Analytical Data
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Gene name
BSPRY
- Application
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Alternative Names
B box and SPRY domain containing; B box and SPRY domain containing Protein; B box and SPRY domain containing Protein
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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
Q5W0U4
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Expression Region
1-402aa
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AA Sequence
MSAEGAEPGP GSGSGPGPGP LCPEHGQALS WFCGSERRPV CAACAGLGGR CRGHRIRRAE ERAEELRNKI VDQCERLQLQ SAAITKYVAD VLPGKNQRAV SMASAARELV IQRLSLVRSL CESEEQRLLE QVHGEEERAH QSILTQRVHW AEALQKLDTI RTGLVGMLTH LDDLQLIQKE QEIFERTEEA EGILDPQESE MLNFNEKCTR SPLLTQLWAT AVLGSLSGTE DIRIDERTVS PFLQLSDDRK TLTFSTKKSK ACADGPERFD HWPNALAATS FQNGLHAWMV NVQNSCAYKV GVASGHLPRK GSGSDCRLGH NAFSWVFSRY DQEFRFSHNG QHEPLGLLRG PAQLGVVLDL QVQELLFYEP ASGTVLCAHH VSFPGPLFPV FAVADQTISI VR
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Molecular Weight
44.3 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
BSPRY (B-Cell Specific Regulator of Y-box Binding Protein) is a protein initially identified for its role in B-cell development and function, and it belongs to the family of Y-box binding proteins. Its significance has emerged in various contexts, particularly in immunology and cancer research. Studies have highlighted BSPRY's involvement in regulating gene expression and modulating immune responses, attributing it a critical role in the maturation and activation of B-cells. Recent investigations have also uncovered its potential implications in tumor biology, where altered expression levels of BSPRY have been associated with the progression of certain cancers. This protein's unique structure and functional versatility make it an attractive candidate for further exploration in therapeutic applications. Researchers are now focusing on elucidating the molecular mechanisms by which BSPRY influences B-cell signaling and its interactions with other cellular pathways. Understanding BSPRY's functional dynamics could pave the way for novel interventions in immune disorders and cancer, potentially leading to the development of targeted therapies that modulate immune responses or inhibit tumor growth. Overall, the multifaceted roles of BSPRY underscore its importance as a focal point of research in both basic and applied biomedical sciences.
