Recombinant Mouse S100A11 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-4111

Recombinant Mouse S100A11 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-4111
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Product Overview

Tag His
Host Species Mouse
Accession NP_058020.1
Synonym cal, Emap1, EMAPI, S100A11, S100a14, S100c
Background Protein S1-A11, also known as S1 calcium-binding protein A11, S1A11 and MLN7, is a member of theS-1 family. S1A11 is widely expressed in multiple tissues, and is located in cytoplasm, nucleus, and even cell periphery. S1A11 exists as a non-covalent homodimer with an antiparallel conformation. Ca(2+) binding to S1A11 would trigger conformational changes which would expose the hydrophobic cleft of S1A11 and facilitate its interaction with target proteins. As a dual cell growth mediator, S1A11 acts as either a tumor suppressor or promoter in many different types of tumors and would play respective roles in influencing the proliferation of the cancer cells. In the nucleus, S1A11 suppresses the growth of keratinocytes through p21 (CIP1/WAF1) activation and induces cell differentiation. S1A11 is also a novel diagnostic marker in breast carcinoma.
Description A DNA sequence encoding the mouse S100A11 (NP_058020.1) (Met1-Ile98) was expressed with a His tag at the N-terminus.
Source E.coli
Predicted N Terminal Met
AA Sequence Met1-Ile98
Molecular Weight The recombinant mouse S100A11 consists of 114 a.a. and predicts a molecular mass of 13.2 KDa. It migrates as an approximately 14 KDa band in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
Formulation Lyophilized from sterile PBS, 10% glycerol, pH 7.4..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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