Recombinant Human S100A1 Protein

Beta LifeScience SKU/CAT #: BLPSN-4106

Recombinant Human S100A1 Protein

Beta LifeScience SKU/CAT #: BLPSN-4106
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Product Overview

Tag N/A
Host Species Human
Accession NP_006262.1
Synonym S100, S100-alpha, S100A
Background S1A1 is a Ca2+binding protein of the EF-hand type that belongs to the S1 protein family. S1 proteins consisting of at least 19 members exist as dimers in the cytoplasm and/or nucleus of a wide range of cells, and are involved in the regulation of a number of cellular processes such as cell-cycle progression and cell differentiation.This protein has been shown to function in the processes including stimulation of Ca2+-induced Ca2+ release, inhibition of microtubule assembly, and inhibition of PKC-mediated phosphorylation.. Phosphoglucomutase is a target protein whose activity is antagonistically regulated by S1A1, and recently, S1A1 is also identified as a potent molecular chaperone and a new member of the Hsp7/Hsp9 multichaperone complex. S1A1 displays a tissue-specific expression pattern with highest levels in myocardium and is considered to be an important regulator of cardiac contractility. Accordingly, reduced expression or mutations of S1A1 gene have been implicated in cardiomyopathies.
Description A DNA sequence encoding the human S100A1 (NP_006262.1) (Met 1-Ser 94) was expressed.
Source E.coli
Predicted N Terminal Met 1
AA Sequence Met 1-Ser 94
Molecular Weight The recombinant human S100A1 consists of 94 a.a. and has a predicted molecular mass of 10.5 kDa.
Purity >97% as determined by SDS-PAGE
Endotoxin Please contact us for more information.
Bioactivity 1. Measured by its binding ability in a functional ELISA.2. Immobilized recombinant human Fc-S100B at 10 ug/mL (100 ul/well) can bind biotinylated human S100A1 with a linear range of 15.6-250 ng/mL.3. Measured by its ability to bind human His-S100B in functional ELISA.
Formulation Lyophilized from sterile PBS, 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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