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Validated All-in-One™ qPCR Primer for LCP2(NM_005565.4) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
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 comprised of three modular domains. The NH2-terminus contains an acidic region that includes a PEST domain and several tyrosine residues which 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.
Gene References into function
- Shb links SLP-76 and Vav with the CD3 complex in Jurkat T cells (SLP-76)
- SLP-76 is essential for NF-kappa B activation and lipid raft translocation of protein kinase C theta and the I kappa B kinase complex.
- SLP-76 is required for intracellular calcium ion mobilization in response to SDF-1alpha/CXCL12-induced prolonged activation of extracellular signal-related protein kinase in Jurkat T cells.
- SLP-76 is necessary for T cell receptor stimulation-induced polarization of the T cell's microtubule-organizing center, as it moves toward the interface of the T cell and antigen-presenting cell.
- Study provides the first data to address the mechanisms controlling SLP-76 transcription by providing evidence for several key cis-regulatory elements in the promoter region.
- the proline-rich domain in SLP-76 has a role in subcellular localization and T cell function
- Data suggest that SLP-76 may play a role in signaling pathways by interacting with the p85 subunit of phosphoinositide 3-kinase (PI3K).
- SLP-76 need not interact with SH3(PLC) to activate PLC-gamma1, and the P-I region of SLP-76 serves a structural role that is sequence-independent and is not directly related to protein-protein interactions
- Data show that the adaptor molecules LAT and SLP-76 are specifically targeted by Yersinia to inhibit T cell activation.
- TCR-induced association of Vav3 with SLP-76 is required for its membrane/IS localization and function
- the Lck binding region of SLP-76 is essential for T cell antigen receptor signaling and normal T cell development and function
- In T cells all SLP-76 proteins are in a approximately 400 kDa complex with the small adaptor protein Grb2-like adaptor protein Gads.
- findings show that retinoic acid(RA) induced the expression of SLP-76, which when co-expressed with an RA-induced receptor, c-FMS, enhanced RA-induced cell differentiation and G0 cell cycle arrest
- The costimulatory effect of CD6 is mediated through phosphorylation-dependent binding of a specific tyrosine residue, 662Y, in its cytoplasmic region to the adaptor SLP-76.
- The P-I region deletion disrupted Vav association and reduced SLP-76-associated kinase activity.
- The integrity of T-cell receptor signaling in vivo is sustained both by strong selection of SLP-76 for the Gads C-SH3 domain and by a capacity to buffer intrinsic crossreactivity.
- phosphorylation of the adaptor molecule SLP-76 is essential for recruitment of the exchange factor Vav leading to Ca(2+) flux and IL-2 production
- Required for activation of IL-2-inducible T cell kinase (ITK); furthermore, an ongoing physical interaction between SLP-76 and ITK is required to maintain ITK in an active conformation.
- study reports that T cell costimulation by the integrin VLA-4 (alpha4beta1) required SLP-76 domains implicated in microcluster assembly