Analytical Data
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Gene name
Igl
- Application
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Alternative Names
Igl；CD36L1；CLA1；Scavenger receptor class B member 1
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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
P0DOX8
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Expression Region
1-216aa
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AA Sequence
QSALTQPPSASGSLGQSVTISCTGTSSDVGGYNYVSWYQQHAGKAPKVIIYEVNKRPSGVPDRFSGSKSGNTASLTVSGLQAEDEADYYCSSYEGSDNFVFGTGTKVTVLGQPKANPTVTLFPPSSEELQANKATLVCLISDFYPGAVTVAWKADGSPVKAGVETTKPSKQSNNKYAASSYLSLTPEQWKSHRSYSCQVTHEGSTVEKTVAPTECS
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Molecular Weight
22.8 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
IgL (Immunoglobulin Light Chain) recombinant proteins are essential in the study of the immune response and antibody functionality. Antibodies, or immunoglobulins, are glycoproteins produced by B cells that play a crucial role in identifying and neutralizing pathogens. The light chains of antibodies are pivotal for their structural integrity and specificity. Research into IgL recombinant proteins has gained momentum due to their potential applications in therapeutic development, diagnostic tools, and as research reagents in immunology. The ability to produce these proteins in a recombinant form enables scientists to study their properties in isolation, manipulate them for enhanced functionalities, and utilize them in various experimental and clinical settings. As diseases like cancer and autoimmune disorders often involve dysfunctional antibody responses, understanding IgL recombinants can lead to novel treatment strategies and improve existing therapies. Furthermore, advances in biotechnology and protein engineering have enabled the design of IgL proteins with tailored characteristics, enhancing their efficacy and specificity in therapeutic applications. This research is complemented by computational modeling and structural biology techniques, which help elucidate the relationships between IgL structure and function, paving the way for more effective interventions in immune-mediated diseases. Overall, the study of IgL recombinant proteins represents a significant intersection of molecular biology and therapeutic innovation, with far-reaching implications for health and disease management.
