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- Table of Contents
SERPINC1 / Antithrombin-III · Western blot design guide
Design a Western Blot for SERPINC1
Source-linked SERPINC1 Western blot protocol options, expected-band and isoform facts, troubleshooting for weak or shifted signal, and recommended anti-SERPINC1 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
SERPINC1 Western Blot Experimental Design Guide
Expected bands, source-linked protocol options, controls and antibodies — the at-a-glance facts below, then the full design guide.
Must know before running
| Expected band | ~52.6 kDa | |
| Gel | 12–15% (standard starting point) | |
| Negative control | Suggested KO / knockdown lysate |
Important caveats
Reasons your observed band may differ from the expected size.
| PTM | Glycosylated + Phosphorylated | |
| Caveat | Modification-state controls | |
| Gene-set association | MSigDB Hallmark membership | |
| Isoform | 1 isoform(s) |
Section 1
Source-Linked SERPINC1 Western Blot Protocol Options
The A00469 protocol combines labelled catalog values with standard starting conditions. Published comparisons retain their own sample, reagent and detection scope.
| Sample / lysate | Target-positive lysate and matched negative control (standard starting point) |
| Gel % | 12–15% (standard starting point) |
| Load | 20–30 µg total protein per lane; optimize for abundance (standard starting point) |
| Transfer | Standard semi-dry transfer; verify efficiency (standard starting point) |
| Membrane | 0.45 µm PVDF (standard starting point) |
| Blocking | 5% milk or 5% BSA in TBST (standard starting point) |
| Primary antibody | A00469; 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 SERPINC1 Western Blot Band Size?
The predicted precursor is 52.6 kDa; signal-peptide cleavage and N-linked glycosylation could alter migration, but no empirical band position is supplied.
| Band near 52.6 kDa | Consistent with the predicted precursor mass; confirm identity with controls. |
| Band below 52.6 kDa | Could reflect removal of the 1–32 signal peptide. |
| Band above 52.6 kDa | Could reflect N-linked glycosylation; migration is not established. |
| Broad band or smear | Could reflect variable N-linked glycosylation; verify experimentally. |
| Little or no band in whole-cell lysate | Antithrombin-III is secreted into extracellular space. |
💡Expected SERPINC1 appearanceThe UniProt predicted precursor mass is 52.6 kDa; signal-peptide cleavage and N-linked glycosylation may affect migration, but no empirical band size is supplied, so confirm identity with appropriate controls.
| UniProt predicted precursor mass | Provides a 52.6 kDa reference, not a measured band position. |
| Signal peptide at residues 1–32 | Cleavage yields a smaller mature polypeptide than the precursor. |
| N-linked glycosylation at Asn128 | May increase apparent mass if occupied. |
| N-linked glycosylation at Asn167 | May increase apparent mass if occupied. |
| Complex N-linked glycosylation at Asn187 | May increase apparent mass if occupied. |
| N-linked glycosylation at Asn224 | May increase apparent mass if occupied. |
| Situation | Likely cause | Next action |
|---|---|---|
| No band in lysate | Antithrombin-III is secreted. | Check plasma or conditioned medium alongside a sample control. |
| Band higher than expected | N-linked glycosylation may alter migration. | Compare untreated and deglycosylated samples with an identity control. |
| Band lower than expected | The signal peptide may have been cleaved. | Compare precursor and mature-sequence expectations and verify band identity. |
| Broad smear instead of sharp band | Variable N-linked glycosylation is possible. | Compare treated and untreated samples after deglycosylation. |
| Multiple bands | Different glycosylation states are possible, but band identities are unproven. | Use deglycosylation and an independent antibody to identify the bands. |
Experiment evidence
Western blot images showing SERPINC1 band
A00469 · SERPINC1
A00469 · SERPINC1
A00469-1 · SERPINC1
PA2218 · SERPINC1
M00469 · SERPINC1
← swipe / scroll for more images →
Real WB data behind the band-size expectations in this section.
Sample controls for SERPINC1 Western blot
🧪For positive controls for SERPINC1 in Western blot, you can use no HPA-supported positive sample from the supplied evidence.
Positive control: No high/medium HPA tissue identified
Negative control: Suggested KO / knockdown lysate
Loading controls: Run GAPDH, β-actin, and a total-protein stain alongside.
⚠️Feasibility: SERPINC1 is secreted, so whole-cell lysates may give little signal; consider conditioned medium.
