BMP7 / Bone morphogenetic protein 7 · Western blot design guide

Design a Western Blot for BMP7

Real validated BMP7 Western blot protocols, expected-band and isoform facts, troubleshooting for weak or shifted signal, and recommended anti-BMP7 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
Western blot protocol sheet for BMP7: expected band ~49.3 kDa, hero antibody M00858, catalog values and labelled standard workflow; separate PMC comparisons on the guide
Printable BMP7 Western blot protocol sheet — expected band ~49.3 kDa, antibody M00858, controls and PMC citations. Open the full BMP7 WB guide →

BMP7 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 ~49.3 kDa
Gel 15% (standard starting point)
Negative control ⓘ Suggested KO / knockdown lysate
Important caveats
Reasons your observed band may differ from the expected size.
PTM Glycosylated + Cleaved
Caveat Reducing-condition controls
Gene-set association MSigDB C7 membership
Isoform 1 isoform(s)
Section 1

Real Curated BMP7 Western Blot Protocols

The M00858 protocol combines labelled catalog values with standard starting conditions. Published comparisons retain their own sample, reagent and detection scope.

Recommended Western blot protocol parameters
Sample / lysatehuman fetal kidney lysate (catalog M00858)
Gel %15% (standard starting point)
Load20–30 µg total protein per lane; optimize for abundance (standard starting point)
TransferShort semi-dry transfer; verify retention (standard starting point)
Membrane0.2 µm PVDF (standard starting point)
Blocking5% milk or 5% BSA in TBST (standard starting point)
Primary antibodyM00858; use the WB datasheet starting dilution (standard starting point)
Primary incubationOvernight at 4 °C (standard starting point)
Secondary antibodySpecies-matched HRP conjugate at validated dilution (standard starting point)
Secondary incubation1 h at room temperature (standard starting point)
Wash3 × 5 min in TBST (standard starting point)
DetectionECL; bracket exposures to avoid saturation (standard starting point)
Section 2

What Is the Expected BMP7 Western Blot Band Size?

BMP7 has a predicted 49.3 kDa full-length precursor; cleavage, N-linked glycosylation, and disulfide-linked dimerization may affect migration, but no empirical band is supplied.

What am I looking at on my blot?
Band near 49.3 kDaconsistent with the predicted full-length precursor; identity requires controls
Band below 49.3 kDamay reflect signal-peptide and propeptide cleavage
Band near twice the monomer size under non-reducing conditionsconsistent with a disulfide-linked BMP7 homodimer
Little or no band in whole-cell lysateBMP7 is secreted
Band above the predicted precursor sizeN-linked glycosylation is possible, but its effect on migration is unestablished
💡Expected BMP7 appearanceThe 49.3 kDa UniProt prediction describes the full-length BMP7 precursor; no empirical band size is supplied, and processing, glycosylation, or dimerization may alter migration, so confirm band identity with appropriate controls.
How each factor affects band size
49.3 kDa predicted precursor massprovides the reference size for full-length BMP7
Signal peptide at residues 1–29cleavage yields a smaller product than the full-length precursor
Propeptide at residues 30–292cleavage can yield a smaller mature product
N-linked glycosylation at Asn187, Asn302, Asn321, and Asn372may alter apparent size; the magnitude is not established
Disulfide-linked homodimermay appear near twice the monomer size without complete reduction
Why is my band missing or off?
SituationLikely causeNext action
No band in lysateBMP7 is secretedcheck conditioned medium alongside lysate
Band higher than expecteddisulfide-linked homodimer or possible N-linked glycosylationcompare reducing and non-reducing lanes and verify identity with antibody controls
Band lower than expectedsignal-peptide or propeptide cleavagecompare precursor and processed samples using an antibody with a known epitope
Broad smear instead of sharp bandheterogeneous N-linked glycosylation is possiblecompare matched samples before and after deglycosylation
Multiple bandsprecursor, processed BMP7, or incompletely reduced homodimer may coexistcompare reducing conditions and verify bands with an independent BMP7 antibody
Weak or no signalsecreted BMP7 may be scarce in the sampled fractiontest conditioned medium and a positive control

Sample controls for BMP7 Western blot

🧪For positive controls for BMP7 in Western blot, you can use no tissue or cell line supported by the supplied HPA 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 the samples.
⚠️Feasibility: BMP7 is secreted, so conditioned medium may give a stronger signal than whole-cell lysate.

HPA tissue expression evidence for BMP7

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

TissueCell typeLevelEvidenceSource
No high/medium HPA tissues identified in the supplied evidence.

Lower expression tissues · IHC evidence, not confirmed WB-negative controls

TissueCell typeLevelEvidenceSource
No lower-expression tissue rows available in the supplied evidence.
Section 3

Advanced BMP7 Western Blot Tips

Deeper troubleshooting and optimisation questions for BMP7, answered from its protein features.

How should BMP7 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.
Could annotated BMP7 isoforms explain multiple bands?
Isoforms · The supplied UniProt record lists one isoform and no alternative sequence. Prioritize the annotated signal peptide, propeptide, glycosylation sites, and disulfide-linked homodimer when evaluating multiple bands; their presence does not prove any particular band assignment.
Which BMP7 glycosylation sites matter when interpreting bands?
PTM · UniProt lists N-linked sites at residues 187, 302, 321, and 372, using full-length sequence numbering. Residue 187 lies in the propeptide; the other three follow it. These annotations identify possible contributors to band differences but do not establish site occupancy or a visible shift.
Does this guide establish induction of BMP7?
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 BMP7?
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 M00858 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 BMP7 bands be selected for quantitation?
Quantitation · Define the band form before comparing samples, then use the same fraction and reducing conditions throughout. BMP7 can be processed from its full-length sequence and is annotated as a disulfide-linked homodimer; combining bands without identifying their forms could obscure the comparison.
Why might BMP7 bands differ from its predicted 49.3 kDa mass?
Interpretation · The 49.3 kDa prediction refers to the full-length sequence. UniProt lists a signal peptide at residues 1–29 and a propeptide at 30–292, so processing can produce shorter forms. Glycosylation and disulfide-linked dimerization are also annotated, but these features alone do not establish an apparent band size.

BMP7 is annotated as a disulfide-linked homodimer with four disulfide bonds. Compare reducing and nonreducing samples when assigning a higher band to a dimer. The annotations do not specify the apparent masses of either form.

BMP7 is annotated as secreted. Include a secreted-protein fraction when designing the blot, and record which fraction each lane represents so bands can be compared consistently.

Check whether bands are consistent with processing of the signal peptide (1–29) and propeptide (30–292), N-linked sites at 187, 302, 321, and 372, or the disulfide-linked homodimer. All coordinates use full-length UniProt numbering. None of these annotations alone identifies an observed band.
Boster reagents

BMP7 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 Western blot analysis of BMP7 expression in human fetal kidney lysate.
Anti-BMP7 Rabbit Monoclonal Antibody
Cat # M00858

The listed anti-BMP7 rabbit monoclonal antibody has a Western blot image showing BMP7 expression in human fetal kidney lysate. Its listed reactivity is human, mouse, and rat; the supplied image documents only the human fetal kidney sample.

Which to pick: M00858 is the only listed BMP7 antibody and has a Western blot image from human fetal kidney lysate. For mouse or rat samples, reactivity is listed, but no corresponding Western blot image is supplied.

Source: BosterBio BMP7 gene-info card — filtered to Western-blot-capable antibodies; each card shows that product's actual WB validation figure.