RAG1 Antibodies

V(D)J recombination-activating protein 1 (RAG1)

Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. From the RAG complex, RAG1 mediates the DNA-binding into the conserved recombination signal sequences (RSS) and catalyzes the DNA cleavage activities by introducing a double-strand break between the RSS and the adjacent coding section.

RAG2 isn't a catalytic component but is required for all known catalytic activities. DNA cleavage occurs in two steps: a first nick is introduced at the top strand immediately upstream of the heptamer, generating a 3'- hydroxyl group that may attack the phosphodiester bond on the reverse strand in a direct transesterification reaction, thereby creating 4 DNA endings: 2 hairpin coding ends and two blunt, 5'- phosphorylated ends.

Gene Information

Human
Gene Name:	RAG1
Uniprot:	P15918
Entrez:	5896

Family

Belongs to:
RAG1 family

Alternative Names

MGC43321; RAG-1; recombination activating gene 1; RING finger protein 74; RNF74recombination activating protein 1; V(D)J recombination-activating protein 1

Molecular Weight

Mass (kDA):
119.097 kDA

Genomic Context

Human
Location:	11p12
Sequence:	11; NC_000011.10 (36510353..36579762)

Tissue Specificity

Maturing lymphoid cells.

Subcellular Localizations

Nucleus.

Diseases

• Immunologic Deficiency Syndromes
• Severe Combined Immunodeficiency
• Neoplasms
• Inflammation
• Congenital Combined Immunodeficiency
• Autoimmune Reaction
• Malignant Neoplasms
• Histiocytic Medullary Reticulosis (disorder)
• Lymphoma
• Leukemia
• Chromosomal Translocation
• Colitis
• Autoimmunity

• Infective Disorder
• Autoimmune Diseases
• Cell Transformation, Neoplastic
• Hepatitis
• Intestinal Diseases
• Lymphopenia
• Inflammatory Bowel Diseases

Interacting Proteins

• NCK1

Pathways

• V(d)j Recombination
• Immune Response
• Cell Development
• Pathogenesis
• Transposition
• Localization
• Cell Differentiation
• Dna Repair
• Cell Proliferation
• Cell Activation
• Transport
• Cell Cycle
• Cytokine Production

• Secretion
• Cell Maturation
• Complement Activation
• Inflammatory Response
• Innate Immune Response
• Virulence
• Glucose Transport

PTMs

• Cleavage
• Methylation
• Phosphorylation
• Acetylation
• Deamination

• Nitration
• Biotinylation
• Carboxylation
• Phosphorothioation
• Ubiquitination

• Myristoylation

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/RAG1

Best Uses Of The RAG1 Marker

The RAG1 gene marker is an essential component in the RAG complex, which mediates genomic rearrangements. The RAG complex is vital for vertebrates' adaptive immunity. Boster Bio's antibodies to RAG1 react with the protein in mouse and rabbit samples. Boster Bio samples can be obtained if you are interested in studying RAG1 (or related proteins). This article will cover the RAG1 indicator and its application in biological assays.

RAG1 is a component of the RAG complex that catalyzes.

The RAG1 mark is most useful in neuroscience research due to its ability to bind to DNA. The complex is activated when two complementary signals are present. The binding of the second signals causes a conformational change within RAG1. In vitro these processes might be identical, but they may differ in vivo. In this scenario, RAG proteins could assemble at one site first and then search the second for a naked signal. These two states are likely to differ due to the asymmetry between the signal sites.

The RAG1 markers are highly sensitive in detecting RNA presence in cells. It is useful in many types of cancer research. In some cases, it may be used to identify RAG2 proteins. This marker is particularly useful in cancer research. It is also useful for detecting mutated forms of RNA during cancer treatment. This marker does have some limitations. The RAG1 marker is unable to detect DNA fragments that are tangled, distorted, or tangled.

The RAG1 marker can detect many biological assays. This monoclonal antibody reacts with RAG1 in different animal samples. Boster Bio generates the antibodies using mice and rabbit models. The antibodies are also extremely specific for histidine epitope tags. In this way, the RAG1 marker is a versatile biomarker in molecular biology.

It mediates genome rearrangement

The RAG1 genome encodes the RNA polymerase 2 gene. This is critical for T-cell formation. It is highly damaged during the development and maintenance of thymocytes. It is activated by Notch2 WT or RB1984A. Notch2 doesn't bind to RBPJ (nonamer-bindingdomain dimer), in the Rag2 locus.

The RAG complex is a multiprotein complex involved in the cleavage phase of V(D)J recombination, the process responsible for assembling a large repertoire of T-cell receptor and immunoglobulin genes. RAG1 binds with conserved recombination signals sequences and catalyzes double-strand break between RSS and adjacent coding segments. RAG2 does not directly participate in catalysis but is essential for RAG1's catalytic activities.

The RAG1 gene is required for adaptive immune responses in vertebrates. In addition, RAG1 is expressed in the olfactory Epithelium. It may be responsible to the recombination or rearrangement of DNA strands. RAG1's structure is based upon Notch2's binding mechanism. The RAG1 Protein is found in a variety of tissues including skin and brain.

The Transib transposon from the Transib family is the first to invade vertebrate genes. It invaded the genomes of ancestral jawed vertebrates around 500 million year ago. The RAG1/2 invasion is thought to be the most significant evolutionary event, shaping the agnathan variable lymphocyte receptor and adaptive immune system. It is not known what Notch2's exact role is.

