Analytical Data
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Gene name
C1qB
- Application
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Alternative Names
C1qB；Complement C1q subcomponent subunit B
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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
P02746
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Expression Region
1-253aa
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AA Sequence
MMMKIPWGSIPVLMLLLLLGLIDISQAQLSCTGPPAIPGIPGIPGTPGPD GQPGTPGIKGEKGLPGLAGDHGEFGEKGDPGIPGNPGKVGPKGPMGPKGG PGAPGAPGPKGESGDYKATQKIAFSATRTINVPLRRDQTIRFDHVITNMN NNYEPRSGKFTCKVPGLYYFTYHASSRGNLCVNLMRGRERAQKVVTFCDY AYNTFQVTTGGMVLKLEQGENVFLQATDKNSLLGMEGANSIFSGFLLFPD MEA
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Molecular Weight
26.7 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
C1qB is a crucial component of the complement system, specifically part of the C1 complex involved in the classical pathway of complement activation. The complement system plays a critical role in the immune response, facilitating opsonization, inflammation, and cell lysis. Research on C1qB has gained significant attention due to its dual role in both normal physiological processes and various pathological conditions, including autoimmune diseases and infections. Understanding the structure and function of C1qB is vital for deciphering its involvement in complement-mediated processes. Advances in recombinant protein technology have enabled the expression and purification of C1qB, facilitating studies on its interactions with other complement proteins and immune cells. Furthermore, investigating the therapeutic potential of C1qB-targeted treatments may lead to novel strategies for modulating immune responses in diseases where the complement system plays a key role. As such, the study of C1qB recombinant proteins not only enhances our understanding of immune system dynamics but also opens avenues for potential clinical applications.
