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- SPECIES: Human
- SOURCE SPECIES: E. coli
- RECOMBINANT PROTEIN SEQUENCE: Met1-Trp317
- FUSION TAG: Tag Free
- APPLICATION NOTE: This recombinant protein can be used for biological assays. For research use only.
- PREDICTED MOLECULAR WEIGHT: 35.8 kD
Properties
- PURITY: Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test. - PHYSICAL STATE: Lyophilized
- BUFFER: Lyophilized from a 0.2 um filtered solution of 20mM PB, 250mM NaCl, pH 7.2. It is not recommended to reconstitute to a concentration less than 100 ug/ml. Dissolve the lyophilized protein in ddH2O.
- STORAGE CONDITIONS: Lyophilized protein should be stored at -20°C, though stable at room temperature for 3 weeks.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days.
Aliquots of reconstituted samples are stable at -20°C for 3 months.
Additional Info
- NCBI OFFICIAL SYMBOL: LGALS8
- ADDITIONAL NAMES: Galectin-8, Gal-8, Po66 Carbohydrate-Binding Protein, Po66-CBP, Prostate Carcinoma Tumor Antigen 1, PCTA-1, LGALS8
- Protein Accession Number: O00214
- NCBI GENE ID NUMBER: 3964
Background
- The Galectin family of proteins, with specificity for Nacetyllactosaminecontaining glycoproteins, consists of beta-galactoside binding lectins containing homologous carbohydrate recognition domains (CRDs). At least 14 mammalian galectins family members, which share structural similarities in their carbohydrate recognition domains (CRD), have been identified to date. Unlike the selectin family of proteins, the carbohydrate binding specificity of galectins is calcium-independent. A common function of galectins is to cross-link structures containing N-acetyl-lactosamine located at the cell surface and within the extracellular matrix. 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.
Disclaimer
- FOR RESEARCH USE ONLY
For additional information, visit ProSci's Terms & Conditions Page. - Disclaimer: Products are intended for laboratory research purposes only and should be used by qualified personnel only. They are not intended for use in humans. ProSci is not liable for damages or injuries resulting from receipt and/or use of ProSci materials. Please refer to the Material Safety Data Sheet (MSDS) for safe storage, handling, and use procedures.
Shipping Info
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$35 Dry Ice Shipment fee may be required on some items.
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