; SNAIL1; Zinc finger protein SNAI1;

Immunogens

Immunogen:
Uniprot:

O95863(SNAI1_HUMAN) >>Visit HPA database.

Gene(ID):
SNAI1(6615)
Expression:
O95863 SNAI1_HUMAN:

Expressed in a variety of tissues with the highest expression in kidney. Expressed in mesenchymal and epithelial cell lines.

Description:
This protein has many roles during postimplantation development. It is involved in embryonic mesoderm formation and its maintenance and may also be involved in chondrogenesis and in epithelial-mesenchymal inductive interactions.
Sequence:
MPRSFLVRKPSDPNRKPNYSELQDSNPEFTFQQPYDQAHLLAAIPPPEILNPTASLPMLIWDSVLAPQAQPIAWASLRLQESPRVAELTSLSDEDSGKGSQPPSPPSPAPSSFSSTSVSSLEAEAYAAFPGLGQVPKQLAQLSEAKDLQARKAFNCKYCNKEYLSLGALKMHIRSHTLPCVCGTCGKAFSRPWLLQGHVRTHTGEKPFSCPHCSRAFADRSNLRAHLQTHSDVKKYQCQACARTFSRMSLLHKHQESGCSGCPR

Predictions

Predictions:

Score>80(red) has high confidence and is suggested to be used for WB detection. *The prediction model is mainly based on the alignment of immunogen sequences, the results are for reference only, not as the basis of quality assurance.

Species
Results
Score
Rabbit
100
Horse
100
Pig
86
Bovine
86
Dog
86
Xenopus
86
Chicken
86
Sheep
0
Zebrafish
0
Model Confidence:
High(score>80) Medium(80>score>50) Low(score<50) No confidence

PTMs - O95863 As Substrate

Site PTM Type Enzyme
S11 Phosphorylation P17612 (PRKACA) , P68400 (CSNK2A1) , Q15139 (PRKD1) , Q13131 (PRKAA1)
S82 Phosphorylation P28482 (MAPK1)
S90 Phosphorylation
S92 Phosphorylation P68400 (CSNK2A1) , P49841 (GSK3B) , P67870 (CSNK2B) , Q13131 (PRKAA1)
S96 Phosphorylation P49841 (GSK3B)
S100 Phosphorylation P49841 (GSK3B) , Q13315 (ATM)
S104 Phosphorylation P49841 (GSK3B) , P28482 (MAPK1) , P49674 (CSNK1E)
S107 Phosphorylation P49674 (CSNK1E) , P49841 (GSK3B)
S111 Phosphorylation P49841 (GSK3B)
S112 O-Glycosylation
S115 Phosphorylation P49841 (GSK3B)
S119 Phosphorylation P49841 (GSK3B)
K187 Acetylation
T201 Phosphorylation
T203 Phosphorylation Q9NRM7 (LATS2)
K206 Ubiquitination
K234 Ubiquitination
K235 Ubiquitination
S246 Phosphorylation Q13153 (PAK1) , Q16512 (PKN1)

Research Backgrounds

Function:

Involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration. Binds to 3 E-boxes of the E-cadherin/CDH1 gene promoter and to the promoters of CLDN7 and KRT8 and, in association with histone demethylase KDM1A which it recruits to the promoters, causes a decrease in dimethylated H3K4 levels and represses transcription. The N-terminal SNAG domain competes with histone H3 for the same binding site on the histone demethylase complex formed by KDM1A and RCOR1, and thereby inhibits demethylation of histone H3 at 'Lys-4' (in vitro). During EMT, involved with LOXL2 in negatively regulating pericentromeric heterochromatin transcription (By similarity). SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits (By similarity). Associates with EGR1 and SP1 to mediate tetradecanoyl phorbol acetate (TPA)-induced up-regulation of CDKN2B, possibly by binding to the CDKN2B promoter region 5'-TCACA-3. In addition, may also activate the CDKN2B promoter by itself.

PTMs:

Phosphorylated by GSK3B. Once phosphorylated, it becomes a target for BTRC ubiquitination. Phosphorylation by CSNK1E, probably at Ser-104, provides the priming site for the subsequent phosphorylation by GSK3B, probably at Ser-100 and Ser-96. Phosphorylation by PAK1 may modulate its transcriptional activity by promoting increased accumulation in the nucleus. Phosphorylation at Ser-11 and Ser-92 positively regulates its functions in induction of EMT and cell survival, respectively. Phosphorylation by LATS2, upon mitotic stress, oncogenic stress or Hippo pathway activation, occurs in the nucleus and promotes nuclear retention and stabilization of total cellular protein level.

