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- Table of Contents
Facts about Leupaxin.
Suppresses the integrin-induced tyrosine phosphorylation of paxillin (PXN). May play a crucial role as an adapter protein in the creation of the adhesion zone in osteoclasts.
Human | |
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Gene Name: | LPXN |
Uniprot: | O60711 |
Entrez: | 9404 |
Belongs to: |
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paxillin family |
LDLP; LDPL; leupaxin
Mass (kDA):
43.332 kDA
Human | |
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Location: | 11q12.1 |
Sequence: | 11; NC_000011.10 (58526871..58578239, complement) |
Macrophages, monocytes and osteoclasts (at protein level). Strongly expressed in cells and tissues of hematopoietic origin. Highest expression in lymphoid tissues such as spleen, lymph node, thymus and appendix and in the vascular smooth muscle. Lower levels in bone marrow and fetal liver. Also expressed in peripheral blood lymphocytes and a number of hematopoietic cell lines. Very low levels found in epithelial cell lines. Expressed in prostate cancer (PCa) cells and its expression intensity is directly linked to PCa progression.
Cytoplasm. Cell junction, focal adhesion. Nucleus. Cytoplasm, perinuclear region. Cell projection, podosome. Cell membrane. Shuttles between the cytoplasm and nucleus. Recruited to the cell membrane following B-cell antigen receptor (BCR) cross-linking in B-cells. Enhanced focal adhesion kinase activity (PTK2/FAK) attenuates its nuclear accumulation and limits its ability to enhance serum response factor (SRF)-dependent gene transcription. Targeting to focal adhesions is essential for its tyrosine phosphorylation in response to bombesin.
This article will help you find high affinity primary antibodies that can be used to analyze Leupaxin from a variety of cell types. This article will explain the benefits of using BosterBio Anti-Leupaxin/LPXNMarker and how to validate your antibody on WB or IHC. BosterBio antibodies have many benefits.
LPXN could be an oncogene that plays a role in some human cancers. The molecular mechanism behind this protein's function is not yet known. Nevertheless, studies have revealed that this protein may contribute to bladder cancer cell growth. In particular, studies of LPXN expression have shown that LPXN-overexpressing cells produce larger and heavier tumors and a higher Ki67 proliferation index. LPXN deficient cells showed the opposite effects in terms of the microvascular density (MVD), as well as the Ki67 proliferation index.
To use this gene as a marker in cancer research, it is essential to identify the cancer cells that express the gene. LXPN also promotes cell adhesion and migration in prostate cancer cells. LPXN regulates the actin binding protein caldesmon which may help to promote cancer cell proliferation. Moreover, LPXN regulates MMP-9, MMP-2, and integrin expression.
This gene has been used as a prognostic marker in cancer research. High expression was associated, for example in hypopharyngeal tumors, with poor prognosis. High FAK expression was associated to a shorter overall survival rate and a higher chance of progression in triple-negative breast carcinoma. In bladder cancer, LPXN was associated with poor prognosis, and was related to tumor size and stage.
The Anti-Leupaxin/LPXI Marker, which has recently been made a valuable tool in cancer research, is now available. LPXN participates in actin cytoskeletal restructuring, which is essential for cell movement. ERK is recruited by LPXN as it interacts with CaD. ERK phosphorylates CaD in l–CaD at S534 and S789, respectively, resulting in formation of dynamic actsin structures.
LPXN belongs to the paxillin family of proteins, which is known for their protein-protein interactions. LPXN first appeared in hematopoietic and other cells. Later, it was discovered that it is an important adapter proteins in osteoclasts. This helps to prevent their migration and resorptive capability. LPXN is also found within vascular smooth muscle cells. It regulates their contractile, migratory and migratory properties during vasculogenesis.
RNAi knockout of LPXN decreased its expression in DU 145 cells and PC-3 cells. After 72 hours, CaD was detected by the lysates. Immunoblotting with a caD-specific antibody revealed that CaD co-immunoprecipitated with LPXN. CaD was found at focal adhesion points.
Similarly, knockout mice without LPXN also showed a decrease in surface area. SilpxN knockdown cells maintained their round shape and no protrusions. In the same way, knockout cells showed reduced surface area and adhesion, compared to controls. Additionally, siLPXN-knockdown cells were unable attach to ECM without Lyn coexpression.
