Analytical Data
-
基因名
DNPH1
- Application
-
别名
C6orf108; RCL
-
种属
Human
-
表达系统
E. coli
-
标签
Strep;His
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
O43598-1
-
表达区间
A2-T174
-
蛋白长度
Full Length of Isoform-1
-
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.
Quality inspection process
Related Products
Protein Description
DNPH1, or Dipeptidyl Peptidase-like Protein 1, is a protein that has garnered significant interest in the field of molecular biology and biochemistry due to its role in various cellular processes. It is primarily associated with regulating metabolic pathways and has been implicated in the modulation of immune responses and cell signaling. Current research indicates that DNPH1 is involved in the processing of peptides, which is essential for the presentation of antigens and the activation of T cells. Moreover, aberrations in DNPH1 expression have been linked to various diseases, including metabolic disorders and cancers. Given its potential as a therapeutic target, the recombinant expression of DNPH1 has become a focal point for researchers aiming to elucidate its structure-function relationship and biological significance. By producing and analyzing recombinant DNPH1, scientists aim to better understand its enzymatic activity, substrate specificity, and interaction with other cellular components. Such studies may pave the way for novel therapeutic interventions, especially in conditions where DNPH1 dysregulation contributes to disease pathology. This research not only expands our understanding of DNPH1 but also provides insight into its potential roles in health and disease.












