Analytical Data
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Gene name
OBFC2A
- Application
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Alternative Names
OBFC2A；OBFC2A；SSB2；SOSS complex subunit B2
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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
Q96AH0
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Expression Region
1-204aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMNRVNDP LIFIRDIKPG LKNLNVVFIV LEIGRVTKTK DGHEVRSCKV ADKTGSITIS VWDEIGGLIQ PGDIIRLTRG YASMWKGCLT LYTGRGGELQ KIGEFCMVYS EVPNFSEPNP DYRGQQNKGA QSEQKNNSMN SNMGTGTFGP VGNGVHTGPE SREHQFSHAG RSNGRGLINP QLQGTASNQT VMTTISNGRD PRRAFKR
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Molecular Weight
25 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
Related Products
Protein Description
OBFC2A, a member of the OB-fold protein family, plays a crucial role in maintaining genome stability and regulating DNA replication. Its involvement in the formation of the telomeric complex highlights its significance in protecting chromosome ends from degradation and preventing fusion events. Recent studies have linked OBFC2A to various biological processes, including telomere maintenance and the response to DNA damage, suggesting its potential impact on cancer biology and aging. Researchers are particularly interested in understanding the molecular mechanisms by which OBFC2A interacts with other proteins involved in the replication fork and telomere preservation. The recombinant expression of OBFC2A in various systems has provided valuable insights into its structure-function relationship, enabling the analysis of its oligomerization, interaction with telomere-associated proteins, and enzymatic activities. Investigating OBFC2A's dynamics and functional implications not only deepens our understanding of fundamental cellular processes but also may pave the way for novel therapeutic strategies targeting telomere dysfunction in diseases characterized by genomic instability. Thus, the study of OBFC2A recombinant proteins remains a vital area of research in molecular biology and cancer therapy.