B cells have reported co-localization between LPXN (Lyn) and LPXN. After BCR ligation, LPXN and Lyn co-localization decreased by 15 to 30 minutes. It appears that LPXN and Lyn interact at the plasma membrane of B cells. LPXN and Lyn phosphorylation are likely induced by BCR ligation.
High-affinity primary antibodies are antibodies that bind specific antigens with high affinity. These antibodies are useful in many research applications. They can be used to detect and purify antigens and analyse living cells at the molecular scale. They can also be used to identify proteins that are involved in diseases. Primary antibodies are typically generated by using animal hosts. Some are further validated using protein arrays, while others are subject to knockout validation.
Monovalent antigens with a high affinity binding affinity can be used to produce high-affinity antibody. IgM-expressing B cells recognize NP specific antigens but are only partial in polyreactivity. This could be due in part to the lack IgD, which regulates and regulates B cell activation. IgD-deficient IgD-deficient cell might have a lower threshold for activation, and subsequent immune responses.
IgD deficiency causes delayed generation of high affinity IgM in mice, which can lead to prolonged autoimmune diabetic symptoms. The LPXN marker can be used to make high-affinity primary antibodies. IgD is necessary for the transition from primary autoreactive reactions to secondary antigen-specific antibodies responses. This marker can be used to produce IgM in mice from B cells.
LPXN-tagged LPXN antigens are useful tools for high-affinity antibody detection. These antigens are usually characterized by a high KD (KD), which refers to the rate atwhich antibodies and antigens interact. The affinity of the antibody increases with a decrease in KD.
This marker allows researchers the ability to identify multiple types of antigens simultaneously. Secondary antibodies are then extracted using immobilized serum proteins. These proteins can be used to perform a variety research applications. This method is sometimes called "Highly Cross-Adsorbed" because it is suitable for using multiple primary antibodies in one experiment. It is also more reliable and cheaper.
There are many options for secondary antibodies. The format of secondary antibodies you choose depends on where they were purchased, how you plan to use them and how long you plan to keep them. Invitrogen offers ready-to-use liquid secondary antibody solutions. The liquid secondary antibody should be kept at 20 degrees Celsius. Secondary antibodies should also be aliquoted before they are used. Repeated freezing and thawing can reduce their staining ability.
Valid WB/IHC images are crucial for antibodies to recognize their target. Validation involves proving that antibodies recognize their target and showing that they are suitable for IHC and WB analysis. Multiple bands in a WB or IHC image can indicate that further experiments are needed. A WB image of an Antigen should show a single band unless multiple bands are observed. This could indicate that different posttranslational modifications occurred or multiple bands exist. These should be investigated further for further details on the validity of the antibody.
In contrast, the datasheets for Companies 2-5 showed moderate levels of validation. However, neither company provided detailed information about their antibody validation processes. They did however provide some background on the target immunogen. Three of these companies included the entire target sequence, while the fourth only identified the phosphorylation region. Both datasheets provided at least one example where the antibody successfully identified its target in IHCs or WBs.
In addition to the WB, IHC, and IP techniques, knockout animals are an important tool in antibody validation. Knockout animals can be used to analyze antibodies that are unable to bind to their target in the native conformation. However, knockouts do have some limitations. In this case, knockouts are preferred. However, knockout animal studies have certain limitations. An IP experiment should be conducted to determine if the antibody is indeed specific.
During the validation process, antibodies should be tested on tissue microarrays and fixed cells with or without siRNA. These tests should only be performed on the target cells. The antibody should show a decrease in staining with increasing dilutions. A good antibody should be consistent with published literature in displaying a specific expression pattern.
WB and IHC data may not be complementary, but they can indicate whether an antibody is specific. WB is not recommended for IHC validation if WB and IHC are not comparable. To establish its accuracy, IHC data needs to be correlated in WB and ICC. The LPXN marker can be used to assess the specificity of antibodies.
PMID: 9565592 by Lipsky B.P., et al. Leupaxin is a novel LIM domain protein that forms a complex with PYK2.
PMID: 10604475 by Liu S., et al. Binding of paxillin to alpha4 integrins modifies integrin-dependent biological responses.