Analytical Data
-
Gene name
OBFC2A
- Application
-
Alternative Names
Nucleic acid-binding protein 1Oligonucleotide/oligosaccharide-binding fold-containing protein 2ASensor of single-strand DNA complex subunit B2Sensor of ssDNA subunit B2 ;SOSS-B2Single-stranded DNA-binding protein 2 ;hSSB2
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96AH0
-
Expression Region
1-204aa
-
Molecular Weight
38.4 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
Related Products
Protein Description
OBFC2A is a vital protein involved in the maintenance of telomeres and the regulation of DNA replication. It belongs to a family of OB-fold proteins, which are known for their ability to bind single-stranded DNA (ssDNA). Recent research has illuminated the critical roles of OBFC2A in various cellular processes, including telomere length maintenance and genome stability. Dysregulation of OBFC2A has been implicated in several diseases, including cancer, where telomere dysfunction can lead to genomic instability. This protein has garnered significant interest because of its potential as a therapeutic target and biomarker in cancer treatment and aging-related disorders. The reconstitution of OBFC2A in vitro allows for thorough investigation of its biochemical properties, interactions with other telomeric proteins, and its role in ssDNA binding. Such studies can yield deeper insights into telomere biology and identify novel avenues for medical intervention in diseases linked to telomere dysfunction. Understanding OBFC2A's structure-function relationships is essential, as it may reveal mechanisms of action that can be harnessed for novel therapeutic strategies. Thus, OBFC2A serves as a crucial focal point in molecular biology research aimed at combating age-related diseases and cancer.
