Analytical Data
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Gene name
HHLA2
- Application
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Alternative Names
B7 Homolog 7; B7-H7; HHLA2
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Species
Cynomolgus
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Source
HEK293
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Tag
C-Avi;C-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
XP_005548285.1
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Expression Region
I21-N345
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Molecular Weight
66-80 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
Related Products
Protein Description
HHLA2 (Human High Mobility Group Protein 2) is a member of the B7 family of immune checkpoint molecules, playing a significant role in regulating immune responses, particularly in tumor microenvironments. Identified in recent years, HHLA2 has garnered attention for its potential implications in cancer biology as it interacts with various receptors, influencing T-cell activation and proliferation. Research has shown that HHLA2 is expressed in multiple tumor types, where it may contribute to immune evasion by inhibiting T-cell functions. Consequently, the exploration of HHLA2 as a therapeutic target has emerged as a promising avenue in cancer immunotherapy. Recombinant proteins of HHLA2 are utilized in numerous studies to better understand its biological functions, binding mechanisms, and the development of potential monoclonal antibodies targeting this pathway. By investigating the structure and function of HHLA2, researchers aim to elucidate its role in immune regulation, determine its prognostic value in cancer, and advance the design of innovative therapeutic strategies that can enhance anti-tumor immunity. This research may pave the way for novel immune-modulatory therapies, potentially improving outcomes for patients with malignancies characterized by high expression of HHLA2.