It protects the genome of some neurons

The RAG1/RAG2 Transposase is a key cellular force in jawed vertebrates. RAG1 has an important molecular residue, residue 848. It inhibits transposition. The methionine makes up part of the complex which captures the RAG that is engaged with the transposon end. This explains why transposase acts in a recombinase capacity.

The RAG1 protein transposes DNA after DNA cleavage. The transposon will then release its coding flanks in order to form a signal ending complex. This complex contains the target DNA and is captured by a staggered nucleophilic assault. RAG1-strands bind to target DNA through a strand transport complex. This process requires a lot more DNA.

The RAG1 marker plays an important role during lymphocyte growth, which is associated to immune memory functions. Deletion of the RAG1 gene results in a lack of mature functional lymphocytes. Researchers have found that this transcription occurs in areas of high neuronal density, such the cerebellum. This region is important for memory function and learning. In order to test whether RAG1 transfection of neurons is safe, researchers used lentiviral vector systems to package scrambled sequences within these vectors and inject them stereotaxically into the hippocampal area.

RAG1 plays a critical role in V(D]J Recombination. Its mistargeting is a major threat for genome stability. It is not fully understood, however, how RAG1 is suppressed. Its role is to decrease the number of cryptic signals that can be used for recombination near RAG1 binding locations. RAG1 is also involved with recombination. Lymphocyte maturation is dependent on recombination around RAG1 binding locations.

It is vital for vertebrates' adaptive immunity

The evolutionary origin of the RAG genes was first hypothesized to be the Transib transposons. The ProtoRAG protein was discovered in lamprey lympocytes. Later, it was discovered that the RAG1/RAG2 genetic pair had the same evolutionary origin. RAG recombinase later became a transposition protein and the evolutionary requirements of AID was revealed.

The immunoglobulin Superfamily (IgSF), contains genes that are crucial for the adaptive immune response. The versatile Ig domains are used by many proteins including natural killer cells and phagocytic cells. They also regulate interaction between T- and B lymphocytes. They have received particular attention in searches for the phylogenetic forerunners of the adaptive immune system. The VLR gene, in particular, was discovered in the lamprey (a jawless vertebrate).

Adaptive immune systems rely on recombination and V(D)J DNA recombination to recognize various antigens and trigger an antigen-specific immune response. The recombination-activating gene Rag1/2 plays a central role in adaptive immunity. It is a cell specific marker for lymphoid dedication. In vertebrates, RAG genes have evolved in the jaws and neck. However, it is not known whether RAG1/2 are regulated by lineage-specific transcription factors.

The function and function of the RAG1 genes in vertebrates are not well understood. The discovery of DNA editing in domesticated mammals and cytidine deraminases supports its essentiality for the adaptive immune systems. This discovery provides insight into how the adaptive immune response evolved and highlights the evolution of these genes. RAG1 is also essential for the adaptive immune systems of vertebrates.

It is expressed in the olfactory sensory neuron

RAG1 is an olfactory receptor, expressed predominantly in olfactory sensory neurons. Studies of RAG1-/ mice show that this receptor is present in olfactory sensor neurons. Two studies revealed that mice that were born without RAG1 showed impaired sniffing abilities, while mice that had the gene deleted were capable of finding the cookie in just a few seconds. The RAG-1-/ mice exhibited an impaired sense of smell in both the buried cookie test and the habituation/dishabituation test. A shows how long it took each mouse for the buried cookies to be found. These values represent the means + SEM for n = five mice. Data from four other experiments with similar results are also reported.

In a zebrafish-model, the RAG1 gene is expressed in the olefactory sensory neuron. It is essential for adaptive immunity and is expressed within the olfactory epithelium. Although the RAG1 signal is found in many tissues it is not understood how it functions in olfactory systems. We used a transgenic zebrafish strain to show Rag1 is expressed in olfactory epithelium.

In olfactory sensor neurons, the RAG1 protein colocalized in complex with NeuN. The RAG1 levels were higher in mice who had been subject to context-fear condition. This could be due in part to residual blood within the amygdala. Further studies are needed in order to determine if RAG1 can be expressed in olfactory sensors neurons. If RAG1 is expressed by olfactory neuronal neurons, then the mice are conditioned for context terror.

It is not required for axon targeting or receptor expression

We have shown Rag1 to be expressed in a subset (of zebrafish) of olfactory sensory neurons. GFP-expressing neurons reach the lateral sensory bulb. Only one of the glomerular structures is innervated. In a frontal perspective, neurons expressing GFP contain OMP, while those that express RAG1 don't. GFP-containing Axons can be seen in a deeper section. In a dorsal view only the left olfactory bulbs is stained for anti-GFP axons.

Retinal axons are topographic connections that form topographic connections in the Drosophila vision system with target cells in its optic lobe. Frazzled, which is expressed in DRG sensory neuronal neurons, plays a redundant part in the differentiation and maintenance of target cells. In contrast, ectopic expression of RAG1 does not disrupt the formation of retinal projections. Despite these results, we are still not able to determine the exact mechanism through which this protein influences the morphology and structure of retinal projections.

The local translation of mRNA by the Netrin-1 protein is important for axons. The presence of Netrin-1 has been shown to regulate mRNA export from the nucleus. Netrin-1 has been shown to regulate local mRNA translation in the axons. However, this is not conclusive as RAG1 does not regulate receptor expression or axon targeting.