Bone Analysis

Preparation of Hard Tissue Specimens

1. Preparation of bone tissue specimens

To acquire various information from tissues and cells in bone, gross morphological examinations and histomorphometrical analysis are performed with bone tissue samples prepared. Tissues samples can be classified into two categories; decalcified specimen and non-decalcified specimen.

 

2. Bone Histomorphometry

Bone histomorphometry is one of the means to assess metabolic functions of bone. The follows are measured with non-decalcified thin sections.
1) Bone structure: cancellous tissue content, trabecular thickness, trabecular number, etc.
2) Bone formation: osteoid surface, osteoblast cell surface, bone calcification surface, rate of calcification, etc.
3) Bone resorption: the surface of bone resorption, osteoclast cell number, etc.

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Agilent Gene

 

Cat. No. Description Unit 1-20 cases 21-40 cases 41-50 cases
EO-CA1 *1 Agilent Oligo Microarray Service pair 4000$ 3700$ 3400$
EO-CA2 *2 Agilent Whole Genome Oligo Microarray Service pair 5700$ 5400$ 5100$
ET-1 RNA Extraction Service (from tissue) rx 280$ 240$ 200$
ET-2 RNA Extraction Service (from cell line) rx 280$ 240$ 200$
EL-1 LCM Service target 200$ 170$ 140$
EL-2 LCM to DNA Extr. Service target 170$ 240$ 200$
EL-3 LCM to RNA Extr. Service target 270$ 400$ 330$
EL-4 RNA Linear Amplification Service (2 rounds) target 600$ 540$ 480$
EQ-1 LCM Sample QC & RNA Isolation QC (when samples failed) target 120$ 110$ 100$
EQ-2 Total RNA QC (when samples failed) target 100$ 80$ 70$
*1: Agilent Oligo Array: Human, Mouse, Rat, Yeast, Arabidopsis, Rice
*2: Agilent Whole Genome Oligo Array: Human, Mouse
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Custom Peptide Synthesis

 

Custom Peptide Synthesis
 
The peptides are synthesised using Boc chemistry and purified by HPLC using reverse phase C4 and C18 columns.
 
You receive:
  • 20 mg of crude peptide (40-60% pure) or 5 mg of purified peptide (>95%).
  • MS and HPLC analyses data.
 
Orders are delivered in 3-4 weeks.

Length of the sequence

Crude peptide

(40-60% pure).

Suitable for immunization

HPLC purified (>95%)

10 amino acids

250 $

320 $

11 amino acids

261 $

316 $

12 amino acids

282 $

342 $

13 amino acids

303 $

368 $

14 amino acids

324 $

394 $

15 amino acids

345 $

420 $

16 amino acids

366 $

446 $

17 amino acids

387 $

472 $

18 amino acids

408 $

498 $

19 amino acids

429 $

524 $

20 amino acids

450 $

550 $

21 amino acids

429 $

492 $

22 amino acids

448 $

514 $

23 amino acids

467 $

536 $

24 amino acids

486 $

558 $

25 amino acids

505 $

580 $

26 amino acids

524 $

602 $

27 amino acids

543 $

624 $

28 amino acids

562 $

646 $

29 amino acids

581 $

668 $

30 amino acids

600 $

690 $

31 amino acids

805 $

898 $

32 amino acids

830 $

926 $

33 amino acids

855 $

954 $

34 amino acids

880 $

982 $

35 amino acids

905 $

1010 $

36 amino acids

930 $

1038 $

37 amino acids

955 $

1066 $

38 amino acids

980 $

1094 $

39 amino acids

1005 $

1122 $

40 amino acids

1030 $

1150 $
 
Please request a quote if sequence is shorter than 10 amino acids.
 
Please request a quote if sequence is longer than 40 amino acids.
 
We also provides phosphopeptides, please ask for a quote.

We guarantee: Full confidentiality of all orders.
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Antibody Production

Custom peptide polyclonal antisera have become an instrument of paramount importance in the life science tool-box. However, raising peptide polyclonal antibodies is a laborious process and for a successful outcome, numerous pitfalls have to be avoided.

Genprice offers a complete set of services, from peptide design to affinity purification. Whatever your requirements are, we are confident that we will be able to accommodate you.

Though every project is different, we have a standard custom peptide polyclonal antiserum package. This package can be extended according to your specifications and you will also be able to make modifications and additions during the course of a project.

