ENCAB000AMD
Antibody against Homo sapiens UBTF, Mus musculus UBTF
Homo sapiens
K562, HeLa-S3, HepG2
characterized to standards
Homo sapiens
any cell type or tissue
partially characterized
Mus musculus
any cell type or tissue
partially characterized
Homo sapiens
GM12878
not characterized to standards
- Status
- released
- Source (vendor)
- Santa Cruz Biotech
- Product ID
- sc-13125
- Lot ID
- B1804
- Characterized targets
- UBTF (Homo sapiens), UBTF (Mus musculus)
- Host
- mouse
- Clonality
- monoclonal
- Purification
- other
- Antigen description
- UBF (F-9) is raised against amino acids 1-220 of UBF of human origin.
- External resources
Characterizations
UBTF (Homo sapiens)
K562
not compliant
- Caption
- Immunoprecipitation was performed on nuclear extracts from the cell line: K562, using the antibody sc-13125. The blot shows western blot analysis of input, flowthrough, immunoprecipitate and mock immunoprecipitate using IgG.Molecular Weight: 97.0
- Reviewer comment
- Band appears in the IgG control.
- Submitted by
- Denis Salins
- Lab
- Michael Snyder, Stanford
- Grant
- U54HG006996
- Download
- 1070_1_UBF_sc-13125x.jpg
UBTF (Homo sapiens)
not reviewed
- Caption
- Using antibody SAB1404509 or sc-13125, we observe a major band in Western blots on lysates from cell lines K562, HeLa S3, HepG2, and, at lower intensity, GM12878 that migrates at a position consistent with the predicted size (~89kD) of UBF/UBTF (Panels A,B). This band is specifically immunoprecipitated from K562 lysates by each antibody (Panels C,D). Based on this, SAB1404509 and sc-13125 are validated by this criterion.
- Submitted by
- Michael Snyder
- Lab
- Michael Snyder, Stanford
- Grant
- U54HG004558
UBTF (Homo sapiens)
not reviewed
- Caption
- Because the overlap of the top 40% of peaks from datasets derived from antibodies sc-13125 and SAB1404509 (compared using standard ENCODE scoring methods) exceeds the recommended threshold of 80%, both antibodies meet this criterion for validation.
- Submitted by
- Michael Snyder
- Lab
- Michael Snyder, Stanford
- Grant
- U54HG004558
UBTF (Mus musculus)
not reviewed
- Caption
- Immunoprecipitation of CH12 and MEL nuclear extracts using anti-UBF (sc-13125) efficiently enriches a protein of molecular weight of UBF (~97 kD).
- Submitted by
- Michael Snyder
- Lab
- Michael Snyder, Stanford
- Grant
- RC2HG005602
- Download
- mouse_UBF_validation_Snyder.pdf
UBTF (Mus musculus)
not reviewed
- Caption
- sc-13125 is validated for human cell lines using comparison of ChIP-Seq data obtained using two different antibodies against UBTF. See validation documents for human cell lines for details.
- Submitted by
- Michael Snyder
- Lab
- Michael Snyder, Stanford
- Grant
- RC2HG005602
- Download
- mouse_UBF_validation_Snyder.pdf
UBTF (Homo sapiens)
GM12878K562HeLa-S3HepG2
compliant
- Caption
- Western blot analysis of nuclear lysates prepared from multiple cells lines loaded in the order: GM12878, K562, HeLaS3, HepG2 using the antibody sc-13125. Molecular Weight: 97.0
- Reviewer comment
- No visible band in the lane
- Submitted by
- Nathaniel Watson
- Lab
- Michael Snyder, Stanford
- Grant
- U54HG006996
- Download
- Scan_20160415.jpg
UBTF (Homo sapiens)
K562
compliant
- Caption
- Immunoprecipitation was performed on nuclear extracts from the cell line K562 using the antibody sc-13125. Lane 1: input nuclear lysate. Lane 2: material immunoprecipitated with antibody. Lane 3: material immunoprecipitated using control IgG. Marked bands were excised from gel and subjected to analysis by mass spectrometry. Target molecular weight: 97.0.
- Submitted by
- Nathaniel Watson
- Lab
- Michael Snyder, Stanford
- Grant
- U54HG006996
- Download
- UBF_sc-13125.jpg
UBTF (Homo sapiens)
compliant
- Caption
- IP followed by mass spectrometry. Briefly, protein was immunoprecipitated from K562 nuclear cell lysates using the antibody sc-13125, and the IP fraction was loaded on a 10% polyacrylamide gel (NuPAGEBis-Tris Gel) and separated with an Invitrogen NuPAGE electrophoresis system. The gel was stained by ColloidialCoomassie G-250 stain, gel fragments corresponding to the bands indicated were excised. Then proteins were trypsinized using the in-gel digestion method. Digested proteins were analyzed on an Orbitrap Elite mass spectrometer (Thermo Scientific) by the nanoLC-ESI-MS/MS technique. Peptides were identified by the SEQUEST algorithm and filtered with a high confidence threshold (Peptide false discovery rate < 1%, 2 unique peptides per protein minimum, mass error < 10 ppm).
- Submitted by
- Nathaniel Watson
- Lab
- Michael Snyder, Stanford
- Grant
- U54HG006996
- Download
- UBTF_sc-13125 final.xls.pdf