Analytical Data
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Gene name
HLA-F
- Application
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Alternative Names
HLA-F;HLA-5.4;HLAF;HLA class I histocompatibility antigen. alpha chain F
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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
P30511
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Expression Region
22-305aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSGSHSLRY FSTAVSRPGR GEPRYIAVEY VDDTQFLRFD SDAAIPRMEP REPWVEQEGP QYWEWTTGYA KANAQTDRVA LRNLLRRYNQ SEAGSHTLQG MNGCDMGPDG RLLRGYHQHA YDGKDYISLN EDLRSWTAAD TVAQITQRFY EAEEYAEEFR TYLEGECLEL LRRYLENGKE TLQRADPPKA HVAHHPISDH EATLRCWALG FYPAEITLTW QRDGEEQTQD TELVETRPAG DGTFQKWAAV VVPPGEEQRY TCHVQHEGLP QPLILRWEQS PQPTIPI
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Molecular Weight
39 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-F, a member of the human leukocyte antigen (HLA) class I family, plays a crucial role in the immune response, particularly in the presentation of intracellular antigens to CD8+ T cells. Unlike other classical HLA molecules, HLA-F is primarily expressed in certain tissues and is known for its unique binding properties and interactions with killer immunoglobulin-like receptors (KIRs). Research on HLA-F has gained momentum due to its potential implications in autoimmune diseases, cancer, and organ transplantation. The understanding of HLA-F's structure, function, and regulation is essential for deciphering its role in immune tolerance and activation mechanisms. Moreover, the development of recombinant HLA-F proteins offers opportunities for therapeutic applications, such as the design of novel immunotherapies that can modulate the immune system's response. Investigating HLA-F can also enhance our understanding of its evolutionary significance and its interactions with pathogens. Consequently, ongoing studies focusing on HLA-F recombinant proteins aim to provide insights into their biological functions and potential applications in clinical settings, thereby contributing to advances in immunology and personalized medicine.