The standard package includes:

Peptide Design
Peptide Synthesis, 25 mg
Peptide-Carrier Conjugation
12 week immunisation protocol for 1 rabbit according to:

Day 1 Collection of pre-immune serum
Day 1 Primary immunisation
Day 14 First booster
Day 28 Second booster
Day 42 First serum sample ~10 ml
Day 49 Third booster
Day 63 Second serum sample ~10 ml
Day 70 Fourth booster
Day 84 Production lot ~40 ml

ELISA analysis of the first serum sample.


Documentation of the project.
1200 $

Additional services are available such as
 

Continuation of project
180 $ per four-week cycle

Additional ELISA analyses
120 $ per analysis

Affinity Purification of antisera
735 $

Supplying of antiserum in aliquots
60 $ per serum sample

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Comparison

Comparison of posttranslational modifications of a protein

The primary structure of the protein must be known!
Samples containing a given protein either obtained after expression in different expression systems (e.g. prokaryotic vs. eukaryotic), or before and after induction, or before and after in vitro modification (e.g. phosphorylation) might be compared.

You provide us with a) or b):

a) Homogenous protein per sample, obtained by excision of bands from a dried SDS-gel (stained with Coomassie Blue or Silver, preferably without fixation). Please enclose a gel photo. Please, mention the %age of the gel, clearly mark the bands which were excised from the gel, and specify the molecular weight marker and the estimated molecular weight of the proteins of interest.

b) At least 25 µg of each purified native protein sample(ammonium sulfate precipitate or lyophilized protein). Please, enclose a photo of an analytical SDS-PAGE, mention the %age of the gel, clearly mark the bands which correspond to the purified proteins, and specify the molecular weight marker and the estimated molecular weight of the proteins of interest. Recommend a suitable buffer for dialyzing (ammonium sulfate precipitate) or dissolving (lyophilized material) the proteins. If this is not a standard buffer, add your buffer in sufficient amount (esp. for dialysis). Mention special requirements of your protein with respect to solubility and stability (especially important for membrane proteins).

Required Information:

Protein identity (incl. database entry number) and source of the protein samples (organism, tissue, cell fraction etc.), and assumption which protein modification is anticipated.

Please ship the protein without cooling (dried gel bands, lyophilized protein) or on blue ice (ammonium sulfate precipitate) to:

Gentaur
Avenue de l'Armée 68/B4
B-1040 Brussels BELGIUM
 
Our service:
  1. (In gel) trypsination of the protein (bands) of interest (Protein is cleaved at arg and lys sites into peptides)
  2. MALDI-TOF Mass Spectometry analysis of the tryptic peptides
  3. Peptides carrying posttranslational modifications are identified by comparing their actual mass with their theoretical mass peak by peak. This process is carried out by trained scientists. A list of experimental peptides that correspond to unmodified peptides is generated, then a list of experimental peptides that match to peptides which carry modifications of cystein residues, methionine residues, or other modification as documented in SWISS-PROT is created. In order to find novel modifications, the mass differences between all experimental peptides and all theoretical peptides are calculated. If a mass difference corresponds to the mass of any known modification the peptide is classified as potentially modified. Within the peptide the potential amino acid(s) that may carry the modification in question is/are suggested.
  4. A comparison list of modifications for the different protein samples is delivered.
 
Order Information:

Cat. Nr. CPPM01: Comparison of Posttranslational Modifications of a Protein by MALDI-TOF-MS, proteins shipped in protein gel bands
Price: 495 $ per sample (minimum: 2 samples)

Cat. Nr. CPPM02: Comparison of Posttranslational Modifications of a Purified Protein by MALDI-TOF-MS
Price: 720 $ per sample (minimum: 2 samples)

Please note: In case the protein amount or purity was not sufficient to perform MALDI-TOF MS, a set up fee of $ 175 is charged.
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posttranslational

 

Identification of posttranslational protein modifications
 

The primary structure of the protein must be known!

You provide us with: a) or b):

a) Homogenous protein in an excised band from a dried SDS-gel (stained with Coomassie Blue or Silver, preferably without fixation). Please enclose a gel photo. Please mention the %age of the gel, clearly mark the band which was excised from the gel, and specify the molecular weight marker and the estimated molecular weight of the protein of interest.

b) At least 25 µg purified native protein (ammonium sulfate precipitate or lyophilized protein). Please, enclose a photo of an analytical SDS-PAGE, mention the %age of the gel, clearly mark the band which corresponds to the purified protein, and specify the molecular weight marker and the estimated molecular weight of the protein of interest. Recommend a suitable buffer for dialyzing (ammonium sulfate precipitate) or dissolving (lyophilized material) the protein. If this is not a standard buffer, add your buffer in sufficient amount (esp. for dialysis). Mention special requirements of your protein with respect to solubility and stability (especially important for membrane proteins).

