Analytical Data
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Gene name
GEM
- Application
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Alternative Names
GEM; KIRGTP-binding protein GEM; GTP-binding mitogen-induced T-cell protein; RAS-like protein KIR
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P55040
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Expression Region
1-296aa
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AA Sequence
MTLNNVTMRQ GTVGMQPQQQ RWSIPADGRH LMVQKEPHQY SHRNRHSATP EDHCRRSWSS DSTDSVISSE SGNTYYRVVL IGEQGVGKST LANIFAGVHD SMDSDCEVLG EDTYERTLMV DGESATIILL DMWENKGENE WLHDHCMQVG DAYLIVYSIT DRASFEKASE LRIQLRRARQ TEDIPIILVG NKSDLVRCRE VSVSEGRACA VVFDCKFIET SAAVQHNVKE LFEGIVRQVR LRRDSKEKNE RRLAYQKRKE SMPRKARRFW GKIVAKNNKN MAFKLKSKSC HDLSVL
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Molecular Weight
33.9 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
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Protein Description
GEM (GTPase-activating proteins) are a family of proteins that play crucial roles in cellular signal transduction processes by regulating the activity of small GTPases, which are key players in various signaling pathways. The dysfunction of these proteins is linked to a range of diseases, including cancer and neurodegenerative disorders. In recent years, the study of GEM recombinant proteins has gained momentum as researchers seek to understand their structural and functional characteristics in detail. By producing these proteins in a recombinant form, scientists can examine their interactions, post-translational modifications, and the impact of specific mutations on their behavior. This research not only elucidates the fundamental mechanisms of cellular signaling but also paves the way for the development of novel therapeutic strategies aimed at targeting these pathways. Recent advancements in protein expression systems and purification techniques have further accelerated the exploration of GEM proteins, allowing for high-yield production and functional assays. The ongoing studies are expected to provide valuable insights into the regulatory roles of GEM proteins in health and disease, facilitating the identification of potential biomarkers and therapeutic targets. Through a better understanding of GEM recombinant proteins, researchers hope to unlock new avenues for treating conditions associated with GTPase dysregulation, highlighting the significance of these studies in the field of molecular biology and medicine.
