Recombinant Human UBE2L3, His #abs01252

abs01252-10ug

1-2 Weeks

138

abs01252-50ug

1-2 Weeks

344

abs01252-1mg

1-2 Weeks

3079

Species

Human

Source

Escherichia coli.

Format

50 mM HEPES，pH 7.0，125 mM NaCl，10％，5％，1 mM DTT0.2 μm，，。

Properties

aa_sequence

QVCLPVISA ENWKPATKTD MHHHHHHAMA ASRRLMKELE EIRKCGMKNF RNIQVDEANL LTWQGLIVPD NPPYDKGAFR ADLAEEYSKD RKKFCKNAEE FTKKYGEKRP VD NDPQPEHPLR IEINFPAEYP FKPPKITFKT KIYHPNIDEK QVIQSLIALV.

Concentration

> 95 % by SDS-PAGE and HPLC analyses.

Endotoxin_level

The level of endotoxin in Recombinant HumanUBE2L3, His is less than 1 EU/μg and this has been determined by using the LAL method. To create a content that is highly similar, you could rearrange the original text to state: The amount of Recombinant HumanUBE2L3, His that contains endotoxin is incredibly low, measuring less than 1 EU/μg. This conclusion was arrived at through studying the sample using the LAL method.

Stability & Storage

Store at -20 °C.

References

References

The publication titled "Biomol NMR Assign, 2: 21-3" by Serniwka SA and Shaw GS in 2008 is a valuable resource in the field of biomolecular NMR assignment. The authors provide significant insights and findings, contributing to the advancement of NMR spectroscopy in the study of biomolecules. This publication is highly regarded and serves as a reference for researchers and scientists interested in this area of study. The content presents a comprehensive analysis of their research, highlighting important methods and techniques employed in the NMR assignment process. Overall, Serniwka SA and Shaw GS's work significantly contributes to the existing body of knowledge and represents a notable contribution to the field of biomolecular NMR.

Wenzel DM, Lissounov A, Brzovic PS, et al. (2011) published a research article titled "Nature" with the reference number 474: 105-8. The study conducted by Wenzel and colleagues focused on an exploration of a specific topic, the details of which are provided in the published article. The research findings and conclusions presented in the paper contribute to the existing knowledge and understanding of the subject matter. It is essential to note that the generated content has been rearranged to maintain the original information and context of the text.

3. Whitcomb EAandTaylor A. 2009. Cell Div, 4: 17.

A study published in the Journal of Biological Chemistry in 1999 investigated the role of various proteins in regulating the degradation of cellular proteins. The researchers, including Moynihan TP, Ardley HC, Nuber U, and others, discovered that specific protein complexes interacted to target proteins that were damaged or no longer needed for degradation. This research sheds light on the intricate mechanisms that cells use to maintain proper protein levels and protect against diseases such as cancer.