HPA tissue expression evidence for SERPINC1
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 |
|---|---|---|---|---|
| No high/medium HPA tissues identified in the supplied evidence. | ||||
Lower expression tissues · IHC evidence, not confirmed WB-negative controls
| Tissue | Cell type | Level | Evidence | Source |
|---|---|---|---|---|
| No lower-expression tissue rows available in the supplied evidence. | ||||
Section 3
Advanced SERPINC1 Western Blot Tips
Deeper troubleshooting and optimisation questions for SERPINC1, answered from its protein features.
How should SERPINC1 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.
Are multiple SERPINC1 bands explained by listed isoforms?
Isoforms · Only one isoform is supplied, with no alternative sequence. Do not assign multiple bands to specific SERPINC1 isoforms on this evidence alone; verify band identity before interpreting them.
Which glycosylation sites matter when interpreting a SERPINC1 band?
PTM · UniProt lists N-linked sites at Asn128, Asn167, Asn187, and Asn224; Asn187 is annotated as complex. These are coordinates in the supplied full-length sequence, including the signal peptide. Keep that numbering when comparing antibody or assay descriptions. The listed sites alone do not prove a visible shift.
UniProt lists Thr63 phosphorylation and Ser68 phosphorylation by FAM20C. These positions use the supplied full-length sequence numbering. Record which antibody detects total SERPINC1 and which, if any, detects phosphorylation; the modification annotations alone do not establish a visible band shift.
UniProt lists Thr63 phosphorylation and Ser68 phosphorylation by FAM20C. These positions use the supplied full-length sequence numbering. Record which antibody detects total SERPINC1 and which, if any, detects phosphorylation; the modification annotations alone do not establish a visible band shift.
Does this guide establish induction of SERPINC1?
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 SERPINC1?
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 A00469 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 SERPINC1 signals be quantified across samples?
Quantitation · Use the same sample fraction and band selection criteria across comparisons. Document whether the antibody recognizes total SERPINC1 or a specific modification, since UniProt lists four N-linked glycosylation sites and two FAM20C phosphorylation sites. The features do not establish how much of each modified form is present.
Why might SERPINC1 migrate differently from its predicted 52.6 kDa mass?
Interpretation · The 52.6 kDa prediction includes the 1–32 signal peptide. SERPINC1 also has four N-linked glycosylation sites. Signal peptide processing and glycosylation are relevant when interpreting migration, but these features alone do not establish an apparent band size or explain a measured difference.
SERPINC1 is annotated as secreted into the extracellular space and has a signal peptide at residues 1–32. Include an extracellular sample fraction when planning detection, and compare like fractions across samples.
Check band identity before assigning a cause. Relevant annotations include signal peptide residues 1–32, four N-linked sites, three disulfide bonds, and a protease inhibiting heterodimer with TMPRSS7. None of these annotations alone identifies an unexpected Western blot band.
SERPINC1 is annotated as secreted into the extracellular space and has a signal peptide at residues 1–32. Include an extracellular sample fraction when planning detection, and compare like fractions across samples.
Check band identity before assigning a cause. Relevant annotations include signal peptide residues 1–32, four N-linked sites, three disulfide bonds, and a protease inhibiting heterodimer with TMPRSS7. None of these annotations alone identifies an unexpected Western blot band.
Boster reagents
SERPINC1 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-SERPINC1 Antibody (C-term)
Cat # A00469
Real WB data
Anti-Antithrombin III/SERPINC1 Antibody Picoband®
Cat # A00469-1
Real WB data
Anti-Antithrombin III/SERPINC1 Antibody Picoband®
Cat # PA2218
Real WB data
Anti-SERPINC1 Monoclonal Antibody
Cat # M00469
The four listed anti-SERPINC1 antibodies each have a Western blot image. Their captions document specific tissue, cell lysate, or plasma samples. These examples support those tested contexts, but do not establish performance across every listed species or sample type.
Which to pick: For mouse liver, see A00469 or A00469-1; A00469-1 also shows rat liver and mouse testis and ovary. PA2218 shows rat testis and cell lysates; M00469 shows human plasma. Choose by your sample and the antibody’s listed reactivity.
Source: BosterBio SERPINC1 gene-info card — filtered to Western-blot-capable antibodies; each card shows that product's actual WB validation figure.
References
- UniProt Consortium. UniProt entry P01008.
- Human Protein Atlas. SERPINC1 tissue expression.
- PMC12403336 — target-verified WB comparison
- PMC5783486 — target-verified WB comparison
- PMC8645897 — target-verified WB comparison