Recombinant Human Chromodomain-Helicase-Dna-Binding Protein 1-Like (CHD1L) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-02474P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CHD1L.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CHD1L.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CHD1L.
Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Homo sapiens (Human) CHD1L.

Recombinant Human Chromodomain-Helicase-Dna-Binding Protein 1-Like (CHD1L) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-02474P
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Product Overview

Description Recombinant Human Chromodomain-Helicase-Dna-Binding Protein 1-Like (CHD1L) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q86WJ1
Target Symbol CHD1L
Synonyms ALC1; Amplified in liver cancer 1; Amplified in liver cancer protein 1; chd1l; CHD1L_HUMAN; CHDL; Chromodomain helicase DNA binding protein 1 like; Chromodomain-helicase-DNA-binding protein 1-like; FLJ22530
Species Homo sapiens (Human)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence SAELDYQDPDATSLKYVSGDVTHPQAGAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKGQDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAARGIPTYIYYFPRSKSAVLHAQSSSSSSRQLVP
Expression Range 704-897aa
Protein Length Partial
Mol. Weight 37.3kDa
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 DNA helicase which plays a role in chromatin-remodeling following DNA damage. Targeted to sites of DNA damage through interaction with poly(ADP-ribose) and functions to regulate chromatin during DNA repair. Able to catalyze nucleosome sliding in an ATP-dependent manner. Helicase activity is strongly stimulated upon poly(ADP-ribose)-binding.
Subcellular Location Nucleus.
Protein Families SNF2/RAD54 helicase family
Database References

HGNC: 1916

OMIM: 613039

KEGG: hsa:9557

STRING: 9606.ENSP00000358262

UniGene: PMID: 30024537

  • overexpression of CHD1L in embryonic cells upregulated the expression of ectoderm genes, especially PAX6 PMID: 28946814
  • implies a previously unappreciated role for ALC1 in DNA replication, in which ALC1 may regulate replication-fork slowing at CPT-induced DNA-damage sites PMID: 29408941
  • Upon DNA damage, binding of PARylated PARP1 by the macro domain induces a conformational change that relieves autoinhibitory interactions with the ATPase motor, which selectively activates ALC1 remodeling upon recruitment to sites of DNA damage. PMID: 29220652
  • NAD(+)-metabolite and nucleic acid poly-ADP-ribose triggers ALC1 to drive chromatin relaxation. Modular allostery in this oncogene tightly controls its robust, DNA-damage-dependent activation. PMID: 29220653
  • ALC1 is a unique base excision repair factor that functions in a chromatin context, most likely as a chromatin-remodeling enzyme. PMID: 29149203
  • CHD1L exerts its anti-apoptotic role through the apoptotic pathway involving caspase-9-caspase-3 apoptotic pathway in MM cells. In addition, we determined that CHD1L expression is increased when MM cells were adhered to fibronectin (FN) or bone marrow stromal cells PMID: 27258734
  • CHD1L is involved in the progression of glioma. PMID: 26162969
  • Overexpression of CHD1L is positively associated with tumor metastasis of lung adenocarcinoma, and might serve as a novel prognostic biomarker and potential therapeutic target for patients. PMID: 26360781
  • This study identified CHD1L as a potential anti-metastasis target for therapeutic intervention in breast cancer. PMID: 26599012
  • Relative mRNA expression level of CHD1L was higher in breast cancer cell lines. PMID: 25153161
  • These results indicated that CHD1L could serve as a prognostic marker for gastric cancer PMID: 24258459
  • CHD1L is now considered to be a novel independent biomarker for progression, prognosis and survival in several solid tumors. [Review] PMID: 24359616
  • Data indicate that chromodomain helicase/ATPase DNA-binding protein 1-like (CHD1L) might be an diagnostic and prognostic marker for bladder cancer (BC) patients. PMID: 23807680
  • TRIM33 plays a role in PARP-dependent DNA damage response and regulates ALC1 activity by promoting its timely removal from sites of DNA damage. PMID: 23926104
  • CHD1L is the target oncogene within the 1q21 amplicon and plays a pivotal role in colorectal carcinoma pathogenesis. PMID: 23746766
  • positive expression of CHD1L protein is significantly correlated with the metastasis proceeding of ovarian carcinoma, and CHD1L protein expression, as examined by IHC, may act as a novel prognostic biomarker for patients with ovarian carcinoma. PMID: 23020525
  • the model that PAR present on PARylated PARP1 acts as an allosteric effector of ALC1 nucleosome remodeling activity. PMID: 23132853
  • data support a model in which poly(ADP-ribosyl)ation of DDB2 suppresses DDB2 ubiquitylation and outline a molecular mechanism for PARP1-mediated regulation of nucleotide excision repair through DDB2 stabilization and recruitment of the chromatin remodeler ALC1 PMID: 23045548
  • Mutation in CHD1L is associated with congenital anomalies of the kidneys and urinary tract. PMID: 22146311
  • CHD1L/TCTP/Cdc25C/Cdk1 molecular pathway causes the malignant transformation of hepatocytes with the phenotypes of accelerated mitotic progression and the production of aneuploidy PMID: 21953552
  • 1q21.1 copy number variant (CNV) results in newly identified function such as decatenation (chromatid untangling) checkpoint (DCC) activation in the case of CHD1l/ALC1 in lymphoblast cell lines. PMID: 21824431
  • Overexpression of CHD1L was significantly associated with tumour microsatellite formation, advanced tumour stage, overall survival time of patients who received transarterial chemoembolisation treatment and chemoresistance in hepatocellular carcinoma. PMID: 21068133
  • CHD1L promotes hepatocellular carcinoma progression and metastasis in mice and is associated with these processes in human patients. PMID: 20335658
  • ALC1 is the target oncogene within the chromosome 1q21 amplicon and plays a pivotal role in hepeatocellular carcinoma pathogenesis. PMID: 18023026
  • results define ALC1 as a DNA damage-response protein whose role in this process is sustained by its association with known DNA repair factors and its rapid poly(ADP-ribose)-dependent recruitment to DNA damage sites PMID: 19661379
  • Poly(ADP-ribosyl)ation directs recruitment and activation of the ATP-dependent chromatin remodeler ALC1 PMID: 19666485
  • Alc1 is a chromatin remodeling enzyme activated by binding of its macrodomain to poly(ADP-ribosyl)ated Parp1. Alc1 is recruited to nucleosomes in vitro and to chromatin in cells when Parp1 catalyzes poly(ADP-ribose) synthesis at sites of DNA damage. PMID: 19666485
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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.

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