Recombinant Human ANLN 293 Cell Lysate
Cat.No. : | ANLN-8845HCL |
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Description : | Antigen standard for anillin, actin binding protein (ANLN) is a lysate prepared from HEK293T cells transiently transfected with a TrueORF gene-carrying pCMV plasmid and then lysed in RIPA Buffer. Protein concentration was determined using a colorimetric assay. The antigen control carries a C-terminal Myc/DDK tag for detection. |
Source : | HEK 293 cells |
Species : | Human |
Components : | This product includes 3 vials: 1 vial of gene-specific cell lysate, 1 vial of control vector cell lysate, and 1 vial of loading buffer. Each lysate vial contains 0.1 mg lysate in 0.1 ml (1 mg/ml) of RIPA Buffer (50 mM Tris-HCl pH7.5, 250 mM NaCl, 5 mM EDTA, 50 mM NaF, 1% NP40). The loading buffer vial contains 0.5 ml 2X SDS Loading Buffer (125 mM Tris-Cl, pH6.8, 10% glycerol, 4% SDS, 0.002% Bromophenol blue, 5% beta-mercaptoethanol). |
Size : | 0.1 mg |
Storage Instruction : | Store at -80°C. Minimize freeze-thaw cycles. After addition of 2X SDS Loading Buffer, the lysates can be stored at -20°C. Product is guaranteed 6 months from the date of shipment. |
Applications : | ELISA, WB, IP. WB: Mix equal volume of lysates with 2X SDS Loading Buffer. Boil the mixture for 10 min before loading (for membrane protein lysates, incubate the mixture at room temperature for 30 min). Load 5 ug lysate per lane. |
Gene Name : | ANLN anillin, actin binding protein [ Homo sapiens ] |
Official Symbol : | ANLN |
Synonyms : | ANLN; anillin, actin binding protein; anillin (Drosophila Scraps homolog), actin binding protein , anillin, actin binding protein (scraps homolog, Drosophila); actin-binding protein anillin; ANILLIN; scra; Scraps; DKFZp779A055; |
Gene ID : | 54443 |
mRNA Refseq : | NM_018685 |
Protein Refseq : | NP_061155 |
UniProt ID : | Q9NQW6 |
Chromosome Location : | 7p15-p14 |
Function : | actin binding; |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (17)
Ask a questionThere have been reports of genetic mutations in the ANLN gene that are associated with certain diseases. For example, mutations in ANLN have been linked to certain forms of breast cancer, lung adenocarcinoma, and congenital heart disease. However, these mutations are relatively rare and further research is needed to fully understand their functional impact and significance in disease development.
In addition to its involvement in cell division and migration, ANLN protein may have connections to other cellular processes. It has been suggested to participate in the regulation of cell adhesion, cell cycle progression, and DNA damage response. However, more research is necessary to fully understand ANLN's role in these processes and its underlying mechanisms.
ANLN protein has been investigated as a potential biomarker in cancer diagnosis. Studies have shown that increased ANLN expression is associated with various cancers and can be detected in blood and tumor tissues of affected individuals. However, further research is needed to determine its specificity and sensitivity as a diagnostic biomarker, and its utility may vary depending on the cancer type.
Yes, ANLN has been implicated in cell migration and invasion, particularly in the context of cancer metastasis. ANLN promotes cell migration by modulating actin dynamics and cytoskeletal rearrangements. It interacts with focal adhesion proteins and signaling molecules, such as RhoA, Rac1, and Cdc42, to regulate cell migration and adhesion. ANLN also plays a role in epithelial-mesenchymal transition (EMT), a process in which epithelial cells acquire a more migratory and invasive phenotype. Dysregulation of ANLN expression or function can lead to enhanced cell migration and invasion, contributing to tumor metastasis.
Yes, ANLN protein can interact with a variety of other proteins to form complexes that are involved in various cellular processes. For example, ANLN interacts with RhoA and myosin to facilitate actin cytoskeleton organization during cytokinesis. ANLN has also been shown to interact with components of the Hippo signaling pathway, such as YAP and LATS, to regulate cell division and cell growth.
Currently, there are no specific drugs or therapies targeting ANLN protein. However, given its involvement in various diseases, ANLN has the potential to be a therapeutic target in the future. Developing specific inhibitors or modulators of ANLN's function could potentially be explored for therapeutic purposes. Additionally, targeting signaling pathways that regulate ANLN, such as the Hippo pathway, may indirectly influence ANLN activity and could be a potential avenue for drug development.