Ubiquitinated on Lys-98, Lys-137 and Lys-146 by FBXL14 and BTRC leading to degradation. BTRC-triggered ubiquitination requires previous GSK3B-mediated SNAI1 phosphorylation. Ubiquitination induced upon interaction with NOTCH1 or TP53/p53 is mediated by MDM2.

O-GlcNAcylation at Ser-112 is enhanced in hyperglycaemic conditions, it opposes phosphorylation by GSK3B, and stabilizes the protein.

ADP-ribosylation by PARP1 increases protein half-life and may be involved in TGFB-induced SNAI1 up-regulation.

Subcellular Location:

Nucleus. Cytoplasm.
Note: Once phosphorylated (probably on Ser-107, Ser-111, Ser-115 and Ser-119) it is exported from the nucleus to the cytoplasm where subsequent phosphorylation of the destruction motif and ubiquitination involving BTRC occurs.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
Tissue Specificity:

Expressed in a variety of tissues with the highest expression in kidney. Expressed in mesenchymal and epithelial cell lines.

Subunit Structure:

Interacts with FBXL14 and GSK3B. Interacts with BTRC; interaction occurs when it is phosphorylated on the destruction motif. Interacts (via SNAG domain) with WTIP (via LIM domains) (By similarity). Interacts (via SNAG domain) with LIMD1 (via LIM domains), and AJUBA (via LIM domains). Interacts with LOXL2 and LOXL3. Interacts (via N-terminal region) with CSNK2A1. Interacts with EGR1 upon TPA induction. Interacts (via N-terminal region) with LATS2; the interaction is dependent on LATS2 kinase activity but independent of SNAI1 Thr-203 phosphorylation. Interacts (via zinc fingers) with KPNB1 and TNPO1; the interactions mediate nuclear import. Interacts (via zinc fingers) with KPNA1; the interaction disrupts the transport complex with KPNB1 and prevents nuclear import increasing SNAI1 degradation in the cytoplasm. Interacts (via zinc fingers) with KPNA2; the interaction, in combination with KPNB1, mediates nuclear import. Interacts with KPNA4; this interaction mediates nuclear import. May interact (via zinc fingers) with IPO7. Interacts (via zinc fingers) with PARP1; the interaction requires SNAI1 to be poly-ADP-ribosylated and non-phosphorylated (active) by GSK3B. Interacts (via SNAG domain) with KDM1A. Interaction with KDM1A is necessary for the down-regulation of dimethylated H3K4 mark and promoter activity of E-cadherin/CDH1, CDN7 and KRT8. Interacts with TP53/p53 and (via zinc fingers) with NOTCH1 (via intracellular domain); the interactions induce SNAI1 degradation via MDM2-mediated ubiquitination and inhibit SNAI1-induced cell invasion. Interacts with MDM2; the interaction promotes SNAI1 ubiquitination. Interacts (via zinc fingers) with CSNK1E. Interacts with PAK1.

Family&Domains:

Belongs to the snail C2H2-type zinc-finger protein family.

Research Fields

· Cellular Processes > Cellular community - eukaryotes > Adherens junction.   (View pathway)

References

1). Zhong W et al. Cartilage Oligomeric Matrix Protein promotes epithelial-mesenchymal transition by interacting with Transgelin in Colorectal Cancer. Theranostics 2020 Jul 9;10(19):8790-8806. (PubMed: 32754278) [IF=11.600]

Application: WB    Species: Human    Sample: HCT116 cells

Figure 4. COMP promotes EMT in colorectal cancer. (A) Cell phenotypic changes in cells treated with COMP siRNA and COMP overexpression. (B) WB analysis of COMP and EMT-related markers in HCT116 cells under COMP knockdown or overexpression. (C) Cell wound scratch assay of HCT116, HCT-8, and SW620 cells treated with COMP siRNA or COMP overexpression vectors. (D) Transwell assay of HCT116, HCT-8, and SW620 cells treated with COMP siRNA or COMP overexpression vectors. (E) Immunofluorescence assay of HCT116, HCT-8, and SW620 cells treated with COMP siRNA or COMP overexpression vectors. Image J software was used to analyze the relative intensity of E-cadherin and Vimentin. (F) HCT116 and HCT-8 cells with knocked down or overexpressed COMP were transplanted on nude mice. Tumor volumes were measured every 4 days. (G) Tumor weight in the control, COMP knockdown, and COMP overexpression groups. (H) The in situ spleen model of the colorectal cancer cell line SW620 showed that overexpression of COMP promoted liver metastasis of colorectal cancer, while downregulation of COMP inhibited liver metastasis of colorectal cancer. (I) IHC staining to identify EMT biomarkers and COMP-related proteins in the control, COMP knockdown, and COMP overexpression groups. COMP knockdown displayed strong E-cadherin staining and reduced Vimentin, Snail1, Twist1, and MMP-2 staining. The expression levels of other proteins were identical to those observed in WB experiments. (J) Staining indices of COMP, E-cadherin, Vimentin, Snail1, Twist1, and MMP2. The error bars in all graphs represented SD, and each experiment was repeated three times. * and ** stand for P<0.05 and P<0.01, respectively.
2). Li Y et al. ITGB1 enhances the Radioresistance of human Non-small Cell Lung Cancer Cells by modulating the DNA damage response and YAP1-induced Epithelial-mesenchymal Transition. Int J Biol Sci 2021 Jan 18;17(2):635-650. (PubMed: 33613118) [IF=10.750]

