Analytical Data
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Gene name
OBFC2B
- Application
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Alternative Names
NABP2; OBFC2B; SSB1; LP3587; SOSS complex subunit B1; Nucleic acid-binding protein 2; Oligonucleotide/oligosaccharide-binding fold-containing protein 2B; Sensor of single-strand DNA complex subunit B1; Sensor of ssDNA subunit B1; SOSS-B1; Single-stranded DNA-binding protein 1; hSSB1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BQ15
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Expression Region
1-211 aa
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AA Sequence
MTTETFVKDI KPGLKNLNLI FIVLETGRVT KTKDGHEVRT CKVADKTGSI NISVWDDVGN LIQPGDIIRL TKGYASVFKG CLTLYTGRGG DLQKIGEFCM VYSEVPNFSE PNPEYSTQQA PNKAVQNDSN PSASQPTTGP SAASPASENQ NGNGLSAPPG PGGGPHPPHT PSHPPSTRIT RSQPNHTPAG PPGPSSNPVS NGKETRRSSK R
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Molecular Weight
22.3 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
OBFC2B, or oligomerization domain containing protein B, is a crucial protein involved in various biological processes, particularly in nucleic acid metabolism and cellular stress responses. Research into OBFC2B has gained significance due to its potential role in maintaining genomic stability and DNA repair mechanisms. The protein is known to interact with other nucleic acid-binding proteins, suggesting a collaborative function in the maintenance of cellular homeostasis. Additionally, OBFC2B has been implicated in certain diseases, including cancers, where its dysfunction may lead to genomic instability and tumor progression. The study of OBFC2B recombinant proteins allows researchers to investigate its structure-function relationships and elucidate its specific roles in biological pathways. By understanding the molecular mechanisms underlying OBFC2B's activity, scientists aim to identify potential therapeutic targets and develop strategies to counteract its associated pathologies. As a result, OBFC2B serves as a model for studying protein interactions and their implications in health and disease, making it an important subject in molecular biology and biochemistry research.
