Recombinant Proteins

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CARD17 Human

Caspase Recruitment Domain Family, Member 17 Human Recombinant

CARD17 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 133 amino acids (1-110) and having a molecular mass of 14.3 kDa.
CARD17 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5167
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

CARD18 Human

Caspase Recruitment Domain Family, Member 18 Human Recombinant

CARD18 Human Recombinant produced in E. coli is a single polypeptide chain containing 110 amino acids (1-90) and having a molecular mass of 12.3kDa.
CARD18 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5202
Source
E.coli.
Appearance
Sterile Filtered colorless solution.
Definition and Classification

The Caspase Recruitment Domain (CARD) family is a group of protein interaction modules that play a crucial role in the regulation of apoptosis, inflammation, and immune responses. CARD domains are typically found in proteins involved in signaling pathways that lead to the activation of caspases, which are proteases essential for the execution of apoptosis. The CARD family can be classified into several subfamilies based on their structural and functional characteristics, including CARD-only proteins, CARD-containing adaptors, and CARD-containing enzymes.

Biological Properties

Key Biological Properties: CARD domains are characterized by their ability to mediate homotypic protein-protein interactions, which are essential for the formation of signaling complexes. These domains are typically composed of six to seven alpha-helices arranged in a compact, globular structure.

Expression Patterns: CARD-containing proteins are expressed in a variety of tissues and cell types, with some members showing ubiquitous expression while others are more restricted to specific cell types or tissues.

Tissue Distribution: CARD proteins are found in many tissues, including the immune system (e.g., lymph nodes, spleen), the nervous system (e.g., brain, spinal cord), and other organs such as the liver, lungs, and kidneys.

Biological Functions

Primary Biological Functions: The primary function of CARD domains is to facilitate the assembly of signaling complexes that activate caspases and other downstream effectors. This process is crucial for the regulation of apoptosis, inflammation, and immune responses.

Role in Immune Responses: CARD-containing proteins play a vital role in the immune system by mediating the activation of inflammatory pathways and the production of cytokines in response to pathogen recognition.

Pathogen Recognition: Some CARD proteins are involved in the recognition of pathogen-associated molecular patterns (PAMPs) and the initiation of innate immune responses.

Modes of Action

Mechanisms with Other Molecules and Cells: CARD domains interact with other CARD-containing proteins to form signaling complexes. These interactions are often mediated by homotypic CARD-CARD interactions, which are essential for the activation of downstream signaling pathways.

Binding Partners: CARD proteins can bind to a variety of other proteins, including caspases, kinases, and adaptors, to form multiprotein complexes that regulate apoptosis and inflammation.

Downstream Signaling Cascades: The formation of CARD-mediated signaling complexes leads to the activation of downstream effectors, such as caspases and nuclear factor-kappa B (NF-κB), which are involved in the execution of apoptosis and the production of inflammatory cytokines.

Regulatory Mechanisms

Regulatory Mechanisms: The expression and activity of CARD-containing proteins are tightly regulated at multiple levels, including transcriptional regulation, post-translational modifications, and protein-protein interactions.

Transcriptional Regulation: The expression of CARD genes is controlled by various transcription factors and regulatory elements that respond to cellular signals and environmental cues.

Post-Translational Modifications: CARD proteins can undergo various post-translational modifications, such as phosphorylation, ubiquitination, and proteolytic cleavage, which can modulate their activity, stability, and interactions with other proteins.

Applications

Biomedical Research: CARD-containing proteins are important targets for biomedical research due to their roles in apoptosis, inflammation, and immune responses. Understanding the function and regulation of these proteins can provide insights into the mechanisms of various diseases and identify potential therapeutic targets.

Diagnostic Tools: CARD proteins can serve as biomarkers for the diagnosis and prognosis of diseases associated with dysregulated apoptosis and inflammation, such as cancer, autoimmune disorders, and infectious diseases.

Therapeutic Strategies: Targeting CARD-mediated signaling pathways holds promise for the development of novel therapeutic strategies for the treatment of diseases characterized by aberrant apoptosis and inflammation. This includes the design of small molecules, peptides, and biologics that can modulate the activity of CARD-containing proteins.

Role in the Life Cycle

Role Throughout the Life Cycle: CARD-containing proteins play critical roles throughout the life cycle, from development to aging and disease. During development, these proteins are involved in the regulation of cell death and differentiation, which are essential for proper tissue formation and homeostasis.

From Development to Aging and Disease: In adulthood, CARD proteins continue to regulate apoptosis and immune responses, maintaining tissue homeostasis and protecting against infections and malignancies. Dysregulation of CARD-mediated pathways can contribute to the development of various diseases, including cancer, neurodegenerative disorders, and chronic inflammatory conditions.

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