TRIM5 Antibodies

Tripartite motif-containing protein 5 (TRIM5)

Capsid-specific restriction factor that prevents disease from non-host-adapted retroviruses. Blocks viral replication early in the life span, after viral entry but before reverse transcription.

In addition to acting as a capsid-specific restriction factor, also functions as a pattern recognition receptor which triggers innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates'Lys-63'-linked polyubiquitin chains, which then are catalysts in the autophosphorylation of the MAP3K7/TAK1 complicated (contains TAK1, TAB2, and TAB3).

Gene Information

Human
Gene Name:	TRIM5
Uniprot:	Q9C035
Entrez:	85363

Family

Belongs to:
TRIM/RBCC family

Alternative Names

EC 6.3.2; EC 6.3.2.-; RING finger protein 88; RNF88tripartite motif protein TRIM; TRIM5alpha; tripartite motif containing 5; tripartite motif protein TRIM5; tripartite motif-containing 5; tripartite motif-containing protein 5

Molecular Weight

Mass (kDA):
56.338 kDA

Genomic Context

Human
Location:	11p15.4
Sequence:	11; NC_000011.10 (5590906..5685108, complement)

Subcellular Localizations

Cytoplasm. Nucleus. Predominantly localizes in cytoplasmic bodies (PubMed:12878161, PubMed:20357094). Localization may be influenced by the coexpression of other TRIM proteins, hence partial nuclear localization is observed in the presence of TRIM22 or TRIM27 (By similarity). In cytoplasmic bodies, colocalizes with proteasomal subunits and SQSTM1 (By similarity).

Diseases

• Hiv Infections
• Immunologic Deficiency Syndromes
• Retroviridae Infections
• Leukemia
• Virus Diseases
• Acquired Immunodeficiency Syndrome
• Infective Disorder
• Simian Acquired Immunodeficiency Syndrome
• Innate Immune Response
• Monkey Diseases
• Permissiveness, Biological Function

• Vesicular Stomatitis
• Stomatitis
• Malignant Neoplasms
• Chimera Disorder
• Tumor Virus Infections
• Viremia

Interacting Proteins

• SNAI1
• TRIM32

Pathways

• Reverse Transcription
• Viral Replication
• Pathogenesis
• Tropism
• Immune Response
• Innate Immune Response
• Localization
• Rna Interference
• Virion Assembly
• Transposition
• Cell Activation
• T Cell Activation
• Proteolysis

• Membrane Fusion
• Conjugation
• Drug Resistance
• Translation
• Cell Cycle
• Cell Differentiation
• Nuclear Import

PTMs

• Ubiquitination

• Sumoylation

• Cleavage

Research Areas

• Immunology
• Lipid and Metabolism
• Virology, Bacteria and Parasites
• Zinc Finger

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/TRIM5

Boster Bio: Best Uses Of The TRIM5 Marker

You have found the right place to look for reliable antibodies against TRIM5. Boster has high-affinity prima antibodies that have been widely used over the past 25 years. Their antibodies have also been validated for use in ELISA, Immunohistochemistry, and Western Blotting. Continue reading to learn more about this protein.

TRIM5 Rh-21R

The intracellular motility function of TRIM5 proteins is crucial. Its cytoplasmic organs are dynamic and quickly turn over. This protein was tracked using a software function. These are the best ways to use this marker in your research. Let's take a look at these advantages. These proteins have been proven to be useful in studying intracellular motility. They can also be used for understanding how TRIM5 protein affect intracellular motility.

The TRIM5 proteins are a tripartite molecular motif that includes three conserved amino-terminal domains. These domains include a SPRY domain and a cyclophilin A domain. The TRIM5 proteins binds to retroviral capsids and imposes a post entry block on the infection.

HIV-1 infection has been shown to be resistant in nonhuman primate models. Humans and rhesus Macaque cells are immune to HIV-1 infection. Researchers identified the TRIM5a mutant as a post-entry inhibitor to HIV-1 infection. They discovered that lipid starvation and repletion could restore endogenous post-entry restriction in HIV-1 infections. It is important that humans and rhesus monkeys encode a polymorphic version of the TRIM5 proteins, which may explain the dramatic differences in susceptibility between these two species.

Researchers were able use live cell microscopy to study TRIM5a's behavior in living cells. Their findings showed that TRIM5a cells exhibit two types of motility. Some cells displayed fast unidirectional long range movements while others displayed multidirectional short-distance saltatory movements. Its application in this context looks very promising. Although it is not only used for imaging, researchers hope to explore the role of TRIM5 in cancer research.

