Leupaxin (N-terminal region) Blocking Peptide
€155.00
In stock
SKU
ECM-LX4535
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.
Sequence: Leupaxin (N-terminal) synthetic peptide corresponding to amino acid residues in the N-terminal region of human leupaxin. This peptide sequence is highly conserved in rat and mouse leupaxin, and has low homology to other paxillin family proteins.
Specificity: The peptide is specifically recognized by anti-Leupaxin (N-terminal region) antibody (LP4531) in ELISA, and has been shown to block the reactivity of LP4531 during Western blot. In addition, the peptide is recommended for use in blocking LP4531 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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.
Sequence: Leupaxin (N-terminal) synthetic peptide corresponding to amino acid residues in the N-terminal region of human leupaxin. This peptide sequence is highly conserved in rat and mouse leupaxin, and has low homology to other paxillin family proteins.
Specificity: The peptide is specifically recognized by anti-Leupaxin (N-terminal region) antibody (LP4531) in ELISA, and has been shown to block the reactivity of LP4531 during Western blot. In addition, the peptide is recommended for use in blocking LP4531 reactivity in immunocytochemistry.
Buffer/Storage:
Blocking Peptide is supplied in 50µl phosphate-buffered saline and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
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