Analytical Data
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Gene name
BIN1
- Application
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Alternative Names
BIN1；AMPHL；Myc box-dependent-interacting Protein 1
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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
O00499-7
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Expression Region
1-439aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMAEMGSKGVTAGKIASNVQKKLTRAQEKVL QKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASK KLNECLQEVYEPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYL GQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKAEEELIK AQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQ NLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPDGSPAATPEIR VNHEPEPAGGATPGATLPKSPSQPAEASEVAGGTQPAAGAQEPGETAASE AASSSLPAVVVETFPATVNGTVEGGSGAGRLDLPPGFMFKVQAQHDYTAT DTDELQLRAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVF PENFTERVP
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Molecular Weight
50 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
BIN1 (Bridging Integrator 1), also known as Amphiphysin 2, is a protein that plays crucial roles in various cellular processes, including endocytosis, membrane dynamics, and cytoskeletal organization. Its involvement in these processes has sparked significant interest in the scientific community, particularly due to its association with neurodegenerative diseases and cancer. Research has shown that BIN1 interacts with several key proteins and signaling pathways, underscoring its importance in maintaining cellular homeostasis. Interestingly, mutations and alterations in BIN1 expression have been linked to conditions such as Alzheimer's disease, where it is believed to influence tau pathology and amyloid-beta metabolism. Moreover, studies indicate that BIN1 may also act as a tumor suppressor, highlighting its potential role in regulating cell proliferation and apoptosis in cancer. Given its multifunctional nature and the complexity of its interactions, the study of recombinant BIN1 proteins has become pivotal for elucidating its biological functions, therapeutic potential, and mechanisms underlying its involvement in disease. Understanding BIN1's structure-function relationship through recombinant protein studies not only provides insights into its physiological roles but also opens avenues for developing targeted interventions in related pathologies. The continuous exploration of BIN1 and its recombinant forms promises to shed light on its contributions to cellular integrity and the broader implications for human health.
