关键信息
-
基因名
BETVIII
- 应用
-
别名
BETVIII；Calcium-binding allergen Bet v 3
-
种属
Human
-
表达系统
E. coli
-
标签
His tag N-Terminus
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P43187
-
表达区间
1-205aa
-
氨基酸序列
MPCSTEAMEKAGHGHASTPRKRSLSNSSFRLRSESLNTLRLRRIFDLFDK NSDGIITVDELSRALNLLGLETDLSELESTVKSFTREGNIGLQFEDFISL HQSLNDSYFAYGGEDEDDNEEDMRKSILSQEEADSFGGFKVFDEDGDGYI SARELQMVLGKLGFSEGSEIDRVEKMIVSVDSNRDGRVDFFEFKDMMRSV LVRSS
-
分子量
43 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
-
稳定性测试
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.
-
保存条件 & 期限
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.
-
运输条件
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.
质检流程
相关产品
背景信息
BETVIII (Bromodomain and Extra-Terminal Domain-containing protein VIII) is a member of the bromodomain and extraterminal (BET) protein family, which plays a crucial role in regulating gene expression. Research on BET proteins has gained significant attention due to their involvement in various cellular processes, including transcriptional regulation, chromatin remodeling, and cell differentiation. BETVIII, in particular, has been implicated in the pathogenesis of several diseases, including cancer and inflammatory disorders, making it a potential therapeutic target. The study of the structural and functional properties of BETVIII is essential for understanding its precise role in these biological processes. Advances in techniques such as cryo-electron microscopy and X-ray crystallography have enabled researchers to elucidate the complex interactions between BETVIII and its binding partners, paving the way for the development of small-molecule inhibitors that could disrupt these interactions. As a result, the investigation of BETVIII and its potential as a drug target represents a promising avenue for innovative therapeutic strategies aimed at treating diseases associated with dysregulated gene expression.
