Analytical Data
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Gene name
INHbB
- Application
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Alternative Names
INHbB;Inhibin beta B chain
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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
P09529
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Expression Region
1-407aa
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AA Sequence
MDGLPGRALGAACLLLLAAGWLGPEAWGSPTPPPTPAAQPPPPPPGSPGG SQDTCTSCGGFRRPEELGRVDGDFLEAVKRHILSRLQMRGRPNITHAVPK AAMVTALRKLHAGKVREDGRVEIPHLDGHASPGADGQERVSEIISFAETD GLASSRVRLYFFISNEGNQNLFVVQASLWLYLKLLPYVLEKGSRRKVRVK VYFQEQGHGDRWNMVEKRVDLKRSGWHTFPLTEAIQALFERGERRLNLDV QCDSCQELAVVPVFVDPGEESHRPFVVVQARLGDSRHRIRKRGLECDGRT NLCCRQQFFIDFRLIGWNDWIIAPTSYYGNYCEGSCPAYLAGVPGSASSF HTAVVNQYRMRGLNPGTVNSCCIPTKLSTMSMLYFDDEYNIVKRDVPNMI VEECGCA
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Molecular Weight
45.1 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
INHbB, or the inhibitor of nuclear factor kappa-B binding protein, plays a crucial role in various biological processes, including cellular signaling and immune responses. Recent studies have highlighted its significant involvement in cancer progression, inflammation, and autoimmune diseases, making it a compelling target for therapeutic intervention. The recombinant form of INHbB has been developed to better understand its functional properties and interactions at the molecular level. Researchers are focusing on its potential to modulate pathways associated with NF-kB (nuclear factor kappa-light-chain-enhancer of activated B cells), which is known for regulating genes involved in immune response, cell proliferation, and survival. By producing and characterizing recombinant INHbB proteins, scientists aim not only to elucidate the protein's structure-function relationships but also to explore its therapeutic applications, including the design of new drugs that can either inhibit or enhance its activity in disease contexts. Such advances could provide novel strategies for treating various conditions linked to dysregulation of NF-kB signaling, affirming the importance of INHbB in both fundamental research and clinical applications.











