Analytical Data
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Gene name
BFSP2
- Application
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Alternative Names
BFSP2Phakinin; 49 kDa cytoskeletal Protein; Beaded filament structural Protein 2
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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
Q13515
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Expression Region
1-415aa
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AA Sequence
MSERRVVVDL PTSASSSMPL QRRRASFRGP RSSSSLESPP ASRTNAMSGL VRAPGVYVGT APSGCIGGLG ARVTRRALGI SSVFLQGLRS SGLATVPAPG LERDHGAVED LGGCLVEYMA KVHALEQVSQ ELETQLRMHL ESKATRSGNW GALRASWASS CQQVGEAVLE NARLMLQTET IQAGADDFKE RYENEQPFRK AAEEEINSLY KVIDEANLTK MDLESQIESL KEELGSLSRN YEEDVKLLHK QLAGCELEQM DAPIGTGLDD ILETIRIQWE RDVEKNRVEA GALLQAKQQA EVAHMSQTQE EKLAAALRVE LHNTSCQVQS LQAETESLRA LKRGLENTLH DAKHWHDMEL QNLGAVVGRL EAELREIRAE AEQQQQERAH LLARKCQLQK DVASYHALLD REESG
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Molecular Weight
45.8 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
BFSP2 (Bifunctional Spectrin Protein 2) is a crucial cytoskeletal protein predominantly expressed in the lens of the eye, playing a significant role in maintaining lens transparency and structural integrity. The research background surrounding BFSP2 is rooted in its essential function in forming the architectural scaffold that supports lens fibers and facilitates their proper alignment. Mutations in the BFSP2 gene have been implicated in various hereditary cataracts, leading to compromised vision and emphasizing its importance in ocular health. Studies have aimed to elucidate the protein's biochemical properties, structural characteristics, and the mechanisms by which it interacts with other cellular components. Understanding BFSP2's role at the molecular level may provide insights into cataractogenesis and potential therapeutic avenues for lens opacities. Moreover, the study of BFSP2 has broader implications in the field of cell biology, as it highlights the dynamic interplay between cytoskeletal proteins and cellular function. Researchers are increasingly interested in the potential for recombinant BFSP2 proteins in biomedical applications, including the development of biomaterials for ocular drug delivery systems. Through advanced techniques such as X-ray crystallography and cryo-electron microscopy, ongoing investigations aim to map the protein's structural dynamics under various physiological conditions, which could further elucidate its functional roles in the lens microenvironment. Overall, BFSP2 represents a significant focus of research due to its vital contributions to lens physiology and the potential impact of its dysregulation on eye health.
