Analytical Data
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Gene name
HLA-G
- Application
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Alternative Names
(HLA G antigen)(MHC class I antigen G)
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Species
Human
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Source
Baculovirus
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P17693
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Expression Region
25-319aa
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Molecular Weight
53.1 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
HLA-G is a non-classical human major histocompatibility complex (MHC) class I molecule with immune-regulatory properties, primarily expressed in trophoblast cells during pregnancy, but also found in various tissues under pathological conditions. It plays a crucial role in maintaining maternal-fetal tolerance by inhibiting maternal immune responses against the semi-allogeneic fetus. The unique expression patterns and functions of HLA-G have drawn significant interest for therapeutic applications, particularly in transplantation, autoimmunity, and cancer immunotherapy. Recombinant HLA-G proteins have been developed for detailed studies on its biological functions and interactions with receptors such as ILT2 and ILT4, which are implicated in modulating immune responses. Understanding the diverse roles of HLA-G can provide insights into its potential as a biomarker for immune-related disorders and its possible use in enhancing graft acceptance in transplantation. Furthermore, research into HLA-G has the potential to leverage its immune-modulatory capabilities to design novel therapeutic interventions aimed at overcoming immune-related challenges in various clinical settings. As such, the study of recombinant HLA-G proteins not only advances our knowledge of immune regulation but also paves the way for innovative strategies in clinical practice.
