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The protein encoded by RAG1 is involved in activation of immunoglobulin V-D-J recombination. De plus, nous expédions RAG1 Kits (32) et RAG1 Anticorps (30) et beaucoup plus de produits pour cette protéine.
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Results confirm that Rag-1 is necessary for the generation of lymphocytes in pigs, and Rag-1-deficient piglets exhibit a T and B cell deficient severe combined immune deficiency(T-B-SCID (Montrer PRKDC Protéines)) phenotype similar to that of rodents and humans.
Piglets with biallelic mutations in either RAG1 or RAG2 (Montrer RAG2 Protéines) exhibit hypoplasia of immune organs, fail to perform V(D)J rearrangement, and lose mature B and T cells.
the ability of the RAG nuclease (Montrer DCLRE1C Protéines) to minimize the risks of genome disruption by coupling the breakage and repair steps of the V(D)J reaction. This implies that the RAG genes, derived from an ancient transposon, have undergone strong selective pressure to prohibit transposition in favor of promoting controlled DNA end joining in cis (Montrer CISH Protéines) by the ubiquitous DNA damage response and DNA repair machineries.
Leaky SCID (Montrer PRKDC Protéines) can be caused by hypomorphic mutations in RAG1 and RAG2 (Montrer RAG2 Protéines) that result in only partial loss of enzymatic function of the proteins respectively encoded by these genes.
We report two siblings with SCID (Montrer PRKDC Protéines) and an atypical phenotype of osteopetrosis (OP (Montrer CSF1 Protéines)). A biallelic microdeletion encompassing the 5' region of TRAF6 (Montrer TRAF6 Protéines), RAG1 and RAG2 (Montrer RAG2 Protéines) genes was identified. TRAF6 (Montrer TRAF6 Protéines), a tumor necrosis factor (Montrer TNF Protéines) receptor-associated family member, plays an important role in T cell signaling and in RANKL (Montrer TNFSF11 Protéines)-dependent osteoclast differentiation and activation but its role in human OP has not been previously reported
The show that DNA damage caused by RAG1 activity in pre-B cells was able to downmodulate RAG1 expression and activity, confirming the existence of a negative feedback regulatory mechanism.
Our findings suggest that mutations in RAG1, specifically the p.R474C variant, can be associated with relatively mild clinical symptoms or delayed occurrence of T cell and B cell deficiencies but may predispose to progressive multifocal leukoencephalopathy.
This study compares T-cell development of patients with RAG1-dependent immune deficiencies, and elucidates important differences that help to explain the wide range of immunologic phenotypes that result from different mutations within the same gene of various patients.
Agammaglobulinemia associated to nasal polyposis due to a hypomorphic RAG1 mutation
mutation c.256_257delAA in RAG1 gene seems to occur quite frequently in the Polish patients with severe combined immunodeficiency (Montrer PRKDC Protéines) and may result in classical OS as well as in severe combined immunodeficiency (Montrer PRKDC Protéines) without clinical and laboratory features of OS when occurred in homozygous state
study reported 4 patients with RAG1 deficiency: classic severe combined immune deficiency (SCID (Montrer PRKDC Protéines)) was seen in 2 patients, Omenn syndrome was observed in 1 patient and atypical SCID (Montrer PRKDC Protéines) was seen in one patient
Study reports that RAG1 associates with chromatin at thousands of active promoters and enhancers in the genome of developing lymphocytes. The mouse and human genomes appear to have responded by reducing the abundance of "cryptic" recombination signals near RAG1 binding sites.
this study determined that the depletion of uterine innate lymphoid cells in Rag1-/- mice resulted in impaired uterine spiral artery remodeling and reduced fetal viability
Describe spontaneous S. xylosus infection in a genetically modified murine model. S. xylosus infection in Rag1-/-Tpl2 (Montrer MAP3K8 Protéines)-/- mice correlated with disseminated bacteria and elevated numbers of circulating monocytes.
This study demonstrated that the lymphocyte-deficient Rag1 animals demonstrated a significantly lower rate of aneurysm formation and rupture.
This work provides important mechanistic insight into how spatiotemporal expression of the Rag genes is tightly controlled during B lymphocyte (Montrer AKAP17A Protéines) development to prevent mistimed dsDNA breaks and their deleterious consequences.
a novel RAG1/2-mediated insertion pathway distinct from DNA transposition and trans-V(D)J recombination that destabilizes the genome and shares features with reported oncogenic DNA insertions.
loss of the BH3-only (Montrer BBC3 Protéines) protein BIM (Montrer BCL2L11 Protéines) accelerated lymphoma development in p53 (Montrer TP53 Protéines)-deficient mice. This process was negated by concomitant loss of RAG1/2-mediated antigen receptor gene rearrangement.
Nonamer binding domain (NBD) of RAG1 plays a central role in the recognition of recombination signal sequence.
Overall, these findings suggest that the V(D)J recombination-activating gene 1, RAG1, may play a role in long-term memory consolidation.
propose that pre-B cells toggle between pre-BCR (Montrer BCR Protéines) signals and a RAG1 DNA double-strand break-dependent checkpoint to maintain genome stability while iteratively assembling Igl chain genes
Differential gene expression following TLR stimulation in rag1-/- mutant zebrafish tissues and morphological descriptions of lymphocyte-like cell populations
first report of any rag1(-/-) mutant vertebrate mounting a protective secondary immune response to a bacterial pathogen
target-selected inactivation of the rag1 gene
Rag1 has a role in developing zebrafish cortex-medullary regionalization
by embryonic day 4, rag1 transcripts are seen in the pancreas
Recombination signal sequences are recognized by rag1 protein.
Rag1 expression is restricted to a subpopulation of zebrafish olfactory neurons projecting to the lateral olfactory bulb; Rag11 catalytic activity is not essential for axon targeting
This report describes the leukocyte populations in a unique model, recombination activation gene 1-/- mutant zebrafish (rag1 mutants).
The protein encoded by this gene is involved in activation of immunoglobulin V-D-J recombination. The encoded protein is involved in recognition of the DNA substrate, but stable binding and cleavage activity also requires RAG2. Defects in this gene can be the cause of several diseases.
V(D)J recombination-activating protein 1
, recombination activation protein 1
, recombination activating gene 1
, recombination activating protein 1
, recombination-activating gene 1
, recombinase activating protein
, V(D)J recombination-activating protein 1-like
, RING finger protein 74
, recombinase activating gene 1
, recombination activating protein