Recombinant Human LGALS3 293 Cell Lysate

• Cat.No.: LGALS3-4766HCL

Specification

• Description: Antigen standard for lectin, galactoside-binding, soluble, 3 (LGALS3), transcript variant 1 is a lysate prepared from HEK293T cells transiently transfected with a TrueORF gene-carrying pCMV plasmid and then lysed in RIPA Buffer. Protein concentration was determined using a colorimetric assay. The antigen control carries a C-terminal Myc/DDK tag for detection.
• Source: HEK 293 cells
• Species: Human
• Components: This product includes 3 vials: 1 vial of gene-specific cell lysate, 1 vial of control vector cell lysate, and 1 vial of loading buffer. Each lysate vial contains 0.1 mg lysate in 0.1 ml (1 mg/ml) of RIPA Buffer (50 mM Tris-HCl pH7.5, 250 mM NaCl, 5 mM EDTA, 50 mM NaF, 1% NP40). The loading buffer vial contains 0.5 ml 2X SDS Loading Buffer (125 mM Tris-Cl, pH6.8, 10% glycerol, 4% SDS, 0.002% Bromophenol blue, 5% beta-mercaptoethanol).
• Size: 0.1 mg
• Storage Instruction: Store at -80°C. Minimize freeze-thaw cycles. After addition of 2X SDS Loading Buffer, the lysates can be stored at -20°C. Product is guaranteed 6 months from the date of shipment.
• Applications: ELISA, WB, IP. WB: Mix equal volume of lysates with 2X SDS Loading Buffer. Boil the mixture for 10 min before loading (for membrane protein lysates, incubate the mixture at room temperature for 30 min). Load 5 ug lysate per lane.

Gene Information

• Gene Name: LGALS3 lectin, galactoside-binding, soluble, 3 [ Homo sapiens ]
• Official Symbol: LGALS3
• Synonyms: LGALS3; lectin, galactoside-binding, soluble, 3; LGALS2; galectin-3; galectin 3; GALIG; MAC 2; lectin L-29; 35 kDa lectin; MAC-2 antigen; IgE-binding protein; laminin-binding protein; galactose-specific lectin 3; carbohydrate-binding protein 35; L31; GAL3; MAC2; CBP35; GALBP
• Gene ID: 3958
• mRNA Refseq: NM_001177388
• Protein Refseq: NP_001170859
• MIM: 153619
• UniProt ID: P17931
• Chromosome Location: 14q22.3
• Pathway: Advanced glycosylation endproduct receptor signaling, organism-specific biosystem; Hedgehog signaling events mediated by Gli proteins, organism-specific biosystem; Immune System, organism-specific biosystem; Innate Immune System, organism-specific biosystem
• Function: IgE binding; protein binding; sugar binding

Reviews

09/30/2022

My experimentation flourishes, as if guided by the hands of magic, all thanks to this extraordinary reagent.

03/18/2020

Compared to similar products, this reagent demonstrates superior cost-effectiveness, satisfying both in terms of quality and price.

08/01/2017

The storage conditions for the reagent are simple and do not require special storage environments.

Q&As

Are there any diagnostic or prognostic implications of LGALS3 in cancer?

 LGALS3 has been investigated as a potential diagnostic and prognostic marker in various types of cancer. Its expression levels have been correlated with tumor stage, grade, and patient survival. LGALS3 can be detected in blood, urine, and tissue samples, making it a promising biomarker for non-invasive cancer detection and monitoring. Additionally, LGALS3 expression patterns, subcellular localization, and glycosylation status have been associated with specific cancer subtypes and clinical outcomes, providing insights into disease progression and patient prognosis.

How is the expression of LGALS3 regulated in different tissues and under different conditions?

The expression of LGALS3 is regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational regulation. Transcription factors, such as Sp1, AP-1, and NF-κB, bind to the promoter region of the LGALS3 gene and regulate its expression. Epigenetic modifications, including DNA methylation and histone acetylation, can also influence LGALS3 expression. Additionally, microRNAs and RNA-binding proteins can regulate the stability and translation of LGALS3 mRNA. Moreover, various extracellular signals, such as cytokines and growth factors, can modulate LGALS3 expression in a tissue-specific and context-dependent manner.

What is the role of the protein LGALS3 in cellular processes?

LGALS3, also known as galectin-3, is a multifunctional protein involved in various cellular processes. It plays a role in cell adhesion, migration, apoptosis, immune response, and inflammation. LGALS3 can interact with glycosylated proteins and lipids, modulating their functions and signaling pathways. It also acts as a receptor for extracellular matrix proteins and plays a role in tissue remodeling. Additionally, LGALS3 has been implicated in cancer progression and metastasis, as well as in the regulation of fibrosis and wound healing.

Are there therapeutic implications of targeting LGALS3 in cancer treatment?

Targeting LGALS3 has emerged as a potential therapeutic strategy in cancer treatment. Inhibition of LGALS3 expression or activity can impede tumor cell survival, migration, and invasion. Additionally, blocking LGALS3-mediated immune evasion mechanisms could enhance anti-tumor immune responses. Various approaches, such as small molecule inhibitors, antibodies, and gene silencing techniques, have been explored to target LGALS3 in preclinical and clinical studies. However, further research is needed to optimize these strategies and evaluate their efficacy and safety in cancer patients.

How does LGALS3 contribute to immune response and inflammation?

LGALS3 plays a critical role in immune response and inflammation. It can modulate the activation and function of immune cells, including macrophages, dendritic cells, and T cells. LGALS3 can promote cell adhesion and migration, facilitating immune cell recruitment to sites of inflammation. It also regulates the production of pro-inflammatory cytokines and chemokines, and can act as a chemoattractant for immune cells. Additionally, LGALS3 can modulate the clearance of apoptotic cells and regulate the resolution of inflammation.

What are the functional domains and motifs present in LGALS3?

LGALS3 contains a conserved carbohydrate recognition domain (CRD) that allows it to bind to glycosylated proteins and lipids. The CRD is responsible for LGALS3's interaction with specific glycan structures, mediating its diverse functions. LGALS3 also has a N-terminal domain involved in protein-protein interactions and a C-terminal domain that regulates its oligomerization. Moreover, LGALS3 can undergo post-translational modifications, such as phosphorylation and glycosylation, which can affect its localization, stability, and function.

What is the involvement of LGALS3 in cancer progression and metastasis?

 LGALS3 has been implicated in various aspects of cancer progression and metastasis. It can promote tumor cell survival, migration, invasion, and angiogenesis. LGALS3 is involved in the modulation of epithelial-mesenchymal transition (EMT), a process essential for cancer cell metastasis. It also interacts with components of the extracellular matrix, promoting tumor cell adhesion and invasion. Furthermore, LGALS3 can influence immune evasion mechanisms employed by cancer cells, contributing to tumor immune escape and resistance to therapy.