Analytical Data
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基因名
TRIM22
- Application
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别名
TRIM22; RNF94; STAF50; E3 ubiquitin-Protein ligase TRIM22; EC 2.3.2.27; 50 kDa-stimulated trans-acting factor; RING finger Protein 94; RING-type E3 ubiquitin transferase TRIM22; Staf-50; Tripartite motif-containing Protein 22
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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
Q8IYM9
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表达区间
1-498 aa
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氨基酸序列
MDFSVKVDIE KEVTCPICLE LLTEPLSLDC GHSFCQACIT AKIKESVIIS RGESSCPVCQ TRFQPGNLRP NRHLANIVER VKEVKMSPQE GQKRDVCEHH GKKLQIFCKE DGKVICWVCE LSQEHQGHQT FRINEVVKEC QEKLQVALQR LIKEDQEAEK LEDDIRQERT AWKNYIQIER QKILKGFNEM RVILDNEEQR ELQKLEEGEV NVLDNLAAAT DQLVQQRQDA STLISDLQRR LRGSSVEMLQ DVIDVMKRSE SWTLKKPKSV SKKLKSVFRV PDLSGMLQVL KELTDVQYYW VDVMLNPGSA TSNVAISVDQ RQVKTVRTCT FKNSNPCDFS AFGVFGCQYF SSGKYYWEVD VSGKIAWILG VHSKISSLNK RKSSGFAFDP SVNYSKVYSR YRPQYGYWVI GLQNTCEYNA FEDSSSSDPK VLTLFMAVPP CRIGVFLDYE AGIVSFFNVT NHGALIYKFS GCRFSRPAYP YFNPWNCLVP MTVCPPSS
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分子量
56.9 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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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
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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.
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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.
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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
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Protein Description
TRIM22, a member of the Tripartite Motif (TRIM) protein family, has garnered significant attention due to its multifaceted roles in immune response and viral defense mechanisms. This protein is characterized by a RING finger domain, which is integral to its E3 ubiquitin ligase activity, allowing it to modulate various cellular pathways through protein degradation and modification. Previous studies have indicated that TRIM22 plays a crucial role in restricting viral replication, particularly against HIV and other RNA viruses, by targeting viral proteins for ubiquitination and subsequent degradation. Additionally, TRIM22 has been implicated in the regulation of interferon signaling pathways, enhancing the host's antiviral response. The exploration of TRIM22 as a recombinant protein has advanced our understanding of its structural and functional properties, providing insights into its potential as a therapeutic target for viral infections and its involvement in various diseases, including cancer and autoimmune disorders. Researchers are actively investigating the mechanistic pathways influenced by TRIM22, aiming to harness its properties for innovative therapeutic strategies. This evolving field of study underscores the importance of TRIM22 in host-pathogen interactions and its potential as a biomarker for disease prognosis and treatment outcomes. As we delve deeper into the complexities of TRIM22, the developments in recombinant protein technology offer promising avenues for the design of novel vaccines and antiviral therapies, making it a pivotal focus of current biomedical research.
