B9428
Monoclonal Anti-Bin1 antibody produced in mouse
clone 99D, ascites fluid
Synonym(s):
Anti-Amphiphysin II, Anti-SH3P9, Anti-ampl
Product Name
Monoclonal Anti-Bin1 antibody produced in mouse, clone 99D, ascites fluid
biological source
mouse
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
99D, monoclonal
mol wt
antigen 65-75 kDa
contains
15 mM sodium azide
species reactivity
rabbit, mouse, rat, avian, human
technique(s)
flow cytometry: suitable
immunocytochemistry: suitable using nucleoplasm, subnuclear punctate compartment, and cytoplasm
immunohistochemistry (frozen sections): suitable
immunoprecipitation (IP): suitable
indirect ELISA: suitable
western blot: 1:50,000 using a rat brain cytosol preparation
isotype
IgG2b
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... BIN1(274)
mouse ... Bin1(30948)
rat ... Bin1(117028)
Application
Monoclonal Anti-Bin1 antibody produced in mouse has been used in:
- western blotting
- enzyme linked immunosorbent assay (ELISA)
- immunoprecipitation
- immunocytochemistry
- immunohistochemistry
- flow cytometry
Biochem/physiol Actions
Box-dependent myc-interacting protein-1 (Bin1) interacts with and inhibits the oncogenic activity of the myc oncoprotein that has a major role in many human cancers. The loss of Bin1 may contribute to growth deregulation in cancer cells in carcinoma of the breast, colon, lung, cervix, prostate and liver. In bin1 locus mid-2q region that is deleted in approx. 42% of metastatic prostate cancers, and at the syntenic murine locus, in >90% of radiation-induced myeloid leukemias. In addition to the role of Bin1 in controlling neoplastic cell growth and cell cycle by the inhibition of transformation by both myc and the adenovirus E1A protein. Deficits in expression are functionally significant, because ectopic Bin1 can inhibit the growth of tumor cells that lack endogenous expression. Bin1 has also been found to be highly expressed in murine skeletal muscle; overexpression of Bin1 promotes myotube formation and upregulation of myosin heavy chain, while interference with Bin1 expression significantly impairs these processes.
The antibody reacts specifically with a 33-residue segment of the myc-binding domain (MBD, amino acids 323-356) of the human Bin1 molecule. It does not react with the Bin1-related 45 kDa polypeptide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
Monoclonal Anti-Bin1 (SH3P9, Amphiphysin II, amphl) (mouse IgG2b isotype) is derived from the 99D hybridoma produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a recombinant polypeptide, containing amino acids 189-398 of human Bin1. Bin1 [Box-dependent myc-interacting protein-1, also known as SH3P9, amphiphysin II and amphl (amphiphysin-like)] is a novel protein that has features of a tumor suppressor. The human BIN1 gene has been mapped to chromosome 2q14. In human and rodent cells it appears as a short-lived (half-life of approx. 2 hrs) monomeric phosphoprotein (approx. 70 kDa). Bin1 molecule appears in different isoforms or conformations, and the localization varies between normal and tumor cells. In normal cells, Bin1 is predominantly nucleoplasmic, but is also present in a subnuclear compartment. In a panel of tumor cells that express Bin1, the predominant localization of the molecule is in the subnuclear compartment.
Immunogen
recombinant polypeptide containing amino acids 189-398 of human Bin1.
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Storage Class
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Endocytic proteins in the regulation of nuclear signaling, transcription and tumorigenesis
Pyrzynska B, et al.
Molecular Oncology, 3(4), 321-338 (2009)
Laura Picas et al.
Nature communications, 5, 5647-5647 (2014-12-10)
Phosphoinositides play a central role in many physiological processes by assisting the recruitment of proteins to membranes through specific phosphoinositide-binding motifs. How this recruitment is coordinated in space and time is not well understood. Here we show that BIN1/M-Amphiphysin2, a
Accumulation of caveolin-3 protein is limited in damaged muscle in chicken muscular dystrophy
Matsumoto H, et al.
Comparative Biochemistry and Physiology. Part A, Molecular & Integrative Physiology, 157(1), 68-72 (2010)
Loss of heterozygosity and tumor suppressor activity of Bin1 in prostate carcinoma
Ge K, et al.
International Journal of Cancer. Journal International Du Cancer, 86(2), 155-161 (2000)
Bin1 SRC homology 3 domain acts as a scaffold for myofiber sarcomere assembly
Fernando P, et al.
The Journal of Biological Chemistry, 284(40), 27674-27686 (2009)
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