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- Table of Contents
C1QC / Complement C1q subcomponent subunit C · Western blot design guide
Design a Western Blot for C1QC
Real validated C1QC Western blot protocols, expected-band and isoform facts, troubleshooting for weak or shifted signal, and recommended anti-C1QC WB antibodies. Everything you need to plan the experiment before you commit precious samples.
Evidence assembled September 2026 · For research use; verify linked source records and product datasheet before use
C1QC Western Blot Experimental Design Guide
Expected bands, validated protocols, controls and antibodies — the at-a-glance facts below, then the full design guide.
Must know before running
| Expected band | ~25.8 kDa | |
| Gel | 12–15% (standard starting point) | |
| Positive control | Skin (IHC candidate; verify WB) +4 more | |
| Negative control | Adipose tissue (IHC candidate; verify WB) |
Important caveats
Reasons your observed band may differ from the expected size.
| PTM | Glycosylated + Cleaved | |
| Caveat | Peptide-blocking control | |
| Gene-set association | MSigDB Hallmark membership | |
| Isoform | 1 isoform(s) |
Section 1
Real Curated C1QC Western Blot Protocols
The A05666-1 protocol combines labelled catalog values with standard starting conditions. Published comparisons retain their own sample, reagent and detection scope.
| Sample / lysate | lysates from rat lung, (catalog A05666-1) |
| Gel % | 12–15% (standard starting point) |
| Load | 20–30 µg total protein per lane; optimize for abundance (standard starting point) |
| Transfer | Short semi-dry transfer; verify retention (standard starting point) |
| Membrane | 0.45 µm PVDF (standard starting point) |
| Blocking | the synthesized peptide (catalog A05666-1) |
| Primary antibody | A05666-1; use the WB datasheet starting dilution (standard starting point) |
| Primary incubation | Overnight at 4 °C (standard starting point) |
| Secondary antibody | Species-matched HRP conjugate at validated dilution (standard starting point) |
| Secondary incubation | 1 h at room temperature (standard starting point) |
| Wash | 3 × 5 min in TBST (standard starting point) |
| Detection | ECL; bracket exposures to avoid saturation (standard starting point) |
Section 2
What Is the Expected C1QC Western Blot Band Size?
C1QC has a predicted 25.8 kDa full-length precursor; cleavage and disulfide linkage could affect migration, but no empirical band size is supplied.
| Band near 25.8 kDa | Consistent with the predicted full-length C1QC precursor; identity needs confirmation |
| Band below 25.8 kDa | May reflect removal of the 1–28 signal peptide; mature migration is not established |
| Band near twice the reduced monomer size under non-reducing conditions | Consistent with subunits linked by the inter-chain disulfide at Cys32 |
| Little or no band in whole-cell lysate | C1QC is secreted and also occurs at the cell surface |
💡Expected C1QC appearanceUniProt predicts a 25.8 kDa full-length precursor, but supplies no empirical band size; signal-peptide cleavage and disulfide linkage may change the pattern, so confirm band identity with ordinary controls.
| Predicted full-length mass | 25.8 kDa is the sequence-based precursor size, not a measured band |
| Signal peptide at residues 1–28 | Cleavage makes the mature subunit smaller than the precursor; its band size is unknown |
| O-linked glycosylation of hydroxylysine 75 | May affect apparent migration, but a visible shift is not established |
| Inter-chain disulfide at Cys32 | Linked subunits may migrate near twice the reduced monomer size without complete reduction |
| Situation | Likely cause | Next action |
|---|---|---|
| No band in lysate | C1QC is secreted or cell-surface associated | Check conditioned medium or an appropriate cell-surface fraction alongside lysate |
| Band higher than expected | Inter-chain disulfide linkage may persist with incomplete reduction | Compare reducing and non-reducing lanes |
| Band lower than expected | The 1–28 signal peptide may have been cleaved | Compare with a suitable full-length reference and verify antibody specificity |
| Multiple bands | Reduced and disulfide-linked subunits may coexist | Repeat with complete reduction and use a specificity control |
| Weak or no signal | Secreted C1QC may be scarce in the sampled lysate | Test conditioned medium and include a positive sample and peptide-blocking control |
Experiment evidence
Western blot images showing C1QC band
A05666-1 · C1QC
← swipe / scroll for more images →
Real WB data behind the band-size expectations in this section.
Sample controls for C1QC Western blot
🧪HPA-IHC candidate guidance (verify in WB): For positive controls for C1QC in Western blot, you can use skin tissue, which has high HPA expression.
Positive control: Skin (IHC candidate; verify WB)
Negative control: Adipose tissue (IHC candidate; verify WB)
Loading controls: Run GAPDH, β-actin, and a total-protein stain alongside the samples.
⚠️Feasibility: Because C1QC is secreted, whole-cell lysate may give a weak signal; consider conditioned medium.
HPA tissue expression evidence for C1QC
Comprehensive Human Protein Atlas IHC scoring per tissue. Rows are taken directly from the HPA tissue chart — click any row's HPA link to view the source.