The regulation of ANLN protein involves multiple mechanisms. It is transcriptionally regulated by various transcription factors and signaling pathways, such as the Hippo signaling pathway. Post-translational modifications, including phosphorylation and ubiquitination, also play a role in controlling ANLN's activity and stability. Additionally, interactions with other proteins, such as RhoA and myosin, contribute to the regulation of ANLN during cytokinesis.
Yes, ANLN protein is highly conserved across different species. It is found in a wide range of organisms, including humans, mice, fruit flies, and plants. The ANLN gene and its protein sequence have been shown to be highly conserved, indicating its importance and evolutionary significance.
ANLN protein consists of several functional domains. It contains an N-terminal domain that interacts with F-actin and bundles actin filaments. The central region of ANLN contains multiple anillin repeats, which are important for protein-protein interactions and binding to myosin. At the C-terminus, there is a Src homology 3 (SH3) domain that mediates binding to various signaling molecules.
ANLN protein is expressed in various tissues throughout the body. Its expression is often observed in dividing cells during embryonic development and tissues with high proliferative capacity, such as the epithelial linings of organs like the intestines and skin.
Yes, ANLN protein has been implicated in several diseases. Dysregulated expression or dysfunction of ANLN has been linked to various types of cancer, including breast, lung, pancreatic, and bladder cancer. Additionally, ANLN abnormalities have been observed in certain kidney disorders and neurological conditions like Alzheimer's disease.
es, ANLN expression and function can be regulated by various signaling pathways. One of the key pathways that regulate ANLN is the Hippo signaling pathway. The Hippo pathway controls organ development, tissue homeostasis, and tumor suppression. Activation of the Hippo pathway leads to phosphorylation and inactivation of the transcriptional co-activator Yes-associated protein (YAP) and its paralog transcriptional co-activator with PDZ-binding motif (TAZ). In its active form, YAP/TAZ translocates to the nucleus and interacts with TEA domain (TEAD) transcription factors to promote ANLN transcription. Other signaling pathways, such as the Rho GTPase pathway, also regulate ANLN function by modulating its interactions with actin cytoskeleton components and other binding partners.
Yes, abnormal ANLN expression or function has been implicated in various diseases and conditions. In cancer, increased ANLN expression has been observed in several types of tumors and is associated with tumor progression and poor prognosis. ANLN has also been implicated in cardiovascular diseases, such as atherosclerosis and cardiac hypertrophy. Additionally, ANLN dysfunction has been linked to neurodegenerative disorders, such as Alzheimer's disease and Parkinson's disease. However, further research is needed to fully understand the role of ANLN in these conditions and its potential as a therapeutic target.
ANLN has been implicated in development and tissue regeneration processes. During embryonic development, ANLN is crucial for proper organ formation and embryogenesis. Knockdown or disruption of ANLN in animal models has been shown to cause defects in organ development, such as cardiac and neural tube defects. ANLN is also involved in tissue regeneration, particularly in regenerative tissues, such as the liver and skin. In these contexts, ANLN promotes cell proliferation and tissue repair following injury. Further studies are needed to elucidate the exact mechanisms by which ANLN participates in these processes.
Numerous research studies have examined ANLN and its significance in different biological processes and diseases. For instance, studies have highlighted ANLN's role in promoting cell division, regulating cell migration, and modulating cancer progression. Researchers have also investigated ANLN as a potential diagnostic and prognostic marker in cancer, with some studies suggesting its utility in predicting patient outcomes and treatment response.
Currently, there are no approved drugs specifically targeting ANLN protein. However, ongoing research on the functional significance of ANLN may lead to therapeutic development or the identification of potential drug targets in the future.
While ANLN's primary role is in cytokinesis and cell division, recent research suggests that it may also have functions outside of these processes. Studies have indicated that ANLN is involved in cell migration, invasion, and epithelial-mesenchymal transition, which are important aspects of cancer metastasis. Additionally, ANLN has been implicated in maintaining cell shape and polarity in certain tissues.
Customer Reviews (4)
Write a reviewBeyond its superb performance in Western blotting, the ANLN protein has also proven invaluable in protein electron microscopy structure analysis.
Its stability and purity make it an ideal candidate for studying protein structures at a high resolution, providing crucial insights into the organization and function of the ANLN protein.
I highly recommend the ANLN protein for its exceptional performance in Western blot analysis.
It has consistently demonstrated outstanding results, consistently producing clear and sharp bands, allowing for accurate and reliable protein detection and quantification.
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