Application: WB    Species: human    Sample: NSCLC cells

Figure 8. |ITGB1 could promote radioresisntance of NSCLC cells by regulating EMT. A-C. Protein levels of E-cadherin, N-cadherin, Snail, vimentin, and Zeb1 were detected by western blotting of cells from shITGB1 and ITGB1 overexpression groups.

Application: WB    Species: Human    Sample: NSCLC cells

Figure 8 ITGB1 could promote radioresisntance of NSCLC cells by regulating EMT. A-C. Protein levels of E-cadherin, N-cadherin, Snail, vimentin, and Zeb1 were detected by western blotting of cells from shITGB1 and ITGB1 overexpression groups.
3). Fu X et al. Molecular mechanism of albumin in suppressing invasion and metastasis of hepatocellular carcinoma. Liver Int 2022 Mar;42(3):696-709. (PubMed: 34854209) [IF=8.754]

Application: WB    Species: Human    Sample: HepG2 and Huh7 cells

FIGURE 7 A, Representative images of the western blot results for uPAR, MMP2 and MMP9 in ALB knockdown HepG2 and Huh7 cells; B, Zymography analysis illustrates MMP2 and MMP9 activity in ALB knockdown HepG2 and Huh7 cells; C, Quantitative analysis results and representative images of the western blot results for the EMT‐associated markers, E‐cadherin, N‐cadherin, vimentin, Snail and Twist by western blot in ALB knockdown HepG2 and Huh7 cells; D, Quantification shows a significantly higher uPAR in HCC group with ALB <3.5 g/dL compared to ALB ≥3.5 g/dL (*P < .05); E, Scatterplot showing the correlation between plasma levels of ALB and uPAR. The vertical position represents the expression levels of uPAR (lg pg/mL)
4). Sun C et al. DSC2 Suppresses the Metastasis of Gastric Cancer through Inhibiting the BRD4/Snail Signaling Pathway and the Transcriptional Activity of β-Catenin. Oxid Med Cell Longev 2022 Sep 6;2022:4813571. (PubMed: 36120591) [IF=7.310]
5). Li H et al. MicroRNA-181a regulates epithelial-mesenchymal transition by targeting PTEN in drug-resistant lung adenocarcinoma cells. Int J Oncol 2015 Oct;47(4):1379-92 (PubMed: 26323677) [IF=5.884]

Application: WB    Species: human    Sample: A549 cells

Figure 3. A549/DDP and A549/PTX cells showed molecular and morphological changes that were consistent with EMT. (A) microscopy at x200 magnification was used to assess cell morphology. The A549 cells (parental cells) had an epithelioid, rounded cobblestone appearance and there was limited formation of pseudopodia. A549/PTX and A549/DDP cells exhibited a spindle-shaped morphology and an increased formation of pseudopodia, indicating a loss of cell polarity. (B) E-cadherin, β-catenin, vimentin, MMP-2 and MMP-9 which are EMT-related proteins, were assessed in terms of expression levels. EMT-related transcription factors (Snail, Slug, Twist and ZEB1) were measured in A549/PTX and A549/DDP cells using western blot analysis. (C) The expression changes were confirmed at the mRNA level by qRT-PCR. Expression was standardized to the expression of GAPDH and normalized to 1.0 in the parental cells (compared with the parental A549 cells, means ± SEM, n=3, * P<0.05)

Application: WB    Species: human    Sample: A549/PTX cells

Figure 7.| miR-181a downregulation in A549/PTX cells reverses both drug resistance and morphological and molecular changes. (C) Western blot analysis was used to detect the expression of E-cadherin, β-catenin, vimentin, MMP-9, MMP-2, Snail, Slug,Twist and ZEB1 after transfection.
6). Wang Y et al. Cinnamaldehyde Suppressed EGF-Induced EMT Process and Inhibits Ovarian Cancer Progression Through PI3K/AKT Pathway. Front Pharmacol 2022 May 12;13:779608. (PubMed: 35645793) [IF=5.810]
7). Xu S et al. γ-Glutamyl cyclotransferase contributes to endometrial carcinoma malignant progression and upregulation of PD-L1 expression during activation of epithelial-mesenchymal transition. Int Immunopharmacol 2020 Apr;81:106039. (PubMed: 31757677) [IF=5.714]

