Protein
- +1 609-736-0910
- [email protected]
- 90 State Street, STE 700 Office 40, Albany, NY 12207 United States
Product Background
Catalog Number |
ALP64562 |
Product Name |
Recombinant Rhesus Macaque CD160 Protein, Fc Tag |
Synonyms |
CD160, CD160 protein, Rhesus Macaque CD160 Protein, Recombinant Rhesus Macaque CD160 Protein, protein CD160 antibody, CD160 antigen |
Alias |
CD160 antigen, CD160 |
Official symbol |
CD160 |
Species |
Rhesus Macaque |
Expression host |
HEK293 Cells |
Protein family |
Immunoglobulin Superfamily |
Size |
50ug, 100ug |
Purification |
Affinity Purification |
Purity |
>90%-95% as determined by SDS-PAGE |
Endotoxin |
<1.0 EU/ug determined by the LAL method |
Buffer |
Supplied in PBS, pH7.4 |
Storage |
For long term storage, store the reagent at -80°C. Avoid repeated freeze-thaw cycles. |
Shipping Condition |
Lyophilized powder is shipped at ambient temperature. Liquid form is shipped in dry ice. |
Note |
This product is for research use only. This product can not be used for human. |
FAQ
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What is affinity chromatography and how is it used for protein purification?
Affinity chromatography utilizes the specific binding affinity between a target protein and a ligand immobilized on a chromatography matrix. The target protein selectively binds to the matrix, allowing for its purification in a highly specific manner. Common affinity tags include histidine tags, antibody tags, and protein-specific ligands.
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What is ion exchange chromatography and how is it used for protein purification?
Ion exchange chromatography separates proteins based on their net charge at a specific pH. Proteins with a net positive charge bind to negatively charged ion exchange resins (anion exchange chromatography), while proteins with a net negative charge bind to positively charged resins (cation exchange chromatography).
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What is size exclusion chromatography and how is it used for protein purification?
Size exclusion chromatography separates proteins based on their size and shape. Larger proteins elute first from the chromatography column, while smaller proteins are excluded from the pores of the stationary phase. This method is commonly used for desalting and buffer exchange as well as for the purification of protein complexes.
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How are purity and yield assessed during protein purification?
Purity and yield are typically assessed using analytical techniques such as SDS-PAGE, western blotting, UV absorbance spectroscopy, and Bradford or BCA protein assays. These techniques provide quantitative and qualitative information about the composition of the purified protein sample.