Analytical Data
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Gene name
JCHAIN
- Application
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Alternative Names
JCHAIN；IGCJ；IGJ；Immunoglobulin J chain
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P01591
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Expression Region
23-159aa
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AA Sequence
QEDERIVLVDNKCKCARITSRIIRSSEDPNEDIVERNIRIIVPLNNRENISDPTSPLRTRFVYHLSDLCKKCDPTEVELDNQIVTATQSNICDEDSATETCYTYDRNKCYTAVVPLVYGGETKMVETALTPDACYPD
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Molecular Weight
28.5 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
JCHAIN, a crucial component of the immune system, encodes the J-chain protein that plays a significant role in the formation and stability of polymeric immunoglobulins, particularly IgM and IgA. Its primary function is to facilitate the secretion of these antibodies by linking monomeric immunoglobulins into larger structures, which are essential for effective immune responses. The understanding of JCHAIN's role has been pivotal in immunology, given that IgM and IgA antibodies are the first line of defense against pathogens. Recent studies have focused on the structural characterization and functional analysis of JCHAIN, employing advanced techniques such as X-ray crystallography and NMR spectroscopy to elucidate its mechanisms of action. These investigations provide insights into the molecular dynamics of immunoglobulin assembly and secretion, highlighting JCHAIN's impact on antibody functionality and immune system efficiency. Moreover, dysregulation in JCHAIN expression has been associated with various immune disorders and pathologies, making it a critical target for therapeutic intervention. Ongoing research aims to further dissect the regulatory pathways governing JCHAIN expression, its interactions with other immunological components, and its potential applications in vaccine development and treatment of autoimmune diseases. Understanding the multifaceted roles of JCHAIN not only enhances our knowledge of immune system dynamics but also opens new avenues for innovative strategies in immunotherapy and disease management.
