Recombinant Human IgJ Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2607

Recombinant Human IgJ Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2607
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Product Overview

Tag His
Host Species Human
Accession NP_653247.1
Synonym IGCJ, JCH
Background Immunoglobulin J chain, also known as IGJ and IGCJ, is a secreted polypeptide which is the first immunoglobulin-related polypeptide expressed during the embryogenesis and differentiation of B cells in the fetal liver. The joining Immunoglobulin J chain is a small polypeptide, expressed by mucosal and glandular plasma cells, which regulates polymer formation of immunoglobulin (Ig)A and IgM. Immunoglobulin J chain / IGJ serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces larger polymers. Immunoglobulin J chain / IGJ also help to bind these immunoglobulins to secretory component. J-chain incorporation into polymeric IgA (pIgA, mainly dimers) and pentameric IgM endows these antibodies with several salient features. Immunoglobulin J chain / IGJ is involved in creating the binding site for pIgR / SC in the Ig polymers, not only by determining the polymeric quaternary structure but apparently also by interacting directly with the receptor protein. Both the immunoglobulin J chain / IGJ and the pIgR/SC are key proteins in secretory immunity.
Description A DNA sequence encoding the mature form of human IGJ (NP_653247.1) (Gln 23-Asp 159) was fused with a His tag at the C-terminus and a pelB singnal peptide at the N-terminus.
Source E.coli
Predicted N Terminal Gln 23
AA Sequence Gln 23-Asp 159
Molecular Weight The recombinant human IGJ comprises 147 a.a. and has a predicted molecular mass of 17 kDa. It migrates as an approximately 26 kDa band in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, pH 8.0.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Serves to link two monomer units of either IgM or IgA. In the case of IgM, the J chain-joined dimer is a nucleating unit for the IgM pentamer, and in the case of IgA it induces dimers and/or larger polymers. It also helps to bind these immunoglobulins to secretory component.
Subcellular Location Secreted.
Database References

Gene Functions References

  1. TLR2 ligands induce CCR9 and CCR10 expression by circulating B-cells and increase their chemotaxis. TLR2 stimulation also induced J chain and IgA production demonstrating the induction of mucosal-like antibody secreting cells. PMID: 20947433

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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