Analytical Data
-
Gene name
SPDYA
- Application
-
Alternative Names
SPDYA; SPDY1; SPY1; Speedy protein A; Rapid inducer of G2/M progression in oocytes A; RINGO A; hSpy/Ringo A; Speedy-1; Spy1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q5MJ70
-
Expression Region
1-313aa
-
AA Sequence
MRHNQMCCET PPTVTVYVKS GSNRSHQPKK PITLKRPICK DNWQAFEKNT HNNNKSKRPK GPCLVIQRQD MTAFFKLFDD DLIQDFLWMD CCCKIADKYL LAMTFVYFKR AKFTISEHTR INFFIALYLA NTVEEDEEET KYEIFPWALG KNWRKLFPNF LKLRDQLWDR IDYRAIVSRR CCEEVMAIAP THYIWQRERS VHHSGAVRNY NRDEVQLPRG PSATPVDCSL CGKKRRYVRL GLSSSSSLSS HTAGVTEKHS QDSYNSLSMD IIGDPSQAYT GSEVVNDHQS NKGKKTNFLK KDKSMEWFTG SEE
-
Molecular Weight
36.4 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
SPDYA (SPRY Domain-containing Protein A) is a protein implicated in various cellular processes, including cell proliferation, differentiation, and apoptosis. Its role in the regulation of signal transduction pathways has garnered increasing interest in the field of molecular biology and biomedical research. SPDYA has been studied for its potential involvement in cancer progression, as its expression levels can be altered in various tumor types, suggesting a possible link to oncogenesis. Understanding the biochemistry and structure of SPDYA is crucial for elucidating its functional mechanisms and potential as a therapeutic target. Recent advancements in protein engineering and recombinant DNA technology have enabled researchers to produce and purify SPDYA in significant quantities, facilitating in-depth studies. Investigating the effects of SPDYA's molecular interactions, post-translational modifications, and its role in the cellular microenvironment may provide insights into its biological significance and therapeutic potential. This research is particularly relevant in the context of developing targeted therapies for diseases where SPDYA is dysregulated. Overall, the study of SPDYA and its recombinant protein forms represents a promising area of research with implications for understanding complex cellular functions and designing innovative medical treatments.
