Analytical Data
-
Gene name
ARPM1
- Application
-
Alternative Names
ACTRT3; ARPM1Actin-related Protein T3; ARP-T3; Actin-related Protein M1
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9BYD9
-
Expression Region
1-372aa
-
AA Sequence
MNHCQLPVVIDNGSGMIKAGVAGCREPQFIYPNIIGRAKGQSRAAQGGLELCVGDQAQDWRSSLFISYPVERGLITSCEDMEIMWKHIYDYNLKLKPCDGPVLITEPALNPLANRQQITEMFFEHLGVPAFYMSIQAVLALFAAGFTTGLVLNSGAGVTQSVPIFEGYCLPHGVQQLDLAGLDLTNYLMVLMKNHGIMLLSASDRKIVEDIKESFCYVAMNYEEEMAKKPDCLEKVYQLPDGKVIQLHDQLFSCPEALFSPCHMNLEAPGIDKICFSSIMKCDTGLRNSFFSNIILAGGSTSFPGLDKRLVKDIAKVAPANTAVQVIAPPERKISVWMGGSILASLSAFQDMWITAAEFKEVGPNIVHQRCF
-
Molecular Weight
67.3 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
ARPM1, a member of the actin-regulating proteins family, has gained attention in recent years due to its potential roles in cellular processes such as cytoskeletal dynamics, cell migration, and signaling pathways. The study of ARPM1 is particularly important as it may contribute to our understanding of various physiological and pathological conditions, including cancer metastasis and neurodegenerative diseases. Recent research has focused on the reconstitution of ARPM1 as a recombinant protein to elucidate its functional properties and mechanisms of action at a molecular level. By expressing ARPM1 in model systems and utilizing techniques such as co-immunoprecipitation and fluorescence microscopy, researchers aim to reveal how this protein interacts with actin filaments and other binding partners. Moreover, understanding the structural characteristics of ARPM1 through techniques like X-ray crystallography and NMR spectroscopy can provide insights into its regulation and role within the cell. Overall, the ongoing investigation of ARPM1 as a recombinant protein is pivotal for expanding our knowledge of actin dynamics and its implications in health and disease.
