Recombinant Human Dna Cross-Link Repair 1A Protein (DCLRE1A) Protein (His)

Name: Recombinant Human Dna Cross-Link Repair 1A Protein (DCLRE1A) Protein (His)
Brand: Beta LifeScience
SKU: BLC-06953P
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 Cross-Link Repair 1A Protein (DCLRE1A) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q6PJP8
Target Symbol	DCLRE1A
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Expression Range	690-1040aa
Protein Length	Partial
Mol. Weight	4.1 kDa
Research Area	Epigenetics And Nuclear Signaling
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	May be required for DNA interstrand cross-link repair. Also required for checkpoint mediated cell cycle arrest in early prophase in response to mitotic spindle poisons. Possesses beta-lactamase activity, catalyzing the hydrolysis of penicillin G and nitrocefin. Exhibits no activity towards other beta-lactam antibiotic classes including cephalosporins (cefotaxime) and carbapenems (imipenem).
Subcellular Location	Nucleus. Note=In some cells it may be found in typically 1 or 2 discrete nuclear aggregates of unknown function which also contain TP53BP1. Also found in multiple discrete nuclear foci which increase in number following treatment with ionizing radiation or interstrand cross-linking agents. These foci overlap with those formed by the MRN complex (composed of MRE11, RAD50 and NBN) and BRCA1.
Protein Families	DNA repair metallo-beta-lactamase (DRMBL) family
Database References	HGNC: 17660 OMIM: 609682 KEGG: hsa:9937 STRING: 9606.ENSP00000355185 UniGene: Hs.1560
Tissue Specificity	Expressed in brain, heart, kidney, liver, pancreas, placenta and skeletal muscle.

Gene Functions References

Strikingly, the addition of the single-stranded DNA (ssDNA)-binding replication protein A (RPA) selectively restores XPF-ERCC1 endonuclease activity on this structure. The 5'-3' exonuclease SNM1A can load from the XPF-ERCC1-RPA-induced incisions and digest past the crosslink to quantitatively complete the unhooking reaction. PMID: 28607004
Different charge distributions along the DNA binding groove may account for the drastic difference in processivity and DNA digestion efficiency, including that of damaged substrates, between SNM1A and SNM1B. PMID: 26582912
differences in the substrate selectivities of SNM1A and SNM1B are likely to be relevant to their in vivo roles PMID: 22692201
collaboration between hSNM1A and XPF-ERCC1 is necessary to initiate interstrand cross-link repair in replicating human cells PMID: 21896658
RAD18-dependent recruitment of SNM1A to DNA repair complexes by a ubiquitin-binding zinc finger PMID: 20385554
Results suggest that 53BP1 and Snm1 may cooperate in the cellular response to genotoxic damage. PMID: 12446782
Snm1 and 53BP1 are components of a mitotic stress checkpoint that negatively targets the APC prior to chromosome condensation PMID: 15542852
The SNM1 enzyme utilizes either DNA or RNA substrates, requires a 5'-phosphate moiety, shows very little activity on double-strand substrates, and functions at a size consistent with a monomer. PMID: 17804464
Human SNM1A suppresses the DNA repair defects of yeast pso2 mutants. PMID: 18006388
hSNM1 appears to represent a second pathway for genome stability PMID: 18180189
These findings suggest that SNM1A acts with ATM to promote the G1 cell cycle checkpoint. PMID: 18848520

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.