Analytical Data
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Gene name
MYL7
- Application
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Alternative Names
MYL7;MYL2A;MYLC2A;Myosin regulatory light chain 2. atrial isoform
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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
Q01449
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Expression Region
1-175aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMASRKA GTRGKVAATK QAQRGSSNVF SMFEQAQIQE FKEAFSCIDQ NRDGIICKAD LRETYSQLGK VSVPEEELDA MLQEGKGPIN FTVFLTLFGE KLNGTDPEEA ILSAFRMFDP SGKGVVNKDE FKQLLLTQAD KFSPAEVEQM FALTPMDLAG NIDYKSLCYI ITHGDEKEE
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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
MYL7, also known as myosin light chain 7, is a crucial component of the myosin complex involved in muscle contraction and various cellular processes. It plays a significant role in cardiac and skeletal muscle function, as well as in the regulation of cell motility and cytoskeletal dynamics. Abnormal expression of MYL7 has been associated with various cardiovascular diseases, including heart failure and hypertrophy. Given its pivotal role in muscle biology and potential implications in pathological conditions, there has been a growing interest in studying the structure, function, and regulatory mechanisms of MYL7. Recombinant MYL7 protein is often generated to facilitate in-depth investigations into its biochemical properties, interactions with other proteins, and contributions to muscle pathology. The production of MYL7 as a recombinant protein allows researchers to analyze its effects in controlled experimental settings, providing insights into its role in muscle contraction and other physiological processes. Understanding MYL7's function at the molecular level could lead to novel therapeutic strategies for treating diseases related to muscle dysfunction. Furthermore, exploring the interaction of MYL7 with other signaling pathways and proteins might uncover new regulatory mechanisms that underpin muscle health and disease, making MYL7 a significant target for biomedical research.
