Recombinant Proteins

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TRIM21 Human

Tripartite Motif Containing 21 (RO52) Human Recombinant

TRIM21 Human Recombinant produced in SF9 is a polypeptide chain having a calculated  molecular mass of 52 kDa.
TRIM21 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT18616
Source
Sf9 insect cells.
Appearance
Sterile Filtered clear solution.

TRIM21 Human Biotin

Tripartite Motif Containing 21 (RO52) Human Recombinant, Biotinylated

TRIM21 Human Recombinant, Biotin produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 52kDa.

TRIM21 is expressed with a -6x His tag at N-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT18666
Source
Sf9 insect cells.
Appearance
Sterile Filtered clear solution.

TRIM28 Human

Tripartite Motif Containing 28 Human Recombinant

TRIM28 Human Recombinant produced in E. coli is a single polypeptide chain containing 460 amino acids (366-802) and having a molecular mass of 48.7 kDa.
TRIM28 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18734
Source
E.coli.
Appearance
Sterile Filtered colorless solution.

TRIM33 Human

Tripartite Motif Containing 33 Human Recombinant

TRIM33 Human Recombinant produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 124,041 Dalton.
TRIM33 is expressed with a -10xHis tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT18824
Source
Sf9 Insect Cells.
Appearance
Sterile Filtered clear solution.
Definition and Classification

The Tripartite Motif (TRIM) family is a large group of proteins characterized by a conserved tripartite motif at the N-terminus, which includes a RING finger domain, one or two B-box zinc finger domains, and a coiled-coil region . The TRIM family is divided into two groups based on their C-terminal domains: Group 1 proteins have a variety of C-terminal domains, while Group 2 proteins possess a SPRY domain .

Biological Properties

Key Biological Properties: TRIM proteins are involved in various cellular processes, including cell proliferation, differentiation, and apoptosis . They function as E3 ubiquitin ligases, mediating the ubiquitination and subsequent degradation of target proteins .

Expression Patterns and Tissue Distribution: TRIM proteins are ubiquitously expressed across different tissues, with some members showing tissue-specific expression patterns . For example, TRIM72 (MG53) is predominantly expressed in striated muscles .

Biological Functions

Primary Biological Functions: TRIM proteins play crucial roles in immune responses and pathogen recognition . They are involved in the regulation of innate immunity by modulating the activity of various signaling pathways .

Role in Immune Responses and Pathogen Recognition: Many TRIM proteins are induced by interferons and are essential for the restriction of viral infections . For instance, TRIM5α is known for its role in recognizing and restricting retroviral infections .

Modes of Action

Mechanisms with Other Molecules and Cells: TRIM proteins interact with various cellular components through their conserved domains . The RING domain confers E3 ubiquitin ligase activity, while the B-box and coiled-coil regions mediate protein-protein interactions .

Binding Partners and Downstream Signaling Cascades: TRIM proteins often form complexes with other proteins to regulate downstream signaling pathways . For example, TRIM21 interacts with antibodies and targets them for degradation, thereby modulating immune responses .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: The expression and activity of TRIM proteins are tightly regulated at multiple levels Transcriptional Regulation: TRIM gene expression is regulated by various transcription factors and signaling pathways Post-Translational Modifications: TRIM proteins undergo post-translational modifications such as ubiquitination, sumoylation, and phosphorylation, which modulate their stability and activity .

Applications

Biomedical Research: TRIM proteins are extensively studied for their roles in various diseases, including cancer, neurodegenerative diseases, and viral infections Diagnostic Tools: TRIM proteins can serve as biomarkers for disease diagnosis and prognosis Therapeutic Strategies: Targeting TRIM proteins offers potential therapeutic strategies for treating diseases such as cancer and viral infections .

Role in the Life Cycle

Role Throughout the Life Cycle: TRIM proteins are involved in various stages of the life cycle, from development to aging . They play critical roles in cell proliferation, differentiation, and apoptosis, which are essential for normal development and tissue homeostasis . In aging and disease, dysregulation of TRIM proteins can contribute to the progression of various pathological conditions .

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