Recombinant Human TAFA2 Protein

Beta LifeScience SKU/CAT #: BL-0770PS

Recombinant Human TAFA2 Protein

Beta LifeScience SKU/CAT #: BL-0770PS
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Product Overview

Tag N/A
Host Species Human
Synonym Family with sequence similarity 19 (chemokine (C-C motif)-like) member A2, Chemokine-like protein TAFA-2, protein FAM19A2.
Background TAFA-2 is a 11 kDa secreted protein that belongs to the FAM19/TAFA family of chemokine-like proteins. Similar to other FAM19/TAFA family members, mature TAFA-1 contains 10 regularly spaced cysteine residues with the same pattern: CX7CCX13CXCX14CX11CX4CX5CX10C (C symbolizes a conserved cysteine residue and X symbolizes any noncysteine amino acid). Human TAFA-2 is 97% aa identical to mouse TAFA-2 and is expressed in the central nervous system (CNS), colon, heart, lung, spleen, kidney, and thymus, however its expression in the CNS is 50 to 1000 fold higher than in other tissues. The biological roles of TAFA family members have not yet been determined.
Description TAFA2 Human Recombinant expressed in E.Coli is a non-glycosylated, Polypeptide chain containing 101a.a. and having a molecular weight of 11.2kDa. The TAFA2 is purified by unique purification methods.
Source E.coli
AA Sequence ANHHKAHHVK TGTCEVVALH RCCNKNKIEE RSQTVKCSCF PGQVAGTTRA APSCVDASIV EQKWWCHMQP CLEGEECKVL PDRKGWSCSS GNKVKTTRVT H
Purity >97.0% as determined by(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
Endotoxin <1.0 EU per μg by the LAL method.
Bioactivity Fully biologically active when compared to standard. Measured by its ability to enhance neurite outgrowth of E16-E18 rat embryonic cortical neurons.
Formulation The protein was lyophilized from a 0.2µm filtered concentrated solution in 1xPBS, pH7.4.
Stability Recombinant protein is stable for 12 months at -70°C
Usage For Research Use Only
Storage Lyophilized TAFA2 although stable at room temperature for 3 weeks, should be stored desiccated below -18C. Upon reconstitution TAFA2 should be stored at 4C between 2-7 days and for future use below -18C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent 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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