Analytical Data
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Gene name
GAPC1
- Application
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Alternative Names
GAPC1；GAPC；GAPDH；Glyceraldehyde-3-phosphate dehydrogenase GAPC1. cytosolic
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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
P25858
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Expression Region
1-338aa
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AA Sequence
MADKKIRIGINGFGRIGRLVARVVLQRDDVELVAVNDPFITTEYMTYMFKYDSVHGQWKHNELKIKDEKTLLFGEKPVTVFGIRNPEDIPWAEAGADYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEHEYKSDLDIVSNASCTTNCLAPLAKVINDRFGIVEGLMTTVHSITATQKTVDGPSMKDWRGGRAASFNIIPSSTGAAKAVGKVLPALNGKLTGMSFRVPTVDVSVVDLTVRLEKAATYDEIKKAIKEESEGKLKGILGYTEDDVVSTDFVGDNRSSIFDAKAGIALSDKFVKLVSWYDNEWGYSSRVVDLIVHMSKA
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Molecular Weight
44.4 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
GAPC1 (GTPase-activating protein, p120) is a critical regulatory protein involved in various cellular processes, including cytoskeletal organization, intracellular signaling, and cellular proliferation. Its primary role is to facilitate GTP hydrolysis in GTP-binding proteins, thereby influencing the activity of downstream signaling pathways. Research into GAPC1 has gained momentum due to its association with several physiological and pathological conditions, including cancer progression and metastasis. Studies have revealed that aberrant expression or mutations of GAPC1 can disrupt normal cellular signaling mechanisms, leading to enhanced cell motility and invasion. Additionally, GAPC1’s interactions with other proteins in the Rho family of GTPases are pivotal for maintaining cellular architecture and regulating cell shape. Investigating GAPC1 at the molecular level, particularly through the creation and characterization of recombinant GAPC1 proteins, provides insights into its structural properties and functional dynamics. Recombinant GAPC1 proteins can serve as valuable tools for elucidating the mechanistic roles of this protein in cellular pathways and for potential therapeutic interventions targeting GAPC1-related diseases. Overall, the study of GAPC1 not only enhances our understanding of fundamental biological processes but also opens avenues for novel diagnostic and therapeutic strategies in oncology and other conditions linked to GAPC1 dysfunction.
