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C-C chemokine receptor type 5 (CCR5) is a G protein-coupled receptor and a co-receptor for the entry of human immunodeficiency virus-1 (HIV-1) into cells. CCR5 chemokine receptor is involved in leucocytes chemotaxis to sites of inflammation and plays an important role in the macrophages, T cells, and monocytes recruitment. The chemokine ligands that bind to CCR5 are regulated on activation, normal T Cell expressed and secreted (RANTES) and macrophage inflammatory protein 1 alpha (MIP1α). GenScript’s human CCR5-expressing stable subline is guaranteed to function properly in the calcium flux assay.

Chemokine (C-X-C motif) receptor 1 (CXCR1) is a rhodopsin-like G protein-coupled receptor. It is one of two high-affinity receptors for the CXC chemokine interleukin-8 (IL-8), a major mediator of immune and inflammatory responses. The structure of human CXCR1 in a lipid bilayer should help to facilitate the discovery of new compounds that interact with GPCRs. GenScript’s human CXCR1-expressing stable subline is guaranteed to function properly in the calcium flux assay.

Chemokine (C-X-C motif) receptor 3 (CXCR3) belongs to the CXC chemokine receptor family. Similar to other chemokine receptors, it is a G protein-coupled receptor (GPCR). CXCR3 has two distinct splice variants, CXCR3A and CXCR3B, demonstrating different binding affinities. CXCR3-A binds to the CXC chemokines CXCL9 (MIG), CXCL10 (IP-10), and CXCL11 (ITAC) while CXCR3-B can also bind to CXCL4 in addition to CXCL9, CXCL10, and CXCL11. GenScript’s human CXCR3A-expressing stable subline is guaranteed to function properly in calcium flux assay.

Chemokine (C-X-C motif) receptor 5 (CXCR5) belongs to the CXC chemokine receptor family. CXCR5 plays crucial roles in B-cells migration into B-cell follicles of spleen and Peyer patches. CXCR5 reduces maintenance of immature neural cell populations and enhances proliferation of subgranular zone cells in the hippocampal dentate gyrus. GenScript’s human CCR1-expressing stable subline is guaranteed to function properly in the calcium flux assay.

4X LDS Sample Buffer is used to prepare protein samples for denaturing polyacrylamide gel electrophoresis (PAGE) with SurePAGE™, ExpressPlus™ and most other types of Bis-Tris gels. LDS sample buffer contains lithium dodecyl sulfate with pH at 8.4, which helps reducing the disulfide bonds and ensure optimal protein separation.

4X LDS Sample Buffer is used to prepare protein samples for denaturing polyacrylamide gel electrophoresis (PAGE) with SurePAGE™, ExpressPlus™ and most other types of Bis-Tris gels. LDS sample buffer contains lithium dodecyl sulfate with pH at 8.4, which helps reducing the disulfide bonds and ensure optimal protein separation.

MES SDS Running Buffer is formulated for running ExpressPlusᵀᴹ and SurePAGEᵀᴹ, Bis-Tris gels. This buffer is ideal for separating small- and medium- sized proteins. For separation of large- to medium- sized proteins, Tris-MOPS SDS buffer (M00138) is recommended.<br/>Reconstitute with 1000 ml deionized water to make 1X running buffer per pack of powder. Do not use acid or base to adjust the pH.

Protein L is a cell surface protein from Peptostreptoccocus magnus that binds to the variable light chains (kappa chain) of immunoglobulins without interfering with antigen binding. In contrast to IgG-binding proteins, such as protein A and protein G, which bind to the Fc region of immunoglobulins, protein L can be used for the detection and purification of mammalian kappa light chain antibodies of all classes. Since no part of the heavy chain is involved in the binding interaction, Protein L binds a wider range of antibody classes than Protein A or G. Protein L binds to representatives of all antibody classes, including IgG, IgM, IgA, IgE and IgD. Single chain variable fragments (scFv) and Fab fragments also bind to Protein L.

Protein L is a cell surface protein from Peptostreptoccocus magnus that binds to the variable light chains (kappa chain) of immunoglobulins without interfering with antigen binding. In contrast to IgG-binding proteins, such as protein A and protein G, which bind to the Fc region of immunoglobulins, protein L can be used for the detection and purification of mammalian kappa light chain antibodies of all classes. Since no part of the heavy chain is involved in the binding interaction, Protein L binds a wider range of antibody classes than Protein A or G. Protein L binds to representatives of all antibody classes, including IgG, IgM, IgA, IgE and IgD. Single chain variable fragments (scFv) and Fab fragments also bind to Protein L.