Monoclonal Anti-Leupaxin antibody produced in mouse

Monoclonal Anti-Leupaxin (mouse IgM isotype) is derived from the hybridoma Leu133 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a peptide corresponding to a sequence at the N-terminus human Leupaxin conjugated to KLH. Leupaxin is a LIM (Lin11, Isl-1 and Mec-3) domain phosphotyrosine protein preferentially expressed in lymphoid tissues and hematopoietic cells. Leupaxin shares homology with the focal adhesion protein paxillin, in the LIM and LD (leucine/aspartate repeat) protein interaction domains. Leupaxin is expressed in cell types that lack FAK, such as human macrophages.

peptide corresponding to a sequence at the N-terminus human Leupaxin, conjugated to KLH. The corresponding sequence is identical in human leupaxin 1 and 2 isoforms.

Monoclonal Anti-Leupaxin antibody produced in mouse has been used in immunoblotting and immunocytochemistry.

Leupaxin LIM domains have been shown to mediate localization to focal contacts and LD motifs have been implicated in focal adhesion kinase (FAK) and vinculin binding, resulting in the localization of FAK to focal adhesions. Leupaxin and protein tyrosine kinase 2 β (PYK2) are both preferentially expressed in leukocytes where they regulate cell type-specific signaling complex. Leupaxin can form a complex with PYK2 and PTP-PEST in several cell types including monocytes and osteoclasts and in prostate cancer cells. In osteoclasts, leupaxin has been suggested to be a critical nucleating component of the osteoclast podosomal signaling complex in the adhesion zone. Leupaxin is expressed in prostate cancer and is thought to play a role in adhesion and invasion of prostate carcinoma cells.

Solution containing 15 mM sodium azide.

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