Product Details

Purity

Greater than 85% as determined by SDS-PAGE.

Target Names

POLM

Uniprot No.

Q9NP87

Research Area

others

Alternative Names

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)

Source

E.coli

Expression Region

1-494aa

Target Protein Sequence

MLPKRRRARVGSPSGDAASSTPPSTRFPGVAIYLVEPRMGRSRRAFLTGLARSKGFRVLDACSSEATHVVMEETSAEEAVSWQERRMAAAPPGCTPPALLDISWLTESLGAGQPVPVECRHRLEVAGPRKGPLSPAWMPAYACQRPTPLTHHNTGLSEALEILAEAAGFEGSEGRLLTFCRAASVLKALPSPVTTLSQLQGLPHFGEHSSRVVQELLEHGVCEEVERVRRSERYQTMKLFTQIFGVGVKTADRWYREGLRTLDDLREQPQKLTQQQKAGLQHHQDLSTPVLRSDVDALQQVVEEAVGQALPGATVTLTGGFRRGKLQGHDVDFLITHPKEGQEAGLLPRVMCRLQDQGLILYHQHQHSCCESPTRLAQQSHMDAFERSFCIFRLPQPPGAAVGGSTRPCPSWKAVRVDLVVAPVSQFPFALLGWTGSKLFQRELRRFSRKEKGLWLNSHGLFDPEQKTFFQAASEEDIFRHLGLEYLPPEQRNA
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.

Mol. Weight

58.8 kDa

Protein Length

Full Length

Tag Info

N-terminal 6xHis-tagged

Form

Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

3-7 business days

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet & COA

Please contact us to get it.

Description

The recombinant Human POLM protein is made through genetic engineering, also called gene splicing or recombinant DNA technology. By putting Human POLM genes into the genetic material of the E.coli system. These microorganisms can be used as factories or producers to make proteins for medical, academic and research uses. DNA to be manipulated it must be placed within a “transport vehicle” in which proteins may be produced from the genetic code of the DNA. The host cells used for Human POLM protein synthesis are E.coli cells, the whole production processes include isolation of POLM gene, amplification of POLM gene, cloning, POLM gene selection, and expression, and the POLM protein purification, the vector contains N-terminal 6xHis tag in addition to the specific DNA sequence, this facilitates the purification of the recombinant protein and it’s finally detected with a purity of 85%+ by SDS-PAGE.

POLM, also called Pol μ, is the only DNA polymerase with template-directed and terminal transferase activities. Pol μ is involved in the gap-filling repair synthesis during the non-homologous end joining (NHEJ) pathway for repair of the DNA double-strand breaks (DSBs). It contributes to the general error-prone bypass of certain kinds of DNA damages like 8-oxo-2′-deoxyguanosine (8-oxodG). Pol μ lacks proofreading activity, with an intrinsically high error rate of 10−3–10−5 for dNTP incorporation. Besides, Pol μ shows a strong preference for manganese over magnesium ions for its terminal deoxynucleotidyltransferase (TdT)-like activity.

Target Background

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.

Gene References into Functions

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

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Subcellular Location

Nucleus.

Protein Families

DNA polymerase type-X family

Tissue Specificity

Expressed in a number of tissues. Abundant in thymus.

Database Links

HGNC: 9185

OMIM: 606344

KEGG: hsa:27434

STRING: 9606.ENSP00000242248

UniGene: Hs.596982

Code	CSB-EP889065HU
Abbreviation	Recombinant Human POLM protein
MSDS	MSDS Datasheet
Size	US$306
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Image	(Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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Recombinant Human DNA-directed DNA/RNA polymerase mu (POLM)

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