Analytical Data
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基因名
PRKCI
- Application
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别名
PRKCI；DXS1179E；Protein kinase C iota type
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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
P41743
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表达区间
2-596aa
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氨基酸序列
PTQRDSSTM SHTVAGGGSG DHSHQVRVKA YYRGDIMITH FEPSISFEGL CNEVRDMCSF DNEQLFTMKW IDEEGDPCTV SSQLELEEAF RLYELNKDSE LLIHVFPCVP ERPGMPCPGE DKSIYRRGAR RWRKLYCANG HTFQAKRFNR RAHCAICTDR IWGLGRQGYK CINCKLLVHK KCHKLVTIEC GRHSLPQEPV MPMDQSSMHS DHAQTVIPYN PSSHESLDQV GEEKEAMNTR ESGKASSSLG LQDFDLLRVI GRGSYAKVLL VRLKKTDRIY AMKVVKKELV NDDEDIDWVQ TEKHVFEQAS NHPFLVGLHS CFQTESRLFF VIEYVNGGDL MFHMQRQRKL PEEHARFYSA EISLALNYLH ERGIIYRDLK LDNVLLDSEG HIKLTDYGMC KEGLRPGDTT STFCGTPNYI APEILRGEDY GFSVDWWALG VLMFEMMAGR SPFDIVGSSD NPDQNTEDYL FQVILEKQIR IPRSLSVKAA SVLKSFLNKD PKERLGCHPQ TGFADIQGHP FFRNVDWDMM EQKQVVPPFK PNISGEFGLD NFDSQFTNEP VQLTPDDDDI VRKIDQSEFE GFEYINPLLM SAEECV
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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
PRKCI (Protein Kinase C iota) is a serine/threonine kinase that plays a crucial role in various cellular processes, including cell proliferation, survival, and differentiation. Its involvement in cancer pathology has drawn significant attention in recent years, as elevated PRKCI expression is often associated with tumor progression and poor prognosis in several malignancies. Researchers have been exploring the potential of PRKCI as a therapeutic target, given its regulatory functions in key signaling pathways, such as those involving cell adhesion and migration. The study of PRKCI recombinant proteins serves multiple purposes: it aids in understanding the molecular mechanisms by which PRKCI influences tumor behavior, provides insights into its potential as a biomarker, and supports the development of PRKCI inhibitors for cancer therapy. Advances in biotechnology have enabled the production of high-purity PRKCI recombinant proteins, facilitating detailed biochemical and structural studies. Understanding the role of PRKCI in oncogenesis could lead to innovative strategies for targeted therapies, highlighting its importance in both basic research and clinical applications. As such, the study of PRKCI recombinant proteins is a promising avenue in the quest to elucidate cancer biology and improve therapeutic options for patients with malignancies associated with aberrant PRKCI activity.
