Recombinant Human Dna-Directed Dna/Rna Polymerase Mu (POLM) Protein (His)

Name: Recombinant Human Dna-Directed Dna/Rna Polymerase Mu (POLM) Protein (His)
Brand: Beta LifeScience
SKU: BLC-10314P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Product Overview

Description	Recombinant Human Dna-Directed Dna/Rna Polymerase Mu (POLM) Protein (His) is produced by our Yeast expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q9NP87
Target Symbol	POLM
Synonyms	DNA-directed DNA polymerase mu; DNA-directed DNA/RNA polymerase mu; DPOLM_HUMAN; FLJ35482; Pol iota; Pol Mu; Polm; POLM protein; Polymerase (DNA directed) mu; Polymerase DNA directed mu; Tdt N; Tdt-N; TdtN; Terminal transferase
Species	Homo sapiens (Human)
Expression System	Yeast
Tag	N-10His
Target Protein Sequence	MLPKRRRARVGSPSGDAASSTPPSTRFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWLTESLGAGQPVPVECRHRLEVAGPRKGPLSPAWMPAYACQRPTPLTHHNTGLSEALEILAEAAGFEGSEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRSERYQTMKLFTQIFGVGVKTADRWYREGLRTLDDLREQPQKLTQQQKAGLQHHQDLSTPVLRSDVDALQQVVEEAVGQALPGATVTLTGGFRRGKLQGHDVDFLITHPKEGQEAGLLPRVMCRLQDQGLILYHQHQHSCCESPTRLAQQSHMDAFERSFCIFRLPQPPGAAVGGSTRPCPSWKAVRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSRKEKGLWLNSHGLFDPEQKTFFQAASEEDIFRHLGLEYLPPEQRNA
Expression Range	1-494aa
Protein Length	Full Length
Mol. Weight	57.3 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ). Participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination.
Subcellular Location	Nucleus.
Protein Families	DNA polymerase type-X family
Database References	HGNC: 9185 OMIM: 606344 KEGG: hsa:27434 STRING: 9606.ENSP00000242248 UniGene: Hs.596982
Tissue Specificity	Expressed in a number of tissues. Abundant in thymus.

Gene Functions References

Polmu point mutations affecting 2 conserved adjacent residues located in the 8 kDa domain, G174S and R175H, limit the efficiency of accurate NHEJ by Polmu in vitro and in vivo due to decreased template dependency during NHEJ, which renders the error-rate of the mutants higher due to the ability of Polmu to randomly incorporate nucleotides at DSBs. PMID: 28973441
Structural accommodation of ribonucleotide incorporation by the DNA repair enzyme polymerase Mu has been described. PMID: 28911097
analysis of template-dependent synthesis by human polymerase mu PMID: 26240373
A study of how Polmu fixes and/or orients the mobile Loop1 part of the protein in accordance with the substrate on which it is polymerizing. PMID: 24878922
specific loop 1 residues contribute to Pol mu's unique ability to catalyze template-dependent NHEJ of DSBs with unpaired 3' ends PMID: 24487959
evidence suggests that Polmu could be regulated in vivo by phosphorylation of the BRCT domain (Ser12/Thr21) and of Ser372, affecting the function of loop1; Polmu's most distinctive activities would be turned off at specific cell-cycle phases (S and G2), when these functions might be harmful to the cell PMID: 23933132
A specific N-terminal extension of the 8 kDa domain of DNA polymerase mu is potentially implicated in the maintenance of a closed conformation throughout the catalytic cycle, and this study indicated that it could be a target of Cdk phosphorylation. PMID: 23935073
A physiological concentration of Mn(2+) ions did benefit Polmicro-mediated non-homologous end joining by improving the efficiency and accuracy of nucleotide insertion. PMID: 23275568
The study points at human Polmicro residues His(329) and Arg(387) as responsible for regulating nucleotide expansions occurring during DNA repair transactions, either promoting or blocking, respectively, iterative polymerization. PMID: 23143108
The results uncovered a new DNA-binding function for the BRCT domain of Polmicro and demonstrated the importance of several residues located at the primer-binding region, for both DNA-binding and polymerization activities. PMID: 23034807
Pol mu binds to DNA through its amino-terminal and pol beta-like regions. PMID: 22897684
DNA polymerase mu performs DNA synthesis at a AAF lesion PMID: 11972346
Association of DNA polymerase mu (pol mu) with Ku and ligase IV: role for pol mu in end-joining double-strand break repair. PMID: 12077346
DNA polymerase mu acts in response to several types of DNA damage with a lesion bypass mechanism PMID: 12228225
expression in B-cell non-Hodgkin's lymphomas PMID: 12368208
Pol mu's substrate specificity is similar to that of pol beta in most respects but has an approximately 1,000-fold-reduced ability to discriminate against ribonucleotides compared to pol beta PMID: 12640116
human DNA polymerase mu has a template-dependent, sequence-independent nucleotidyl transferase activity PMID: 14581466
Poliota incorporates a C opposite the gamma-HOPdG adduct with nearly the same efficiency as opposite a nonadducted G residue. The subsequent extension step is performed by Polkappa, which efficiently extends from the C incorporated opposite the adduct. PMID: 15199127
DNA polymerase mu has been overexpressed, purified, and its fidelity estimated for incorporation of both deoxynucleotides and ribonucleotides based on pre-steady-state kinetic data under single-turnover conditions. PMID: 15504045
Overexpression of DNA polymerase mu in a Burkitt's lymphoma cell line induced an increase in somatic mutations specifically targeted to G/C residues in immunoglobulin variable genes. PMID: 15520469
Pol mu promotes accuracy during Ig kappa recombination. PMID: 16061182
When the terminal deoxynucleotidyl transferase (TdT) loop1 was deleted, human Polmu lacked TdT activity but improved DNA-binding and DNA template-dependent polymerization. PMID: 16963491
Studies shed light on the mechanism by which a rate-limited terminal transferase activity in Polmu could regulate the balance between accuracy and necessary efficiency, providing some variability during NHEJ. PMID: 19805281

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.