TRIM5 Rh -21R coiled-coil domain

The TRIM5 TRIM5 Rh -21R Protein has a coiled coil domain and a b-box 2 area. The chymotrypsin resistant properties of TRIM5 Rh 21R protein are dependent upon its coiled-coil domain. It is also a member the RING domain. The RING domain is located near the amino-terminus of TRIM5 Rh -21R. The B-box domain 2 contains the variable loop as well as the linker 2 area.

The TRIM5 Rh -21R proteins were purified to 0.4mg/ml and crosslinked with glutaraldehyde. This cross-linking process was stopped by Sigma's glycine. The cross-linked proteins are boiled in SDS buffer to remove excess Glycine. Finally, they are stained with Coomassie.

Insect and mammalian cell lines, TRIM5Rh -21R proteins are expressed. The protein has a predicted molecular mass of 64.5 kDa. It was expressed by insect cells using a vector containing recombinant baculovirus expression. The chimeric TRIM5 Rh -21R protein is expressed at a higher level in mammalian cells than the wild-type TRIM5a protein. It also features a His 6N-terminal sequence, Stag and thrombincleavage locations.

The TRIM5 Rh -21R molecule has been proven to be an important determinant in viral specificity. The sequence evolution of TRIM5 in humans and primates suggests a strong positive selection for the gene. The TRIM family has been shown to be associated with a weak restriction for SIV. This suggests that the TRIM families are potential restriction factors in dogs. Interestingly the TRIM families is actively involved gene duplication.

Both TRIM5 Rh -21R proteins have a RING domain and a B-box 2 domain. It is identical to the RING 2 domain. The B-box2 domain is involved with capsid binding. A mutation of the B-box2 domain might lead to modifications in capsid recognition.

Capsid recognition

TRIM5a, a cytoplasmic proteins that recognizes the capsid coating of incoming retroviral Cores and blocks their reproduction, is known as a cytoplasmic protease. It does this by prematurely disassembling a capsid core. TRIM5a's antiviral activities can be explained by several mechanisms. One mechanism involves a PRYSPRY domain, which is located in the C-terminus of TRIM5a.

The TRIM5 gene locus is highly modular, and has high relative nonsynonymous changes rates. It is found within the genomes diverse primate species and is associated to a high number nonsynonymous mutations. TRIM5a sequences were found in many eukaryotic eukaryotic plants and share a common last common ancestor 35 million year ago.

TRIM5 has been implicated both in HIV-1 replication, and in the suppression of host restriction factor. This antiviral compound recognizes the capsid structure and activates E3, ubiquitin, ligase activity. The K63-linked ubiquitin chains are unattached and activate TAK1 kinase as well as other downstream inflammatory mediators. Capsid recognition with the TRIM5 marker is a fundamental process of antiviral immunity.

Researchers continue to study the structural basis that CA recognition is possible. In the presence of the CA lattice, the TRIM5 multimer forms a hexameric TRIM5 protein lattice. This complex interface stimulates formation of soluble subdomains within TRIM5 in order to facilitate TRIM5 bind. This fusion reveals the molecular base for TRIM5 binding.

This research reveals that TRIM5 binds with the capsid lattice to inhibit viral replication in feline cell line lines. TRIM5a is also capable of rescuing infected tissues. Capsid-specific recognition and activation of the TRIM5 marker promotes transcription of inflammatory cytokines, which in turn enhances the host immune response against HIV infection.

Methods for producing and purifying TRIM5-derived products

There are many ways to make and purify TRIM5 protein. These methods should speed up studies about TRIM5 mechanism and structure. These methods were used for preparing TRIM5 derivatives. Each step of the larger research program is described below. The related section below provides more information about each method. This article reviews several of these methods.

The TRIM family of enzymes is a promising target for the development of novel therapeutics. Recent advances in the field have allowed us to better understand ubiquitin as well as the enzymes that play a role in it. The TRIM enzymes of the TRIM families could be used to accelerate drug discovery efforts by targeting all aspects in the ubiquitin chain. However, the intrinsic scaffolding nature these enzymes exhibit limits the ability to develop inhibitors, covalent probes or standard screening methods.

The L2 linker region (which is responsible for oligomerization) is one key element in the TRIM5 structur. This region also impacts the protein's capability to recognize capsids. This region of TRIM5 protein contains a coiled coil structure. Moreover, the TRIM5 Rh -21R proteins has a coiled coil domain that is adjacent the L2 linker.

SDS-PAGE purified the TRIM5 Rh 21R protein and was transferred to Millipore's polyvinylidene fluoride Immobilon filters. This purified TRIM5 protein was reacted with polyclonal rabbit antibodies. They were used as primary and secondary antibodies. The cross-linked proteins are boiled in SDS denature buffer and stained using Coomassie.