Analytical Data
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Gene name
MYL9
- Application
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Alternative Names
MYL9;MLC2;MRLC1;MYRL2;Myosin regulatory light polypeptide 9
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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
P24844
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Expression Region
1-172aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MSSKRAKAKT TKKRPQRATS NVFAMFDQSQ IQEFKEAFNM IDQNRDGFID KEDLHDMLAS LGKNPTDEYL EGMMSEAPGP INFTMFLTMF GEKLNGTDPE DVIRNAFACF DEEASGFIHE DHLRELLTTM GDRFTDEEVD EMYREAPIDK KGNFNYVEFT RILKHGAKDK DD
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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
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Protein Description
MYL9, or Myosin Light Chain 9, is a key component of the cytoskeletal system, primarily involved in muscle contraction and cellular motility. Research into MYL9 has gained significant attention due to its role in regulating smooth muscle contraction, endothelial function, and various cellular processes, including cytokinesis and cell adhesion. The protein is a critical part of the myosin complex, where it interacts with myosin heavy chains to regulate the contractile activity of non-muscle cells. Alterations in MYL9 expression and function have been implicated in various diseases, including cardiovascular conditions, cancer metastasis, and other pathologies characterized by aberrant cell movement and contractility. Understanding MYL9 at the molecular level through recombinant protein studies is essential for elucidating its functional mechanisms and potential therapeutic targets. This research often involves the expression of MYL9 using recombinant DNA technology to produce the protein in various expression systems, facilitating subsequent functional assays and structural analyses. These studies pave the way for novel interventions aimed at modulating MYL9 activity, with implications for treating conditions associated with dysfunctional cytoskeletal dynamics. Overall, the investigation of MYL9 recombinant protein contributes significantly to our understanding of cellular mechanics and the potential development of targeted therapies in multi-faceted diseases.
