Analytical Data
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Gene name
IRGC
- Application
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Alternative Names
IRGC; IIGP5; IRGC1Interferon-inducible GTPase 5; EC 3.6.5.-; Immunity-related GTPase cinema 1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6NXR0
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Expression Region
1-463aa
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AA Sequence
MATSKLPVVPGEEENTILMAKERLEALRTAFESGDLPQAASHLQELLASTESIRLEVGVTGESGAGKSSLINALRGLEAEDPGAALTGVMETTMQPSPYPHPQFPDVTLWDLPGAGSPGCPADKYLKQVDFSRYDFFLLVSPRRCGAVETRLAAEILCQGKKFYFVRTKVDEDLAATRTQRPSGFREAAVLQEIRDHCAERLREAGVADPRIFLVSNLSPARYDFPTLVSTWEHDLPSHRRHAGLLSLPDISLEALQKKKAMLQEQVLKTALVLGVIQALPVPGLAAAYDDALLIHSLRGYHRSFGLDDDSLAKLAEQVGKQAGDLRSVIRSPLANEVSPETVLRLYSQSSDGAMRVARAFERGIPVFGTLVAGGISFGAVYTMLQGCLNEMAEDAQRVRIKALEDDEPQPEVSLEVASDNGVEKGGSGEGGGEEAPLSTCRKLGLLLKYILDSWKKHDSEEK
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Molecular Weight
76.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
The study of recombinant proteins derived from the Iranian Revolutionary Guard Corps (IRGC) is significant in the context of biotechnology and molecular biology, particularly for their potential applications in medicine and immunology. Recombinant proteins are produced through the expression of cloned genes in host cells, allowing for the mass production of proteins that are critical for various biological functions. In recent years, interest in IRGC-related proteins has surged due to their roles in military and security contexts, particularly in understanding their implications in national defense strategies and biotechnological applications. Researchers are exploring the bioengineering of these proteins to develop vaccines, therapeutics, and diagnostic tools, which could enhance public health and safety. Additionally, studying these proteins can provide insights into the mechanisms by which IRGC-related entities operate, potentially aiding in counter-terrorism efforts and international security analysis. Through advanced recombinant DNA technology, the characterization and functional analysis of these proteins provide a deeper understanding of their structure, function, and potential interactions with biological systems. This research holds promise for not only advancing scientific knowledge but also addressing pressing security concerns associated with IRGC activities and biological warfare.
