HOXA10 Antibody (Rabbit mAb) [M2L19]

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000 IP1:30 IF1:50 FCM1:50 CHIP1:100

Application
WB, IP, IF, FCM, ChIP

Reactivity
Human

Source
Rabbit 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 Observed MW
42 kDa 50 kDa, 15 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Positive Control	Human bone marrow tissue; Human testis tissue; THP-1 cells; 293T cells; His-tagged human HOXA10 recombinant protein fragment
Negative Control	K562 cells

Datasheet & SDS

Biological Description

Specificity
HOXA10 Antibody (Rabbit mAb) [M2L19] detects endogenous levels of total HOXA10 protein.

Clone
M2L19

Synonym(s)
HOX1H, HOXA10, Homeobox protein Hox-A10, Homeobox protein Hox-1.8, Homeobox protein Hox-1H, PL

Background
HOXA10, also designated HOX1H, belongs to the homeobox family of transcription factors, and its capacity to select specific target genes among the many DNA sequences it could theoretically bind depends on cooperative interaction with cofactors of the three-amino-acid loop extension family, principally Pbx2 and Meis1, since HOXA10 alone shows limited target specificity while multimeric complex formation with these cofactors imparts the enhanced specificity required for physiological function. In human endometrium, HOXA10 forms a heterodimer with Pbx2 that binds directly to an enhancer element within the EMX2 gene, a validated HOXA10 target, and ablation of the Pbx binding site in this enhancer abolishes dimer binding, while ablation of the HOXA10 binding site alone does not, demonstrating that Pbx2 engagement of DNA is structurally required to stabilize the complex even at a site nominally defined by HOXA10 recognition. HOXA10, Pbx2, and Meis1 are co-expressed in endometrial stroma throughout the menstrual cycle, while glandular expression of HOXA10 and Meis1 specifically varies with cycle stage, and this expression pattern together with EMSA binding data indicates that heterodimeric and trimeric HOXA10-Pbx2-Meis1 complexes, rather than HOXA10 acting alone, determine which target genes are engaged during the window of endometrial receptivity. HOXA10 and its paralog HOXA11 regulate endometrial receptivity through modulation of extracellular matrix remodeling via matrix metalloproteinases, cytokine signaling including leukemia inhibitory factor, and cell adhesion molecules such as beta-3 integrin, and together these downstream effectors drive the epithelial and stromal cell differentiation together with trophoblast invasion competence required for embryo implantation; HOXA10 and HOXA11 expression itself is dynamically regulated by estrogen and progesterone, peaking during the secretory phase of the cycle when implantation occurs. Disruption of this hormonal and transcriptional program produces defined disease consequences: reduced HOXA10 expression in endometriosis arises from DNA hypermethylation coupled with chronic inflammation, disrupting immune modulation and cytokine signaling at the implantation site, while HOXA11-regulated extracellular matrix remodeling and beta-3 integrin expression are separately disrupted in adenomyosis, impairing embryo attachment through a mechanistically distinct route.

Background

HOXA10, also designated HOX1H, belongs to the homeobox family of transcription factors, and its capacity to select specific target genes among the many DNA sequences it could theoretically bind depends on cooperative interaction with cofactors of the three-amino-acid loop extension family, principally Pbx2 and Meis1, since HOXA10 alone shows limited target specificity while multimeric complex formation with these cofactors imparts the enhanced specificity required for physiological function. In human endometrium, HOXA10 forms a heterodimer with Pbx2 that binds directly to an enhancer element within the EMX2 gene, a validated HOXA10 target, and ablation of the Pbx binding site in this enhancer abolishes dimer binding, while ablation of the HOXA10 binding site alone does not, demonstrating that Pbx2 engagement of DNA is structurally required to stabilize the complex even at a site nominally defined by HOXA10 recognition. HOXA10, Pbx2, and Meis1 are co-expressed in endometrial stroma throughout the menstrual cycle, while glandular expression of HOXA10 and Meis1 specifically varies with cycle stage, and this expression pattern together with EMSA binding data indicates that heterodimeric and trimeric HOXA10-Pbx2-Meis1 complexes, rather than HOXA10 acting alone, determine which target genes are engaged during the window of endometrial receptivity. HOXA10 and its paralog HOXA11 regulate endometrial receptivity through modulation of extracellular matrix remodeling via matrix metalloproteinases, cytokine signaling including leukemia inhibitory factor, and cell adhesion molecules such as beta-3 integrin, and together these downstream effectors drive the epithelial and stromal cell differentiation together with trophoblast invasion competence required for embryo implantation; HOXA10 and HOXA11 expression itself is dynamically regulated by estrogen and progesterone, peaking during the secretory phase of the cycle when implantation occurs. Disruption of this hormonal and transcriptional program produces defined disease consequences: reduced HOXA10 expression in endometriosis arises from DNA hypermethylation coupled with chronic inflammation, disrupting immune modulation and cytokine signaling at the implantation site, while HOXA11-regulated extracellular matrix remodeling and beta-3 integrin expression are separately disrupted in adenomyosis, impairing embryo attachment through a mechanistically distinct route.

References
https://pubmed.ncbi.nlm.nih.gov/15494461/ https://pubmed.ncbi.nlm.nih.gov/40305321/

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%