Src substrate cortactin Antibodies

Src substrate cortactin (CTTN)

Contributes to the organization of the actin cytoskeleton and cell shape (PubMed:21296879). Plays a role in the formation of lamellipodia and in cell migration.

Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density (By similarity).

Gene Information

Human
Gene Name:	CTTN
Uniprot:	Q14247
Entrez:	2017

Family

Belongs to:
No superfamily

Alternative Names

1110020L01Rik; Amplaxin; Cortactin; CTTN; ems1 sequence (mammary tumor and squamous cell carcinoma-associated (p80/85 srcsubstrate); EMS1; EMS1amplaxin; FLJ34459; Oncogene EMS1; src substrate cortactin

Molecular Weight

Mass (kDA):
61.586 kDA

Genomic Context

Human
Location:	11q13.3
Sequence:	11; NC_000011.10 (70398506..70436584)

Subcellular Localizations

Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, ruffle. Cell projection, dendrite. Cell projection. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, podosome. Cell junction. Cell junction, focal adhesion. Membrane, clathrin-coated pit. Cell projection, dendritic spine. Cytoplasm, cell cortex. Colocalizes transiently with PTK2/FAK1 at focal adhesions (By similarity). Associated with membrane ruffles and lamellipodia. In the presence of CTTNBP2NL, colocalizes with stress fibers (By similarity). In the presence of CTTNBP2, localizes at the c

Diseases

• Neoplasms
• Malignant Neoplasms
• Carcinoma
• Tissue Adhesions
• Neoplasm Metastasis
• Cell Invasion
• Malignant Squamous Cell Neoplasm
• Mammary Neoplasms
• Neoplasm Invasiveness
• Malignant Neoplasm Of Breast
• Metastatic Malignant Neoplasm To The Lymph Node
• Head And Neck Carcinoma
• Cell Transformation, Neoplastic

• Malignant Paraganglionic Neoplasm
• Tumor Progression
• Head And Neck Neoplasms
• Carcinogenesis
• Lymphatic Metastasis
• Laryngeal Neoplasm
• Adenocarcinoma

Interacting Proteins

• ARRB2
• ASAP1
• Cbll1
• DNM2
• EGFR

• HDAC6
• Kcnma1
• PTPN1
• WAS

Pathways

• Localization
• Cell Migration
• Cell Motility
• Endocytosis
• Cell Proliferation
• Cell Adhesion
• Cell Cycle
• Secretion
• Rna Interference
• Actin Nucleation
• Dna Amplification
• Pathogenesis
• Platelet Activation

• Spermatogenesis
• Transport
• Proteolysis
• Platelet Aggregation
• Anoikis
• Angiogenesis
• Cell Differentiation

PTMs

• Phosphorylation
• Cleavage
• Acetylation
• Dephosphorylation
• Biotinylation

• Deacetylation
• Nitration
• Geranylgeranylation
• Ribosylation
• Ubiquitination

Research Areas

• Cell Biology
• Cellular Markers

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/CTTN

The Best Uses Of The CTTN Marker

Using Steven Boster's CTTN Marker for biomolecular characterization has several advantages. Read on to learn more about the techniques to minimize the cross-linking intensity and optimize Boster Bio's high-quality lysate. Listed below are the main benefits of CTTN markers. Using these techniques will greatly improve your research and your studies. For more information, visit Boster Bio.

Techniques for reducing cross-linking intensity

DNA cross-linking is a common occurrence in all biological systems, and its detection is critical in determining the effectiveness of various molecular biology techniques. These techniques are used to manipulate genetic material and investigate disease processes. For this purpose, Boster Bio provides comprehensive technical resources, including blogs and disease information, as well as web-based digital tools and high-quality lysis buffers. These buffers ensure high-quality results and minimize the effects of cross-linking.

DNA is oxidized to form multiple bands, each corresponding to a specific DNA cross-link. The major bands correspond to oxoA-A and oxoA-T cross-links, respectively. In order to distinguish the minor bands from the major bands, it is essential to analyze multiple data points. If you are not sure what band is responsible for a specific cross-linking, consult the data table to determine the correct method.

Optimizing Boster Bio's high-quality lysate with protein A/G affinity beads

When preparing antibody-protein complexes for immunoprecipitation, it is important to understand the differences between magnetic and agarose beads. While the former offers more surface area, magnetic beads have a higher affinity for antibody molecules, making them better for processing low-volume samples. However, these beads are more expensive than agarose beads and are not recommended for large-scale projects. Regardless of the type of beads you use, be sure to conduct appropriate controls before submitting your sample to protein immunoprecipitation.

Protein A/G beads are coated with either a protein A or G antibody. Both types recognize antibodies and adsorb the protein complex from the lysate. Beads that recognize proteins that are unbound to the antibody support are eluted from the sample by boiling in glycine buffer, pH 2.6. To confirm that the beads have a high affinity for your antibody, perform SDS-PAGE analysis of the protein-coated beads. The binding profile of the beads is listed on the antibody data sheet.

The lysis buffer should be replaced with a sample of 70 to 100 ul. Then, you should add 70-100 mL of beads per sample. After the beads have eluted, keep the sample on ice. To avoid clumping, make sure the pipette tip is cut about 5 mm above the sample.

Before you start immunoprecipitation, you must pre-clear the sample with the antibody. Protein A/G beads are complex mixtures of proteins, lipids, carbohydrates, and nucleic acids. Nonspecific binding of these components can negatively affect the detection of immunoprecipitated targets. Therefore, pre-clearing the sample with protein A/G affinity beads is essential to maximize the efficiency of the immunoprecipitation process.

The purpose of agarose is to enhance the immunoprecipitation process by attaching antibody to a beaded support. Because of their high affinity, Protein A/G beads allow excellent immunoprecipitation results even with low volumes of beads. The binding capacity of the antibody is dependent on its Fc region. Therefore, Protein A/G beads should be used in IP experiments to isolate only specific immunoglobulins.

To prepare the agarose/Sepharose beads, follow the instructions for method A. First, you need to boil the IP sample using 2x Laemmli sample buffer. Next, add the cell lysate or antibody conjugate. Repeat the process twice to obtain the desired protein. A final gel will be obtained after a second wash step.