Analytical Data
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Gene name
FERD3L
- Application
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Alternative Names
Basic helix-loop-helix protein N-twist; bHLHa31; Class A basic helix-loop-helix protein 31; Fer3 like (Drosophila); Fer3-like protein; FER3L_HUMAN; Ferd3l; MGC119861; N TWIST; NATO3; Nephew of atonal 3; Neuronal twist; NTWIST
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96RJ6
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Expression Region
1-167aa
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AA Sequence
MAAYPESCVDTTVLDFVADLSLASPRRPLLCDFAPGVSLGDPALALREGRPRRMARFEEGDPEEEECEVDQGDGEEEEEEEERGRGVSLLGRPKRKRVITYAQRQAANIRERKRMFNLNEAFDQLRRKVPTFAYEKRLSRIETLRLAIVYISFMTELLESCEKKESG
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Molecular Weight
45.5 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
FERD3L, or FER 3-like protein 1, is implicated in various cellular processes, including cell signaling, cytoskeletal organization, and response to stress. Research into FERD3L has surged as scientists uncover its potential roles in human health and disease. Recent studies suggest that FERD3L may be involved in neurodegenerative disorders, given its expression in neuronal tissues and its role in modulating synaptic functions. Additionally, its dysregulation has been associated with cancer progression, prompting investigations into FERD3L as a potential biomarker or therapeutic target. The development of recombinant FERD3L proteins allows researchers to delve deeper into its functional mechanisms and interactions within cellular pathways. By studying these proteins, scientists aim to elucidate the specific contributions of FERD3L in disease contexts and its potential implications in therapeutic strategies. Understanding the structure-function relationship of FERD3L through recombinant protein studies may pave the way for novel interventions targeting its pathways, potentially improving outcomes for conditions linked to its dysregulation. As the exploration of FERD3L continues, it holds promise as a focal point in the quest for innovative solutions in treating complex diseases.
