LASP1 Antibodies

LIM and SH3 domain protein 1 (LASP1)

Plays an important role in the regulation of dynamic actin-based, cytoskeletal actions. Agonist-dependent changes in LASP1 phosphorylation can also function to modulate actin-associated ion transport activities, not just in the parietal cell but also in some other F-actin-rich secretory epithelial cell types (By similarity).

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Gene Information

Human
Gene Name:	LASP1
Uniprot:	Q14847
Entrez:	3927

Family

Belongs to:
No superfamily

Alternative Names

LASP-1; LIM and SH3 domain protein 1; LIM and SH3 protein 1; Metastatic lymph node gene 50 protein; MLN 50; MLN50Lasp-1

Molecular Weight

Mass (kDA):
29.717 kDA

Genomic Context

Human
Location:	17q12
Sequence:	17; NC_000017.11 (38869859..38921770)

Subcellular Localizations

Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Associated with the F-actin rich cortical cytoskeleton.

Diseases

• Malignant Neoplasms
• Neoplasms
• Tissue Adhesions
• Malignant Neoplasm Of Breast
• Mammary Neoplasms
• Neoplasm Metastasis
• Carcinoma
• Cell Transformation, Neoplastic
• Cell Invasion
• Neoplasm Invasiveness
• Colorectal Cancer
• Colorectal Neoplasms

• Liver Neoplasms
• Malignant Neoplasm Of Ovary
• Ovarian Neoplasm
• Liver Carcinoma
• Lipoma
• Nervousness
• Malignant Neoplasm Of Prostate

Interacting Proteins

• ARID5A
• CYSRT1
• FXR2
• GOLGA2
• KRTAP4-2

• LPP
• LZTS2
• MDFI
• PSMA3
• REL

• RHOXF2
• SH2D2A
• SPRY2
• TCF4
• THAP1

• TJP2
• TRIM27
• TRIP13
• ZBTB9
• ZC2HC1A

• ZDHHC17
• ZYX

Pathways

• Cell Migration
• Localization
• Cell Motility
• Cell Proliferation
• Cell Growth
• Cell Cycle
• Wound Healing
• Secretion
• Pathogenesis
• Rna Interference
• Transport
• Protein Phosphorylation
• Cell Adhesion

• Dna Hypermethylation
• Regulation Of Signal Transduction
• Platelet Activation
• Mammary Gland Development
• Chondrocyte Differentiation
• Podosome Assembly
• Cell Division

PTMs

• Phosphorylation

• Methylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/LASP1

Boster Bio - Best Uses Of The LASP1 Marker

There are many reasons why you should improve your research. Boster Bio optimization tips will help you determine the most efficient method for doing this. Troubleshooting guides can help you determine the cause of problems and ways to address them. Each researcher has had to deal with a couple of issues during their research. However, the most effective methods can eliminate the majority of these. This article will explain the most frequently encountered problems and the solutions.

Nonmalignant NSCLS tissue detected

The LASP1 marker was used to identify benign NSLCC tissue. It has been proven that Lasp1 overexpression is linked to larger tumor sizes, TNM stage, and regional lymph node metastasis. Furthermore, the overexpression of Lasp1 also predicted poor prognosis for NSCLC patients. This protein is possibly an upstream regulator for the FAK/AKT signaling pathway that facilitates the proliferation of NSCLC cells by phosphorylating FAK (397).

Normal lung tissues that expressed Lasp1 did not show any expression, but there were high levels in the cytoplasm of NSCLC cancers. In a study of 68 cases of non-cancerous lung tissue, the positive ratio was 14.7%. This was significantly lower than the 48.4 percent positive ratio found in NSCLC tissue. Nonmalignant tissue that expressed positive levels of Lasp1 was associated with tumor size, stage TNM lymph node metastasis, stage TNM and the size of the tumor. However it was not associated with lung adenocarcinoma.

Despite this high sensitivity , the PPV/NPV of AD at the same prevalence was only 15 and 96%, respectively. The high levels of PPV/NPV could be due to a higher rate of growth of the tumor, or the presence of stromal inflammation. The PPV/NPV ratios were calculated for the three biomarkers and the results were analyzed using SPSS version 22.0 for Windows.

Plasma contains a wide range of expression of the LASP1. LASP1 expression was found in blood serum samples that were higher than in serum from healthy subjects. Therefore, LASP1 could be used as a marker for nonmalignant NSCLS. However, it hasn't yet made it into clinical use. To prove its clinical efficacy, further research is needed. Its utility as a marker can aid in the development of disease classifiers.

Lung cancer detection

We have shown that LASP1 is an observable marker for lung cancer cells using an assay of gene expression. We used human lung epithelial cell BEAS-2B and non-small cell lung cancer (NSCLC) cell lines. Both cells were grown in Dulbecco's Modified Eagle's Medium (DMEM) supplemented with 10 percent bovine fetal serum.

