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Mouse Anti-CD2AP Recombinant Antibody (5F8) (CBMAB-BR083LY)

The product is antibody recognizes CD2AP. The antibody 5F8 immunoassay techniques such as: FC, IHC, WB.
See all CD2AP antibodies

Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
5F8
Antibody Isotype
IgG1
Application
FC: 1-3 μg/1x10 cells, IHC: 1:300-1:500 dilution, WB: 0.1-0.5 μg/ml

Basic Information

Immunogen
E. coli-derived human CD2AP recombinant protein (Position: K253-K337)
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1
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
Lyophilized
Preservative
0.05 mg sodium azide
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
CD2 associated protein
Introduction
CD2AP (CD2 Associated Protein) is a Protein Coding gene. Diseases associated with CD2AP include Focal Segmental Glomerulosclerosis 3 and Sporadic Idiopathic Steroid-Resistant Nephrotic Syndrome With Focal Segmental Hyalinosis. Among its related pathways are Primary Focal Segmental Glomerulosclerosis FSGS and Nephrin interactions. Gene Ontology (GO) annotations related to this gene include SH3 domain binding and structural constituent of cytoskeleton. An important paralog of this gene is SH3KBP1.
Entrez Gene ID
Human23607
Mouse12488
Rat316258
UniProt ID
HumanQ9Y5K6
MouseQ9JLQ0
RatF1LRS8
Alternative Names
CD2-associated protein; Adapter protein CMS; Cas ligand with multiple SH3 domains; CD2AP
Function
Seems to act as an adapter protein between membrane proteins and the actin cytoskeleton (PubMed:10339567).
In collaboration with CBLC, modulates the rate of RET turnover and may act as regulatory checkpoint that limits the potency of GDNF on neuronal survival. Controls CBLC function, converting it from an inhibitor to a promoter of RET degradation (By similarity).
May play a role in receptor clustering and cytoskeletal polarity in the junction between T-cell and antigen-presenting cell (By similarity).
May anchor the podocyte slit diaphragm to the actin cytoskeleton in renal glomerolus. Also required for cytokinesis (PubMed:15800069).
Plays a role in epithelial cell junctions formation (PubMed:22891260).
Biological Process
Actin filament organization Source: UniProtKB
Cell-cell adhesion Source: Ensembl
Cell cycle Source: UniProtKB-KW
Cell division Source: UniProtKB-KW
Negative regulation of small GTPase mediated signal transduction Source: UniProtKB
Negative regulation of transforming growth factor beta1 production Source: Ensembl
Positive regulation of protein localization to nucleus Source: Ensembl
Positive regulation of protein secretion Source: UniProtKB
Proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
Protein-containing complex assembly Source: ProtInc
Regulation of actin cytoskeleton reorganization Source: Ensembl
Regulation of receptor-mediated endocytosis Source: Ensembl
Signal transduction Source: ProtInc
Substrate-dependent cell migration, cell extension Source: ProtInc
Vesicle organization Source: Ensembl
Cellular Location
Cytoskeleton; Ruffle; Cell junction. Colocalizes with F-actin and BCAR1/p130Cas in membrane ruffles (PubMed:10339567). Located at podocyte slit diaphragm between podocyte foot processes (By similarity). During late anaphase and telophase, concentrates in the vicinity of the midzone microtubules and in the midbody in late telophase (PubMed:15800069).
Involvement in disease
Focal segmental glomerulosclerosis 3 (FSGS3): A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation.
PTM
Phosphorylated on tyrosine residues; probably by c-Abl, Fyn and c-Src.

Furusawa, K., Takasugi, T., Chiu, Y. W., Hori, Y., Tomita, T., Fukuda, M., & Hisanaga, S. I. (2019). CD2-associated protein (CD2AP) overexpression accelerates amyloid precursor protein (APP) transfer from early endosomes to the lysosomal degradation pathway. Journal of Biological Chemistry, 294(28), 10886-10899.

Tao, Q. Q., Chen, Y. C., & Wu, Z. Y. (2019). The role of CD2AP in the Pathogenesis of Alzheimer's Disease. Aging and disease, 10(4), 901.

Ha, T. S., & Ha, D. S. (2019). Ginseng total saponin attenuates podocyte apoptosis induced by diabetic conditions through the recovery of CD2-associated protein. Journal of medicinal food, 22(2), 170-177.

Tossidou, I., Teng, B., Worthmann, K., Müller-Deile, J., Jobst-Schwan, T., Kardinal, C., ... & Schiffer, M. (2019). Tyrosine phosphorylation of CD2AP affects stability of the slit diaphragm complex. Journal of the American Society of Nephrology, 30(7), 1220-1237.

Ojelade, S. A., Lee, T. V., Giagtzoglou, N., Yu, L., Ugur, B., Li, Y., ... & Shulman, J. M. (2019). cindr, the Drosophila homolog of the CD2AP Alzheimer’s disease risk gene, is required for synaptic transmission and proteostasis. Cell reports, 28(7), 1799-1813.

Takano, T., Bareke, E., Takeda, N., Aoudjit, L., Baldwin, C., Pisano, P., ... & Gupta, I. R. (2019). Recessive mutation in CD2AP causes focal segmental glomerulosclerosis in humans and mice. Kidney international, 95(1), 57-61.

Zhang, H., Zhang, C., Tang, H., Gao, S., Sun, F., Yang, Y., ... & Li, C. (2018). CD2‐Associated Protein Contributes to Hepatitis C, Virus Propagation and Steatosis by Disrupting Insulin Signaling. Hepatology, 68(5), 1710-1725.

Panni, S. (2018). CD2AP (CD2 associated protein). Atlas of Genetics and Cytogenetics in Oncology and Haematology.

Tsuji, K., Păunescu, T. G., Suleiman, H., Xie, D., Mamuya, F. A., Miner, J. H., & Lu, H. A. J. (2017). Re-characterization of the glomerulopathy in CD2AP deficient mice by high-resolution helium ion scanning microscopy. Scientific reports, 7(1), 1-13.

Saurus, P., Tolvanen, T. A., Lindfors, S., Kuusela, S., Holthöfer, H., Lehtonen, E., & Lehtonen, S. (2017). Inhibition of SHIP2 in CD2AP-deficient podocytes ameliorates reactive oxygen species generation but aggravates apoptosis. Scientific reports, 7(1), 1-14.

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

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We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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