Rabbit Anti-SALL4 Polyclonal antibody (DPABH-05831)

Rabbit Anti-Human SALL4 Polyclonal antibody for WB, IP, IHC, IF, ELISA


Host Species
Antibody Isotype
Species Reactivity
Human, Rat


Application Notes
WB: 1:500-1:2000
IP: 0.5-4.0 ug for IP and 1:500-1:1000 for WB
IHC: 1:20-1:200
*Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.


Alternative Names
SALL4; spalt-like transcription factor 4; DRRS; HSAL4; ZNF797; dJ1112F19.1
Entrez Gene ID
UniProt ID


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SOX1 is correlated to sternness state regulator SALL4 through progression and invasiveness of esophageal squamous cell carcinoma


Authors: Rad, Abolfazl; Dizghandi, Saeed Esmaeili; Abbaszadegan, Mohammad Reza; Taghechian, Negin; Najafi, Maryam; Forghanifard, Mohammad Mandi

SOX1, as a tumor suppressor, play anti-tumorigenecity role in different cells and its expression is inhibited in a variety of cancers. The aim of this study was to evaluate SOX1 expression and its correlation with cancer stem cell (CSC) markers in ESCC. Using real time PCR, the relative comparative expression of SOX1 in 40 ESCC samples was assessed compared to related margin normal tissues, and its correlation with CSC markers including SALL4, SOX2, and MEIS1 was analyzed statistically. The results revealed significant under-expression of SOX1 in ESCC in significant correlation with different indices of poor prognosis including depth of tumor invasion (P = 0.02), Stage of tumor cell progression (P = 0.05), and number of involved lymph node metastasis (P = 0.05). Furthermore, the under-expression of SOX1 was associated significantly with SALL4 overexpression. This study was the first to evaluate SOX1 underexpression and its association with poor prognosis in ESCC. Since correlation of SOX1 and SALL4 was detected in advanced stages of ESCC progression, as well as high invasive and aggressive tumor tissues, it may be extrapolated that SOX1 expression may have critical role in inhibition of ESCC invasiveness and aggressiveness especially in advanced stages of the disease. (C) 2016 Elsevier B.V. All rights reserved.

Expression of Cathepsins B, D, and G in Isocitrate Dehydrogenase-Wildtype Glioblastoma


Authors: Koh, Sabrina P.; Wickremesekera, Agadha C.; Brasch, Helen D.; Marsh, Reginald; Tan, Swee T.; Itinteang, Tinte

Aim: To investigate the expression of cathepsins B, D, and G, in relation to the cancer stem cell (CSC) subpopulations, we have previously characterized within isocitrate dehydogenase (IDH)-wildtype glioblastoma (IDHWGB). Methods: 3,3-Diaminobezidine (DAB) immunohistochemical (IHC) staining for cathepsins B, D, and G, was performed on 4 mu m-thick formalin-fixed paraffin-embedded IDHWGB samples obtained from six patients. Two representative DHWGB samples from the original cohort of patients were selected for immunofluorescent (IF) IHC staining, to identify the localization of the cathepsins in relation to the CSC subpopulations. NanoString gene expression analysis and colorimetric in situ hybridization (CISH) were conducted to investigate the transcriptional activation of genes encoding for cathepsins B, D, and G. Data obtained from cell counting of DAB IHC-stained slides and from NanoString analysis were subjected to statistical analyses to determine significance. Results: Cathepsin B and cathepsin D were detected in IDHWGB by DAB IHC staining. IF IHC staining demonstrated the expression of both cathepsin B and cathepsin D by the OCT4(+) and SALL4(+) CSC subpopulations. NanoString gene analysis and CISH confirmed the abundant transcript expression of these cathepsins. The transcriptional and translational expressions of cathepsin G were minimal and were confined to cells within the microvasculature. Conclusion: This study demonstrated the expression of cathepsin B and cathepsin D but not cathepsin G within the CSC subpopulations of IDHWGB at both the transcriptional and translational level. Cathepsin G was expressed at low levels and was not localized to the CSC population of IDHWGB. The novel finding of cathepsin B and cathepsin D in IDHWGB suggests the presence of bypass loops for the renin-angiotensin system, which may facilitate the production of angiotensin peptides. Elucidating the precise role of these cathepsins may lead to better understanding and more effective treatment of this aggressive tumor.

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