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View ProductsSize | 100ug |
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Brand | Arovia |
Product type | Recombinant Proteins |
Product name | Recombinant Human NABP1 Protein, N-His-SUMO |
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Origin species | Human |
Expression system | Prokaryotic expression |
Molecular weight | 23.95 kDa |
Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
Form | Liquid |
Delivery condition | Dry Ice |
Delivery lead time in business days | 3-5 days if in stock; 3-5 weeks if production needed |
Storage condition | 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection) |
Brand | Arovia |
Host species | Escherichia coli (E.coli) |
Fragment Type | Asn22-Gly126 |
Aliases /Synonyms | Nucleic acid-binding protein 1, SOSS complex subunit B2, OBFC2A, Single-stranded DNA-binding protein 2, Sensor of ssDNA subunit B2, hSSB2, SSB2, SOSS-B2, NABP1, Oligonucleotide/oligosaccharide-binding fold-containing protein 2A, Sensor of single-strand DNA complex subunit B2 |
Reference | ARO-P11652 |
Note | For research use only. |
Recombinant Human NABP1 Protein, also known as Nucleic acid-binding protein 1 (NABP1), is a highly conserved protein that is found in all eukaryotic cells. It plays an important role in DNA replication and repair, as well as in maintaining genomic stability. NABP1 is a member of the Nucleic acid-binding protein (NABP) family, which also includes NABP2 and NABP3. These proteins are characterized by their ability to bind to single-stranded DNA and RNA, and are involved in various cellular processes such as DNA replication, transcription, and translation.
Recombinant Human NABP1 Protein is a 42 kDa protein that is composed of 373 amino acids. It contains a highly conserved N-terminal domain, which is responsible for its DNA-binding activity. This domain is composed of two zinc finger motifs, which are essential for the protein’s ability to bind to single-stranded DNA. The C-terminal domain of NABP1 is less conserved and is thought to be involved in protein-protein interactions.
The crystal structure of NABP1 has been determined, revealing the presence of two zinc finger motifs at the N-terminus and a flexible C-terminal domain. These zinc finger motifs are composed of cysteine and histidine residues, which coordinate two zinc ions to form a stable structure. This structure allows NABP1 to bind to single-stranded DNA in a sequence-specific manner.
The main activity of Recombinant Human NABP1 Protein is its ability to bind to single-stranded DNA and RNA. This activity is essential for its role in DNA repair and replication, as well as in maintaining genomic stability. NABP1 is involved in the recognition and binding of damaged DNA, which triggers the recruitment of other DNA repair proteins to the site of damage. It also plays a role in the repair of DNA breaks, which can occur during DNA replication or in response to external factors such as UV radiation or chemicals.
In addition to its role in DNA repair, NABP1 is also involved in DNA replication. It is responsible for recruiting DNA polymerases, the enzymes that synthesize new DNA strands, to the site of replication. NABP1 also interacts with other proteins involved in DNA replication, such as DNA helicases and topoisomerases, to coordinate the complex process of DNA synthesis.
Recombinant Human NABP1 Protein has a wide range of applications in both research and medicine. Its ability to bind to single-stranded DNA and RNA makes it a valuable tool for studying DNA repair and replication processes. It is also used in the development of diagnostic tests for DNA damage and mutations, as well as in the screening of potential anti-cancer drugs.
In the field of medicine, NABP1 has been linked to various human diseases, including cancer and neurodegenerative disorders. Studies have shown that mutations in the NABP1 gene can lead to an increased risk of certain types of cancer, such as breast and colorectal cancer. Recombinant Human NABP1 Protein is therefore being investigated as a potential target for cancer therapy.
In conclusion, Recombinant Human NABP1 Protein is a crucial protein involved in DNA repair and replication processes. Its structure and activity make it a valuable tool for studying these processes, and its potential applications in medicine make it a promising target for future research.
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