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Mouse Anti-BIN1 Recombinant Antibody (CBYY-1942) (CBMAB-2291-YY)

This product is mouse antibody that recognizes BIN1. The antibody CBYY-1942 can be used for immunoassay techniques such as: Dot
See all BIN1 antibodies

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
CBYY-1942
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, ELISA, IHC-P

Basic Information

Immunogen
Amino acids 421-520 mapping within an internal region of Amphiphysin II of human origin.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
Bridging Integrator 1
Introduction
This gene encodes several isoforMouse of a nucleocytoplasmic adaptor protein, one of which was initially identified as a MYC-interacting protein with features of a tumor suppressor. IsoforMouse that are expressed in the central nervous system may be involved in synaptic vesicle endocytosis and may interact with dynamin, synaptojanin, endophilin, and clathrin. IsoforMouse that are expressed in muscle and ubiquitously expressed isoforMouse localize to the cytoplasm and nucleus and activate a caspase-independent apoptotic process. Studies in mouse suggest that this gene plays an important role in cardiac muscle development. Alternate splicing of the gene results in several transcript variants encoding different isoforMouse. Aberrant splice variants expressed in tumor cell lines have also been described.
Entrez Gene ID
UniProt ID
Alternative Names
Bridging Integrator 1; Amphiphysin II; Box-Dependent Myc-Interacting Protein 1; Amphiphysin-Like Protein; AMPHL; Box Dependant MYC Interacting Protein 1;
Function
Is a key player in the control of plasma membrane curvature, membrane shaping and membrane remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling (PubMed:24755653).
Is a negative regulator of endocytosis (By similarity).
Is also involved in the regulation of intracellular vesicles sorting, modulation of BACE1 trafficking and the control of amyloid-beta production (PubMed:27179792).
In neuronal circuits, endocytosis regulation may influence the internalization of PHF-tau aggregates (By similarity).
May be involved in the regulation of MYC activity and the control cell proliferation (PubMed:8782822).
Has actin bundling activity and stabilizes actin filaments against depolymerization in vitro (PubMed:28893863).
Biological Process
Cytoskeleton organization Source: ARUK-UCL
Endocytosis Source: ARUK-UCL
Endosome to lysosome transport Source: ARUK-UCL
Lipid tube assembly Source: Alzheimers_University_of_Toronto
Membrane organization Source: Reactome
Negative regulation of amyloid-beta formation Source: ARUK-UCL
Negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process Source: ARUK-UCL
Negative regulation of calcium ion transmembrane transport via high voltage-gated calcium channel Source: ARUK-UCL
Negative regulation of potassium ion transmembrane transport Source: ARUK-UCL
Negative regulation of ventricular cardiac muscle cell action potential Source: ARUK-UCL
Nucleus localization Source: Ensembl
Nucleus organization Source: WormBase
Positive regulation of actin filament polymerization Source: ARUK-UCL
Positive regulation of apoptotic process Source: AgBase
Positive regulation of astrocyte differentiation Source: Alzheimers_University_of_Toronto
Regulation of cell cycle arrest Source: Alzheimers_University_of_Toronto
Regulation of endocytosis Source: InterPro
Regulation of heart rate by cardiac conduction Source: ARUK-UCL
Regulation of neuron differentiation Source: Alzheimers_University_of_Toronto
T-tubule organization Source: UniProtKB
Viral process Source: UniProtKB-KW
Cellular Location
Isoform BIN1: Nucleus; T-tubule; Cytoplasm; Endosome
Isoform IIA: Cytoplasm
Involvement in disease
Myopathy, centronuclear, 2 (CNM2): A congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers.
BIN1 mutations have been found in families segregating autosomal dominant centronuclear myopathy. Patients show adult-onset, mildly progressive muscle weakness affecting selected proximal muscles and all distal muscles of the lower limbs.
PTM
Phosphorylated by protein kinase C.

Hu, H., Tan, L., Bi, Y. L., Xu, W., Tan, L., Shen, X. N., ... & Yu, J. T. (2021). Association between methylation of BIN1 promoter in peripheral blood and preclinical Alzheimer’s disease. Translational psychiatry, 11(1), 1-13.

Glennon, E. B., Lau, D. H., Gabriele, R. M., Taylor, M. F., Troakes, C., Opie-Martin, S., ... & Noble, W. (2020). Bridging integrator 1 protein loss in Alzheimer’s disease promotes synaptic tau accumulation and disrupts tau release. Brain communications, 2(1), fcaa011.

Gao, P., Ye, L., Cheng, H., & Li, H. (2020). The Mechanistic Role of Bridging Integrator 1 (BIN1) in Alzheimer’s Disease. Cellular and Molecular Neurobiology, 1-10.

Wang, J., Liu, T., Wang, M., Lv, W., Wang, Y., Jia, Y., ... & Liu, L. (2020). SRSF1‐dependent alternative splicing attenuates BIN1 expression in non–small cell lung cancer. Journal of cellular biochemistry, 121(2), 946-953.

Zheng, J., Wang, J., Jia, Y., Liu, T., Duan, Y., Liang, X., & Liu, L. (2019). microRNA‐211 promotes proliferation, migration, and invasion ability of oral squamous cell carcinoma cells via targeting the bridging integrator 1 protein. Journal of cellular biochemistry, 120(3), 4644-4653.

Glennon, E. B., Lau, D. H., Gabriele, R. M., Taylor, M. F., Troakes, C., Elliott, C., ... & Noble, W. (2019). Loss of the Alzheimer’s-linked bridging integrator 1 (BIN1) protein affects synaptic structure and disrupts tau localisation and release. bioRxiv, 646406.

Franzmeier, N., Rubinski, A., Neitzel, J., & Ewers, M. (2019). The BIN1 rs744373 SNP is associated with increased tau-PET levels and impaired memory. Nature communications, 10(1), 1-12.

Crotti, A., Sait, H. R., McAvoy, K. M., Estrada, K., Ergun, A., Szak, S., ... & Ransohoff, R. M. (2019). BIN1 favors the spreading of Tau via extracellular vesicles. Scientific reports, 9(1), 1-20.

Pinali, C., Malik, N., Davenport, J. B., Allan, L. J., Murfitt, L., Iqbal, M. M., ... & Kitmitto, A. (2017). Post‐myocardial infarction t‐tubules form enlarged branched structures with dysregulation of junctophilin‐2 and bridging integrator 1 (BIN‐1). Journal of the American Heart Association, 6(5), e004834.

Malki, I., Cantrelle, F. X., Sottejeau, Y., Lippens, G., Lambert, J. C., & Landrieu, I. (2017). Regulation of the interaction between the neuronal BIN 1 isoform 1 and Tau proteins–role of the SH 3 domain. The FEBS journal, 284(19), 3218-3229.

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For research use only. Not intended for any clinical use.

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