To investigate the interaction between LASP1 and FAK, Wang et al. utilized an anti-F-actin antigen that has a partial homology to the LASP1 sequence. Although this is not conclusive it suggests that FAK and LASP1 could interact. Further research is required to confirm the interactions. In the meantime it appears that LASP1 and FAK are able to co-localize in focal adhesions.

LASP-1 is involved in a variety biological functions in a variety of tissues. This includes cell growth and signal transduction. It is found in numerous human cancers, including colorectal and lung. It may be a biomarker to predict the development of cancer , as it promotes cell growth, migration, and invasion in tumors. The research is still ongoing so keep an eye out for more information!

LASP1 is an essential part of the TGF-b1/Smad/Snail pathway, which affects the nuclear distribution of key signal molecules. It could be a target for drug discovery in the future. LASP1 is a promising indicator to detect lung cancer. It is a useful diagnostic tool and an effective treatment option.

LASP-1 promoter region was markedly amplified in SOX9-immunoprecipitated chromatins, but was absent in controls immunoprecipitated with control IgG. Based on the interaction between probes and nuclear extracts, EMSA revealed a band of DNA/protein with expected mobility. Biotin-labeled probes improved the interaction, compared with negative control (NCI-1650) cells.

LASP1 has been identified as an important factor in the onset and progress of lung cancers other than non-small cell. However the mechanism for this is not well understood. Although the LASP1 gene promotes aggressiveness and the growth of NSCLC However, it isn't evident how it is managed and how it is connected to miR-29a. After transfection of NSCLC tissues and cells with WT-LASP1-3'UTR vectors or MTLASS-LAS vectors LASP1 gene expression was increased.

The detection of the Smad/Snail signaling pathway

A Smad/Snail marker can be found as an antibody. This antibody can be used to determine whether the pathway is active in a particular cell. The antibody is available from Proteintech Group Inc. in the ratio 1:100. The secondary antibody is a peroxidase-conjugated goat anti-rabbit or goat anti-mouse.

The TGF-b1-induced EMT transformation is crucial inause it is linked to the Smad/Snail pathways. By controlling the Smad/Snail signaling pathway, LASP1 enhances EMT. LASP1 overexpression increases the nuclear Snail1. Overexpression of LASP1 leads to changes in the expression of E-cadherin and could be a potential drug target in lung cancer.

The LASP1 gene regulates Smad2 and Smad7. Both are essential for epithelial function and differentiation. LASP1 is also involved in the phosphorylation process of Smad proteins through TGFb1. The overexpression of LASP1 hinders this process, and can increase the activity of Smad2/3. It is not known what LASP1 does in the Smad/Snail pathway of signaling.

The LASP1 gene is involved in the regulation of Smad2/3, Smad1/5, and Snail1. These proteins are vital for cell growth and survival. They are also needed to discover the regulatory system for Smads-mediated signals. These proteins are vital for normal development and healthy aging So, identifying their function requires careful research.

The LASP1 gene is highly expressed in tumors, and is regarded as a novel biomarker for tumor metastasis. If LASP1 can be used to detect cancerous cells and the corresponding treatment regimens remain to be established. The results of the study are encouraging and will help cancer researchers optimize their treatment plans and develop more effective treatment strategies.

The detection of EMT markers

Detection of EMT markers is a promising tool to better understand the biology behind tumors. The invasive characteristics of some cancers are due to their expression of EMT markers. These cells often show stem-like characteristics. In addition to finding EMT in cancer cells, LB can help monitor the behavior of tumors. It is particularly helpful for lung cancer that is typically detected in the late stages which makes it difficult to use traditional biopsies to determine the prognosis of the disease.

Different tissues have different genetic backgrounds, which can make it difficult to express EMT markers. The application of this test has allowed researchers to find EMT markers in tumors without having to undergo extensive, time-consuming and expensive tissue culture. It has been confirmed in multiple human cancers, including those with multiple malignancies as well as fibrosis. Boster Bio's detection of EMT markers is an important step in understanding the nature and behavior of tumors.

Detection of EMT markers using the Boster Bio kit can accurately discern the type of cancer from the normal. While many studies have looked into the role of EMT in the development resistance to targeted treatments in the past its precise role remains unclear. The method is based on the sensitivity-specificity test. This method is extremely precise as the results show. The procedure is fast and accurate, and is compatible with many cancer types.

Methods of detecting molecule EMT can also help scientists identify specific types of cells that undergo this process. Western blotting and immunofluorescent cell staining can identify molecular markers. EMT causes epithelial cells in the body to express less epithelial markers, whereas mesenchymal markers must be expressed by cells that have been promoted by EMT. Actin must be stained onto the cells, resulting in an extended phenotype of mesenchymal cells.

These results are encouraging. The AdnaTest BreastCancerTM breast cancer assay is enriched with CTCs in five ml of blood. It also analyses ALDh2 and EMT markers, HER2, and actin. The AdnaWash buffer permits the proper differentiation of tumor stem cells as well as EMT markers. It also confirms a sensitivity rate of 80 percent when tested on healthy donors.