SLP

SLP may refer to:

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Fujifilm

Fujifilm Holdings Corporation, (富士フイルム株式会社, Fujifuirumu Kabushiki-kaisha), better known as Fujifilm or simply Fuji, is a Japanese multinational photography and imaging company headquartered in Tokyo.

Fujifilm's principal activities are the development, production, sale and servicing of business document solutions, medical imaging and diagnostics equipment, cosmetics, optical films for flat panel displays, optical devices, photocopiers and printers, digital cameras, color film, color paper, photofinishing equipment, photofinishing chemicals, graphic arts equipment and materials.

History

20th century

Fuji Photo Film Co., Ltd. was established in 1934 with the aim of being the first Japanese producer of photographic films. Over the following 10 years, the company produced photographic films, motion-picture films and X-ray films. In the 1940s, Fuji Photo entered the optical glasses, lenses and equipment markets. After the Second World War, Fuji Photo diversified, penetrating the medical (X-ray diagnosis), printing, electronic imaging and magnetic materials fields. In 1962, Fuji Photo and U.K.-based Rank Xerox Limited (now Xerox Limited) launched Fuji Xerox Co., Ltd. through a joint venture.

Lymphocyte cytosolic protein 2

Lymphocyte cytosolic protein 2 (SH2 domain containing leukocyte protein of 76kDa), also known as LCP2 or SLP-76, is a gene that encodes a signal-transducing adaptor protein.

Structure

No full structure for SLP-76 has been solved. The PDB file 1H3H depicts the SH3 domain of GRAP2 in complex with an RSTK-containing peptide representing residues 226-235 of SLP-76.

Function

SLP-76 was originally identified as a substrate of the ZAP-70 protein tyrosine kinase following T cell receptor (TCR) ligation in the leukemic T cell line Jurkat. The SLP-76 locus has been localized to human chromosome 5q33 and the gene structure has been partially characterized in mice. The human and murine cDNAs both encode 533 amino acid proteins that are 72% identical and composed of three modular domains. The NH2-terminus contains an acidic region that includes a PEST domain and several tyrosine residues that are phosphorylated following TCR ligation. SLP-76 also contains a central proline-rich domain and a COOH-terminal SH2 domain. A number of additional proteins have been identified that associate with SLP-76 both constitutively and inducibly following receptor ligation, supporting the notion that SLP-76 functions as an adaptor or scaffold protein. Studies using SLP-76-deficient T cell lines or mice have provided strong evidence that SLP-76 plays a positive role in promoting T cell development and activation as well as mast cell and platelet function.