LGALS8 Protein

Catalog No. ABIN7318523

This Recombinant LGALS8 protein is produced in Escherichia coli (E. coli).

Quick Overview for LGALS8 Protein (ABIN7318523)

Target: LGALS8 (Lectin, Galactoside-Binding, Soluble, 8 (LGALS8))

Protein Type: Recombinant

Biological Activity: Active

Origin: Human

Source: Escherichia coli (E. coli)

Purity: > 95 % as determined by reducing SDS-PAGE.

Product Details

Purpose: Recombinant Human Galectin-8/LGALS8 Protein (Active)

Sequence: Met 1-Trp317

Characteristics: Recombinant Human Galectin-8 is produced by our E.coli expression system and the target gene encoding Met1-Trp317 is expressed.

Endotoxin Level: < 1.0 EU per μg as determined by the LAL method.

Biological Activity Comment: Measured by its ability to agglutinate human red blood cells.

Application Details

Restrictions: For Research Use only

Handling

Format: Lyophilized

Reconstitution: Please refer to the printed manual for detailed information.

Buffer: Lyophilized from a 0.2 μm filtered solution of 20 mM PB, 250 mM NaCl, pH 7.2.

Storage: 4 °C,-20 °C,-80 °C

Storage Comment: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80°C. Reconstituted protein solution can be stored at 4-8°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.

Target Details

Target: LGALS8 (Lectin, Galactoside-Binding, Soluble, 8 (LGALS8))

Alternative Name: Galectin-8/LGALS8

Background:

Background: The Galectin family of proteins, with specificity for Nacetyllactosaminecontaining glycoproteins, consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs). They also possess hemagglutination activity, which is attributable to their bivalent carbohydrate binding properties. Galectins are active both intracellularly and extracellularly. Although they are localized primarily in the cytoplasm and lack a classical signal peptide, galectins can also be secreted by one or more unidentified, non-classical, secretory pathways. They have diverse effects on many cellular functions including adhesion, migration, polarity, chemotaxis, proliferation, apoptosis, and differentiation. Galectins may therefore play a key role in many pathological states, including autoimmune diseases, allergic reactions, inflammation, tumor cell metastasis, atherosclerosis, and diabetic complications. The galectins have been classified into the prototype galectins(1, 2, 5, 7, 10, 11, 13, 14), which contain one CRD and exist either as a monomer or a noncovalent homodimer. The chimera galectins(Galectin3) containing one CRD linked to a nonlectin domain, and the tandemrepeat Galectins(4, 6, 8, 9, 12) consisting of two CRDs joined by a linker peptide.Galectins lack a classical signal peptide and can be localized to the cytosolic compartments where they have intracellular functions. However, via one or more as yet unidentified nonclassical secretory pathways, galectins can also be secreted to function extracellularly. Individual members of the galectin family have different tissue distribution profiles and exhibit subtle differences in their carbohydrate-binding specificities. Each family member may preferentially bind to a unique subset of cell surface glycoproteins.

Synonym: Galectin-8, Gal-8, Po66 Carbohydrate-Binding Protein, Po66-CBP, Prostate Carcinoma Tumor Antigen 1, PCTA-1, LGALS8

Molecular Weight: 35.8 kDa

UniProt: O00214