Analytical Data
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Gene name
MYL12B
- Application
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Alternative Names
DAPK3;ZIPK;Death-associated Protein kinase 3
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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
O14950
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Expression Region
1-172aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMSSKKA KTKTTKKRPQ RATSNVFAMF DQSQIQEFKE AFNMIDQNRD GFIDKEDLHD MLASLGKNPT DAYLDAMMNE APGPINFTMF LTMFGEKLNG TDPEDVIRNA FACFDEEATG TIQEDYLREL LTTMGDRFTD EEVDELYREA PIDKKGNFNY IEFTRILKHG AKDKDD
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Molecular Weight
22 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
Related Products
Protein Description
MYL12B, also known as myosin light chain 12B, is a crucial protein encoded by the MYL12B gene and plays a significant role in the regulation of smooth muscle contraction and various cellular processes, such as cell migration and shape maintenance. The protein is a part of the myosin-II complex, which is essential for muscle contraction and cellular motility. Recent studies have highlighted the importance of MYL12B in various physiological and pathological contexts, including its involvement in cancer cell invasion, metastasis, and the modulation of inflammatory responses. Researchers are increasingly interested in the functional implications of MYL12B in both normal and diseased states, particularly its post-translational modifications and interactions with other cellular components. Additionally, the reconstitution of MYL12B as a recombinant protein enables detailed structural and functional studies, paving the way for potential therapeutic applications aimed at targeted modulation of its activity. Understanding the intricate roles of MYL12B could provide valuable insights into relevant biological pathways and contribute to the development of novel strategies for treating diseases characterized by aberrant cell behavior, including cancer and cardiovascular disorders. Thus, the study of MYL12B and its recombined forms is of great importance in the fields of molecular biology, pharmacology, and medical research, highlighting the need for continued investigation into its mechanisms and potential interventions.
