epitope mapping near the C-terminus of MASL1 of human origin
Modification Notes
The leucine-rich (LRR) repeat is a 20-30 amino acid motif that forms a hydrophobic å/∫ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. MASL1, also known as MFHAS1 (malignant fibrous histiocytoma amplified sequence 1) or LRRC65, is a 1,052 amino acid protein that contains 13 LRR repeats, which are thought to function as structural components for protein-protein interactions during the cell cycle. Ubiquitously expressed, MASL1 is upregulated in malignant fibrous histiocytomas, suggesting that, via its ability to mediate protein interactions during the cell cycle, MASL1 may play a role in tumorigenesis. The gene encoding MASL1 is subject to a chromosomal aberration that is thought to be a cause of B-cell lymphoma, further implying a role for MASL1 in tumor formation.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIFELISA
recommended for detection of MASL1 of mouse, rat and human origin by WB, IF and ELISA also reactive with additional species, including equine, canine and avian:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope mapping near the C-terminus of MASL1 of human origin
Tissue Specificity
epitope mapping near the C-terminus of MASL1 of human origin
Western blot analysis of MASL1 expression in non-transfected: (A) and human MASL1 transfected: (B) 293T whole cell lysates.
Application Notes
recommended for detection of MASL1 of mouse, rat and human origin by WB, IF and ELISA also reactive with additional species, including equine, canine and avian:
Additional Information
Form
Liquid
Storage Instructions
For short-term storage, store at 4° C. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.