Application: WB    Species: Human    Sample: endometrial carcinoma cells

Fig. 4. GGCT contributed to malignant biological behaviors of endometrial carcinoma cells during EMT activation. The expression of the EMT markers E-cadherin, N- cadherin, Vimentin, Twist, Snail, and Slug detected using western blot demonstrated the contribution of GGCT to the EMT process in endometrial carcinoma. This analysis was repeated three times (A, B). Immunohistochemical staining of the EMT markers E-cadherin, N-cadherin, Vimentin, Twist, Snail, and Slug in tumor tissues from the xenograft model demonstrated the contribution of GGCT to the EMT process in vivo (C). *p < 0.05.

Application: IHC    Species: Human    Sample: endometrial carcinoma cells

Fig. 4. GGCT contributed to malignant biological behaviors of endometrial carcinoma cells during EMT activation. The expression of the EMT markers E-cadherin, N- cadherin, Vimentin, Twist, Snail, and Slug detected using western blot demonstrated the contribution of GGCT to the EMT process in endometrial carcinoma. This analysis was repeated three times (A, B). Immunohistochemical staining of the EMT markers E-cadherin, N-cadherin, Vimentin, Twist, Snail, and Slug in tumor tissues from the xenograft model demonstrated the contribution of GGCT to the EMT process in vivo (C). *p < 0.05.

Application: WB    Species: Mice    Sample: tumor tissues

Fig. 4. GGCT contributed to malignant biological behaviors of endometrial carcinoma cells during EMT activation. The expression of the EMT markers E-cadherin, Ncadherin, Vimentin, Twist, Snail, and Slug detected using western blot demonstrated the contribution of GGCT to the EMT process in endometrial carcinoma. This analysis was repeated three times (A, B). Immunohistochemical staining of the EMT markers E-cadherin, N-cadherin, Vimentin, Twist, Snail, and Slug in tumor tissues from the xenograft model demonstrated the contribution of GGCT to the EMT process in vivo (C). *p < 0.05.

Application: IHC    Species: Mice    Sample: tumor tissues

Fig. 4. GGCT contributed to malignant biological behaviors of endometrial carcinoma cells during EMT activation. The expression of the EMT markers E-cadherin, Ncadherin, Vimentin, Twist, Snail, and Slug detected using western blot demonstrated the contribution of GGCT to the EMT process in endometrial carcinoma. This analysis was repeated three times (A, B). Immunohistochemical staining of the EMT markers E-cadherin, N-cadherin, Vimentin, Twist, Snail, and Slug in tumor tissues from the xenograft model demonstrated the contribution of GGCT to the EMT process in vivo (C). *p < 0.05.
8). Xu S et al. γ-Glutamyl cyclotransferase contributes to endometrial carcinoma malignant progression and upregulation of PD-L1 expression during activation of epithelial-mesenchymal transition. Int Immunopharmacol 2020 Apr;81:106039. (PubMed: 31757677) [IF=5.714]
9). Li XH et al. Parthenolide attenuated bleomycin-induced pulmonary fibrosis via the NF-κB/Snail signaling pathway. Respir Res 2018 Jun 5;19(1):111 (PubMed: 29871641) [IF=5.631]

Application: WB    Species: human    Sample: lung epithelial cells

Fig. 2 |PTL inhibits TGF-β1-induced EMT through inhibiting NF-κB/Snail expression in lung epithelial cells.e-h After TGF-β/PTL treatment, NF-κB and Snail were evaluated using Western blot analysis. β-actin was used as a loading control. Data are presented as means of three experiments; error bars represent standard deviation, *P < 0.05, **P < 0.01

Application: IHC    Species: human    Sample: lung

Fig. 7 |PTL attenuates the BLM-induced expression of NF-κB and Snail. a Immunohistochemical staining for NF-κB and Snail in lung sections.
10). Chen G et al. SOSTDC1 inhibits bone metastasis in non-small cell lung cancer and may serve as a clinical therapeutic target. Int J Mol Med 2018 Oct 10 (PubMed: 30320379) [IF=5.314]

Application: WB    Species: human    Sample: A549 and PC9 cells

Figure 3. |Overexpression of SOSTDC1 inhibits the epithelial‑mesenchymal transition process in non‑small cell lung cancer cells. The expression levels of epithelial marker CDH1 and the mesenchymal markers VIM and SNAI1 were detected by western blot analysis following the overexpression of SOSTDC1 in A549 and PC9 cells. SOSTDC1, sclerostin domain‑containing protein 1; CDH1, cadherin 1; VIM, vimentin; SNAI1, zinc finger protein SNAI1; OE, overexpression; CTRL, control.
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