FASLG Human

FAS Ligand Human Recombinant

FASLG Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 173 amino acids (130-281 a.a.) and having a molecular mass of 19.6kDa.
FASLG is fused to a 21 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22536
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

FASLG Human, HEK

FAS Ligand Human Recombinant, HEK

Recombinant Human FAS Ligand produced in HEK293 cells is a polypeptide chain containing 147 amino acids (134-281a.a).
FASLG is fused to a 6 amino acid His-tag at N-terminus and purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22629
Source
HEK293 cells.
Appearance
Sterile Filtered colorless solution.

FAS Human

sFas Receptor Human Recombinant

sFas Receptor Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 157 amino acids and having a molecular mass of 17.6kDa.
The FAS is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22326
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

FAS Human, His

sFas Receptor Human Recombinant, His Tag

Recombinant FAS antigen/ CD95 purified from E. coli is a single non-glycosilated polypeptide chain containing amino acids 157-335 of Fas antigen. The recombinant CD95 is fused to C-terminal 6-histidine amino acids. The FAS antigen is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT22399
Source
Escherichia Coli.
Appearance
Sterile liquid formulation.

FAS Human, Sf9

sFas Receptor Human Recombinant, Sf9

FAS Human Recombinant produced in Baculovirus is a single glycosylated polypeptide chain containing 156 amino acids (26-173 aa) and having a molecular mass of  17.7KDa.
FAS  is fused to a 8 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT22462
Source

Sf9, Baculovirus cells.

Appearance
Sterile Filtered colorless solution.
Definition and Classification

The Fas receptor, also known as Fas, FasR, apoptosis antigen 1 (APO-1 or APT), cluster of differentiation 95 (CD95), or tumor necrosis factor receptor superfamily member 6 (TNFRSF6), is a protein encoded by the FAS gene in humans . It is a death receptor on the surface of cells that leads to programmed cell death (apoptosis) upon binding with its ligand, Fas ligand (FasL) .

Biological Properties

Key Biological Properties: The mature Fas protein has 319 amino acids, with a predicted molecular weight of 48 kilodaltons. It is divided into three domains: an extracellular domain, a transmembrane domain, and a cytoplasmic domain .

Expression Patterns: Fas is expressed in various tissues, including lymphoid tissues, bone marrow, and immune cells such as T cells, B cells, and natural killer (NK) cells .

Tissue Distribution: Fas is widely distributed across different tissues, including the liver, lung, kidney, and heart .

Biological Functions

Primary Biological Functions: Fas plays a crucial role in inducing apoptosis, a form of programmed cell death. This process is essential for maintaining immune homeostasis and eliminating damaged or infected cells .

Role in Immune Responses: Fas is involved in the regulation of the immune system by controlling the activation-induced cell death (AICD) of T cells, thereby preventing autoimmunity .

Pathogen Recognition: Fas-mediated apoptosis helps in the removal of pathogen-infected cells, contributing to the body’s defense mechanisms .

Modes of Action

Mechanisms with Other Molecules and Cells: Fas interacts with its ligand, FasL, to form the death-inducing signaling complex (DISC). This complex recruits the adapter molecule FADD (Fas-associated death domain), which in turn activates caspase-8, leading to a cascade of caspase activation and apoptosis .

Binding Partners: Fas primarily binds with FasL, but it can also interact with other molecules such as FADD and caspase-8 .

Downstream Signaling Cascades: The binding of Fas to FasL triggers the formation of DISC, which activates caspase-8. This activation leads to the cleavage of downstream effector caspases, ultimately resulting in apoptosis .

Regulatory Mechanisms

Transcriptional Regulation: The expression of Fas is regulated by various transcription factors, including NF-κB and p53 .

Post-Translational Modifications: Fas undergoes several post-translational modifications, such as phosphorylation and ubiquitination, which can influence its activity and stability .

Applications

Biomedical Research: Fas is extensively studied in the context of cancer, autoimmune diseases, and infectious diseases. It serves as a model for understanding apoptosis and immune regulation .

Diagnostic Tools: Fas and its ligand FasL are used as biomarkers for diagnosing certain cancers and autoimmune disorders .

Therapeutic Strategies: Targeting the Fas-FasL pathway has potential therapeutic applications in treating cancers, autoimmune diseases, and transplant rejection .

Role in the Life Cycle

Development: Fas-mediated apoptosis is essential during embryonic development for the removal of unwanted cells .

Aging: The regulation of Fas expression and activity changes with age, influencing the aging process and the development of age-related diseases .

Disease: Dysregulation of the Fas-FasL pathway is associated with various diseases, including cancers, autoimmune disorders, and neurodegenerative diseases .

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