Analytical Data
-
Gene name
MYL12A
- Application
-
Alternative Names
MLCB; MYL2B; MRLC3; MRCL3; HEL-S-24; RLC Myosin Regulatory Light Chain 3; Epididymis secretory protein Li 24; Myosin regulatory light chain 2, nonsarcomeric
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P19105
-
Expression Region
Thr10~Asp171
-
Molecular Weight
21kDa
-
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
MYL12A, or Myosin Light Chain 12A, is a crucial component of the myosin II motor protein family, playing a significant role in muscle contraction and various cellular processes such as cytokinesis, cell migration, and adhesion. It is primarily expressed in non-muscle tissues and is essential for the regulation of actin interaction and contraction in non-muscle cells. The study of MYL12A recombinant proteins has gained momentum due to their implications in understanding fundamental cellular mechanisms and their potential role in various diseases. Research has shown that dysregulation of MYL12A can be linked to several pathologies, including cancer, where altered cell migration and adhesion contribute to metastasis. The ability to produce recombinant MYL12A proteins enables researchers to investigate its biochemical properties, binding interactions, and functional significance in detail. Additionally, this research aids in elucidating the molecular basis of MYL12A in cellular functions and its contribution to disease processes. By studying MYL12A through recombinant techniques, scientists hope to unveil new therapeutic targets and innovative strategies for treating conditions associated with its dysregulation.
