Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

SEPT2 Human

Septin-2 Human Recombinant

SEPT2 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 381 amino acids (1-361 a.a.) and having a molecular mass of 43.6kDa. SEPT2 is fused to a 20 amino acid His Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21872
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

SEPT3 Human

Septin-3 Human Recombinant

SEPT3 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 381 amino acids (1-358 a.a) and having a molecular mass of 43.1kDa.
SEPT3 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT21935
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

SEPT5 Human

Septin-5 Human Recombinant

SEPT5 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 392 amino acids (1-369) and having a molecular mass of 45.2 kDa.
The SEPT5 is fused to a 23 amino acid His-Tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22000
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

SEPT6 Human

Septin-6 Human Recombinant

SEPT6 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 457 amino acids (1-434) and having a molecular mass of 52.1 kDa.
SEPT6 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22095
Source
E.coli.
Appearance
Sterile Filtered colorless solution.
Definition and Classification

Septins are a group of highly conserved GTP-binding proteins found in eukaryotic cells, excluding plants . They are part of the cytoskeleton and are involved in various cellular processes. Septins can form hetero-oligomeric complexes that assemble into filaments, rings, and gauzes . These proteins are classified based on their sequence homology and structural features, with humans having 13 different septin genes .

Biological Properties

Key Biological Properties: Septins are known for their ability to bind and hydrolyze GTP, which is crucial for their function in filament formation . They have a conserved GTP-binding domain, a septin unique element (SUE), and a coiled-coil domain .

Expression Patterns and Tissue Distribution: Septins are ubiquitously expressed in various tissues, with specific septins showing distinct expression patterns. For example, Sept7 is widely expressed in the brain, heart, and skeletal muscles . Their expression can vary depending on the cell type and developmental stage .

Biological Functions

Primary Biological Functions: Septins play a critical role in cytokinesis, cell polarity, and vesicle trafficking . They act as scaffolds for recruiting other proteins and form diffusion barriers to compartmentalize cellular regions .

Role in Immune Responses and Pathogen Recognition: Septins are involved in the immune response by forming cages around pathogenic bacteria, preventing their spread . They also participate in phagocytosis and the formation of the immune synapse .

Modes of Action

Mechanisms with Other Molecules and Cells: Septins interact with various cellular components, including actin filaments, microtubules, and cell membranes . They form complexes through their GTP-binding domains and N- and C-terminal interactions .

Binding Partners and Downstream Signaling Cascades: Septins bind to proteins such as anillin, Borg proteins, and kinases, influencing downstream signaling pathways involved in cell division and cytoskeletal organization .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: Septin expression is regulated at the transcriptional level by factors such as E2F and p53 . Post-translational modifications, including phosphorylation, sumoylation, and ubiquitination, also modulate septin activity and stability .

Applications

Biomedical Research: Septins are studied for their role in cancer, neurodegenerative diseases, and infectious diseases . They serve as biomarkers for certain cancers and are potential targets for therapeutic interventions .

Diagnostic Tools and Therapeutic Strategies: Septins are used in diagnostic assays to detect cancer and other diseases. Therapeutic strategies targeting septins include small molecules that disrupt septin filament formation and function .

Role in the Life Cycle

Role Throughout the Life Cycle: Septins are essential for various stages of the life cycle, from embryonic development to aging . They are involved in processes such as cell division, differentiation, and maintenance of cellular integrity . Dysregulation of septin function is associated with aging-related diseases and cancer .

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