Anti-Leupaxin (N-terminal region) Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | O60711 |
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Reactivity | Bovine |
Host | Rabbit |
Clonality | Rabbit Polyclonal |
Isotype | IgG |
Calculated MW | 43332 Da |
Gene ID | 9404 |
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Other Names | Paxillin |
Target/Specificity | The paxillin family of LIM domain-containing proteins includes paxillin, Hic-5, and leupaxin. Similar to other family members, leupaxin is composed of multiple functional modules, including leucine and aspartate motifs and LIM domains. These domains suggest that leupaxin is a molecular adaptor that may be important for integrin-mediated cell signaling. Leupaxin was identified in leukocytes, and has been shown to be expressed in non-hematopoietic lineage cells, including vascular smooth muscle cells and certain cancer cells. In prostate cancer cells, leupaxin expression intensity is directly linked to cancer progression. Leupaxin localizes to the podosomal signaling complex in murine osteoclasts where it may be important for rearrangement of cytoskeletal components. The function of leupaxin in regulating the cytoskeleton may involve protein-protein interactions between leupaxin and focal adhesion proteins, such as Pyk2, FAK, Src, Lyn, and PTP-PEST. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | Anti-Leupaxin (N-terminal region) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Shipping | Blue Ice |

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Background
The paxillin family of LIM domain-containing proteins includes paxillin, Hic-5, and leupaxin. Similar to other family members, leupaxin is composed of multiple functional modules, including leucine and aspartate motifs and LIM domains. These domains suggest that leupaxin is a molecular adaptor that may be important for integrin-mediated cell signaling. Leupaxin was identified in leukocytes, and has been shown to be expressed in non-hematopoietic lineage cells, including vascular smooth muscle cells and certain cancer cells. In prostate cancer cells, leupaxin expression intensity is directly linked to cancer progression. Leupaxin localizes to the podosomal signaling complex in murine osteoclasts where it may be important for rearrangement of cytoskeletal components. The function of leupaxin in regulating the cytoskeleton may involve protein-protein interactions between leupaxin and focal adhesion proteins, such as Pyk2, FAK, Src, Lyn, and PTP-PEST.

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