Snail + Slug N-terminal Antibody (Mouse mAb) [E10J13]

Application: Reactivity: Human

Usage Information

Dilution
IHC1:5000 - 1:10000 IF1:200-1:1000

Application
IHC, IF

Reactivity
Human

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
29 kDa

Positive Control	Human colon tissue; Human cortex tissue; Human breast cancer tissue; Human fallopian tube tissue; Human colorectal cancer tissue; Human testis tissue; Human prostate tissue; BeWo cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
Snail + Slug N-terminal Antibody (Mouse mAb) [E10J13] detects endogenous levels of total Snail and Slug proteins, typically through their N-terminal regions.

Clone
E10J13

Synonym(s)
SNAH, SNAI1, Zinc finger protein SNAI1, Protein snail homolog 1, Protein sna, SLUG, SLUGH, SNAI2, Zinc finger protein SNAI2, Neural crest transcription factor Slug, Protein snail homolog 2

Background
SNAIL and SLUG, also designated SNAI1 and SNAI2, belong to the SNAIL family of zinc finger transcription factors that drive epithelial-mesenchymal transition, and both proteins share a conserved N-terminal SNAG domain that functions as the primary repressive module distinct from the C-terminal zinc finger DNA-binding region. This SNAG domain adopts a structure resembling the N-terminal tail of histone H3, allowing it to act as a pseudosubstrate hook that docks directly into the amino oxidase domain of the histone lysine-specific demethylase LSD1, and this interaction stabilizes a ternary Snail1-LSD1-CoREST complex at target gene promoters, most notably the E-cadherin promoter, CDH1. Once this complex is assembled, transcriptional silencing proceeds through a defined multistage sequence: HDAC1 and HDAC2 within the CoREST-Snail1-LSD1 complex first deacetylate histone H3 and H4, Polycomb repressive complex 2 is then recruited in a manner that requires both an intact Snail1-binding site on the promoter and the SNAG domain itself, directing trimethylation of histone H3 lysine 27, and LSD1 subsequently removes the activating H3K4 methylation mark, together converting an active promoter into a stably silenced one. In Slug, the SNAG domain, spanning the extreme N-terminus, recruits the corepressor NCoR directly, while a separate central region termed the SLUG domain recruits CtBP1, and functional dissection using domain-deletion constructs shows that the SNAG domain is absolutely required for EMT induction, whereas the SLUG domain contributes to efficient E-cadherin repression but exerts a negative modulatory effect on SNAG-driven EMT induction and on NCoR corepressor activity when deleted. Both SNAIL and SLUG require their SNAG domains for E-cadherin promoter repression, but the domain composition governing corepressor recruitment differs between the two paralogs, with Slug relying on two distinct, functionally separable domains that recruit different corepressor complexes rather than a single shared repressive interface. This SNAG-LSD1 interaction is directly druggable: pharmacological inhibition of LSD1 with the enzymatic inhibitor Parnate, or competitive blockade using a cell-permeable TAT-SNAG peptide corresponding to the Slug SNAG domain, disrupts Slug-dependent repression of the E-cadherin promoter and suppresses motility and invasion across tumor cell lines of varying origin without affecting cell proliferation, demonstrating that the SNAG domain interaction with chromatin-modifying enzymes is mechanistically separable from other SNAIL and SLUG functions and represents a defined point of therapeutic intervention in EMT-driven cancer invasion.

Background

SNAIL and SLUG, also designated SNAI1 and SNAI2, belong to the SNAIL family of zinc finger transcription factors that drive epithelial-mesenchymal transition, and both proteins share a conserved N-terminal SNAG domain that functions as the primary repressive module distinct from the C-terminal zinc finger DNA-binding region. This SNAG domain adopts a structure resembling the N-terminal tail of histone H3, allowing it to act as a pseudosubstrate hook that docks directly into the amino oxidase domain of the histone lysine-specific demethylase LSD1, and this interaction stabilizes a ternary Snail1-LSD1-CoREST complex at target gene promoters, most notably the E-cadherin promoter, CDH1. Once this complex is assembled, transcriptional silencing proceeds through a defined multistage sequence: HDAC1 and HDAC2 within the CoREST-Snail1-LSD1 complex first deacetylate histone H3 and H4, Polycomb repressive complex 2 is then recruited in a manner that requires both an intact Snail1-binding site on the promoter and the SNAG domain itself, directing trimethylation of histone H3 lysine 27, and LSD1 subsequently removes the activating H3K4 methylation mark, together converting an active promoter into a stably silenced one. In Slug, the SNAG domain, spanning the extreme N-terminus, recruits the corepressor NCoR directly, while a separate central region termed the SLUG domain recruits CtBP1, and functional dissection using domain-deletion constructs shows that the SNAG domain is absolutely required for EMT induction, whereas the SLUG domain contributes to efficient E-cadherin repression but exerts a negative modulatory effect on SNAG-driven EMT induction and on NCoR corepressor activity when deleted. Both SNAIL and SLUG require their SNAG domains for E-cadherin promoter repression, but the domain composition governing corepressor recruitment differs between the two paralogs, with Slug relying on two distinct, functionally separable domains that recruit different corepressor complexes rather than a single shared repressive interface. This SNAG-LSD1 interaction is directly druggable: pharmacological inhibition of LSD1 with the enzymatic inhibitor Parnate, or competitive blockade using a cell-permeable TAT-SNAG peptide corresponding to the Slug SNAG domain, disrupts Slug-dependent repression of the E-cadherin promoter and suppresses motility and invasion across tumor cell lines of varying origin without affecting cell proliferation, demonstrating that the SNAG domain interaction with chromatin-modifying enzymes is mechanistically separable from other SNAIL and SLUG functions and represents a defined point of therapeutic intervention in EMT-driven cancer invasion.

References
https://pubmed.ncbi.nlm.nih.gov/20517332/ https://pubmed.ncbi.nlm.nih.gov/22567133/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%