Analytical Data
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Gene name
GUCY1A2
- Application
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Alternative Names
Guanylate cyclase soluble subunit alpha-2; GUCY1A2; GCS-alpha-2; GUC1A2; GUCSA2
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Species
Human
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Source
E. coli
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Tag
N-6*His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P33402
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Expression Region
G500-L732
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AA Sequence
GDVAQQLWQGQQVQARKFDDVTMLFSDIVGFTAICAQCTPMQVISMLNELYTRFDHQCGFLDIYKVETIGDAYCVAAGLHRKSLCHAKPIALMALKMMELSEEVLTPDGRPIQMRIGIHSGSVLAGVVGVRMPRYCLFGNNVTLASKFESGSHPRRINVSPTTYQLLKREESFTFIPRSREELPDNFPKEIPGICYFLEVRTGPKPPKPSLSSSRIKKVSYNIGTMFLRETSL
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Protein Length
Partial
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Molecular Weight
28 kDa, based on SDS-PAGE under reducing conditions
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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
GUCY1A2, part of the guanylate cyclase family, encodes the alpha-1 subunit of soluble guanylate cyclase, an essential enzyme involved in the nitric oxide (NO) signaling pathway. This pathway plays a crucial role in various physiological processes, including vasodilation, neurotransmission, and cellular signaling. Mutations in GUCY1A2 have been correlated with various cardiovascular and neurological disorders, highlighting its significance in human health and disease. Recent studies have focused on the recombinant expression of GUCY1A2 to better understand its function and regulatory mechanisms, as well as to develop potential therapeutic strategies for conditions associated with its dysregulation. Recombinant GUCY1A2 protein provides a versatile tool for biochemical assays and structural studies, facilitating the exploration of its interaction with NO and other signaling molecules, and contributing to drug discovery efforts aimed at modulating guanylate cyclase activity. Enhanced understanding of GUCY1A2's role in cellular processes could lead to innovative therapeutic approaches for managing diseases linked to nitric oxide signaling, thus underscoring the importance of continued research in this area.