Higher expression tissues · candidate positive controls from IHC
| Tissue | Cell type | Level | Evidence | Source |
|---|---|---|---|---|
| Skin | extracellular matrix | High | Protein (IHC) | HPA → |
| Colon | glandular cells | Medium | Protein (IHC) | HPA → |
| Endometrium | cells in endometrial stroma | Medium | Protein (IHC) | HPA → |
| Fallopian tube | glandular cells | Medium | Protein (IHC) | HPA → |
| Gallbladder | glandular cells | Medium | Protein (IHC) | HPA → |
Lower expression tissues · IHC evidence, not confirmed WB-negative controls
| Tissue | Cell type | Level | Evidence | Source |
|---|---|---|---|---|
| Adipose tissue | adipocytes | Not detected | Protein (IHC) | HPA → |
| Breast | adipocytes | Not detected | Protein (IHC) | HPA → |
| Caudate | glial cells | Not detected | Protein (IHC) | HPA → |
| Cervix | glandular cells | Not detected | Protein (IHC) | HPA → |
| Epididymis | glandular cells | Not detected | Protein (IHC) | HPA → |
Section 3
Advanced C1QC Western Blot Tips
Deeper troubleshooting and optimisation questions for C1QC, answered from its protein features.
How should C1QC band migration be interpreted?
Band shift · Use the separately labelled calculated mass and catalog-observed evidence above. A sequence annotation does not establish an observed migration shift. Verify target identity with orthogonal controls.
Do listed C1QC isoforms explain multiple bands?
Isoforms · Only one isoform is supplied, with no alternative sequence. The supplied features therefore do not support assigning multiple bands to alternative C1QC isoforms. Evaluate sample fraction, processing and modifications before making a band assignment.
Is C1QC glycosylated at a specified site?
PTM · UniProt lists O-linked glycosylation on hydroxylysine 75, described as Gal-containing. Position 75 uses UniProt sequence numbering, including the 1–28 signal peptide. Consider this site when evaluating band heterogeneity, but do not assign an unexpected band to glycosylation without supporting evidence.
Does this guide establish induction of C1QC?
Induction · No general induction response is established by this guide. A pathway or gene-set association is not evidence of induction in a particular specimen. Verify the relevant treatment and control in a target-specific experiment.
How should transfer be checked for C1QC?
Transfer · Standard workflow guidance: verify transfer efficiency for the intended target size before interpreting a weak signal. Use total-protein assessment and optimize transfer for the membrane, gel and apparatus; the labelled catalog values take precedence.
How should blocking be optimized?
Blocking · Standard workflow guidance: follow the A05666-1 datasheet where specified. Otherwise compare 5% milk or 5% BSA in TBST; for a phospho-specific assay start with BSA. Optimize background and specific signal with matched controls.
How should C1QC Western blot signals be compared quantitatively?
Quantitation · Keep sample fraction and preparation conditions consistent across lanes. C1QC is secreted, can occur at the cell surface, and is part of the C1 complex, so a change in one fraction need not represent a change in total C1QC. Quantify the same assigned band under the same conditions.
Why might C1QC migrate differently from 25.8 kDa?
Interpretation · The 25.8 kDa prediction includes the 1–28 signal peptide. Secreted C1QC may lack that segment and has listed hydroxylation and glycosylation. Use 25.8 kDa as a sequence-based reference, not an expected band position; these features alone do not establish a visible shift or explain any observed difference.
UniProt lists 4-hydroxyproline at positions 36, 39, 42, 45, 54, 63, 81, 93, 96, 99 and 105, plus 5-hydroxylysine at 75. These are UniProt sequence coordinates, which may differ from mature-protein or antibody numbering. Their presence alone does not predict a resolvable band shift.
C1QC has two listed disulfide bonds and participates in the C1 complex. Compare reducing and nonreducing preparations if higher bands appear, and record the preparation conditions. The supplied features do not specify the disulfide positions or establish the identity of any higher band.
C1QC is listed as secreted and present at the cell surface. Check the sample fraction when interpreting a weak or absent cellular band; a cell lysate alone may not represent all C1QC present in the system. Compare like fractions across samples.
UniProt lists 4-hydroxyproline at positions 36, 39, 42, 45, 54, 63, 81, 93, 96, 99 and 105, plus 5-hydroxylysine at 75. These are UniProt sequence coordinates, which may differ from mature-protein or antibody numbering. Their presence alone does not predict a resolvable band shift.
C1QC has two listed disulfide bonds and participates in the C1 complex. Compare reducing and nonreducing preparations if higher bands appear, and record the preparation conditions. The supplied features do not specify the disulfide positions or establish the identity of any higher band.
C1QC is listed as secreted and present at the cell surface. Check the sample fraction when interpreting a weak or absent cellular band; a cell lysate alone may not represent all C1QC present in the system. Compare like fractions across samples.
Boster reagents
C1QC Western Blot Antibodies
Catalog antibodies with Western blot application and product-specific WB images. Evaluate suitability with the reported sample, controls and experimental conditions.
Real WB data
Anti-C1QC/Complement Component C1Qc Antibody
Cat # A05666-1
The catalog reports A05666-1, an anti-C1QC antibody with stated human, mouse, and rat reactivity. Its Western blot image uses rat lung lysate and includes a peptide-blocked lane. The supplied evidence does not show Western blot results for human or mouse samples.
Which to pick: A05666-1 is the only listed option. Its documented Western blot example uses rat lung lysate; human and mouse are listed as reactive, but no Western blot images for those samples are supplied.
Source: BosterBio C1QC gene-info card — filtered to Western-blot-capable antibodies; each card shows that product's actual WB validation figure.
References
- UniProt Consortium. UniProt entry P02747.
- Human Protein Atlas. C1QC tissue expression.
- PMC12678476 — target-verified WB comparison
- PMC12370833 — target-verified WB comparison
- PMC10130088 — target-verified WB comparison