Required Information:

Protein identity (incl. database entry number) and source of the protein (organism, tissue, cell type, sub-cellular fraction etc.).

Please ship the protein without cooling (dried gel bands, lyophilized protein) or on blue ice (ammonium sulfate precipitate) to:

Gentaur
Avenue de l'Armée 68/B4
B-1040 Brussels BELGIUM
 
Our service:
  1. (In gel) trypsination of the protein (band) of interest (protein is cleaved at arg and lys sites into peptides)
  2. MALDI-TOF Mass Spectometry analysis of the tryptic peptides
  3. Peptides carrying posttranslational modifications are identified by comparing their actual mass with their theoretical mass peak by peak. This process is carried out by experienced scientists. A list of experimental peptides that correspond to unmodified peptides is generated, then a list of experimental peptides that match to peptides which carry modifications of cystein residues, methionine residues, or other modification as documented in SWISS-PROT is created. In order to find novel modifications, the mass differences between all experimental peptides and all theoretical peptides are calculated. If a mass difference corresponds to the mass of any known modification the peptide is classified as potentially modified. Within the peptide the potential amino acid(s) that may carry the modification in question is/are suggested.
 
Order Information:

Cat. Nr. IPM01: Identification of Posttranslational Protein Modification by MALDI-TOF-MS, protein shipped in protein gel band
Price: 650 $

Cat. Nr. IPM02: Identification of Posttranslational Protein Modification by MALDI-TOF-MS, purified protein provided
Price: 720 $

Please note: In case the protein amount or purity was not sufficient to perform MALDI-TOF MS, a set up fee of € 175 is charged.

 
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Identification

Storage Logistics

You provide us with a,b, or c:

a) Homogenous protein in an excised band from a dried SDS-gel (stained with Coomassie Blue or Silver, preferably without fixation). Please enclose a gel photo. Please mention the %age of the gel, clearly mark the band which was excised from the gel, and specify the molecular weight marker and the estimated molecular weight of the protein of interest.

b) Homogenous protein in an excised spot from a dried 2-D-Gel (stained with Coomassie Blue or Silver, preferably without fixation). Please enclose a gel photo. Please clearly mark the spot which was excised from the gel.

c) At least 5 µg purified native protein (ammonium sulfate precipitate or lyophilizd protein). Please enclose a gel photo (SDS-PAGE), mention the %age of the gel, clearly mark the band which corresponds to the purified protein, and specify the molecular weight marker and the estimated molecular weight of the protein of interest. Recommend a suitable buffer for dialyzing (ammonium sulfate precipitate) or dissolving (lyophilized material) the protein. If this is not a standard buffer, add your buffer in sufficient amount (esp. for dialysis). Mention special requirements of your protein with respect to solubility and stability (especially important for membrane proteins).

Required Information:

Source of the protein (organism, tissue, cell fraction etc.) and, if possible, any assumption about the nature and/or function of the protein of interest.
If available: Molecular Weight of protein and its subunits, and isoelectrical point.

Please ship the protein without cooling (dried gel bands or spots, lyophilized protein) or on blue ice (ammonium sulfate precipitate) to:

Gentaur bvba
Avenue de l'Armée 68/B4,  B-1040 Brussels
 
Our service:
  1. (In gel) trypsination of the protein (band or spot) of interest (protein is cleaved at arg and lys sites into peptides)
  2. MALDI-TOF Mass Spectometry analysis of the tryptic peptides
  3. Protein identification by computational tools (database searching combined with Bayesian statistics): Masses of peptides from the proteolytic digestion of the corresponding protein are compared to the masses of a peptide database based on the non redundant information extracted from NCBI, GenBank, CDS translations, PDB, SwissProt, PIR, and PRF protein databases. The result is a ranking of candidate proteins based on their calculated posterior probability. The protein identity is re-verified using pI, MW and peptide mass fingerprinting data and comparing them with the theoretical peptides calculated for all proteins of question in the SWISS-PROT/TrEMBL databases. This verification process is carried out by trained scientists who verify the protein identity by checking the peptide pattern peak by peak for plausibility taking trypsin autolysis and trypsin cleavage faults into account.
  4. You receive a detailed analysis report featuring the identity of the protein and the likelihood of the correctness of the identification. In case it is a new protein, the features of similar/related proteins are listed.
 
Order Information:

Cat. Nr. PIPB01: Protein Identification by MALDI-TOF-MS, protein shipped in protein gel band
Price: 500 $

Cat. Nr. PIPS01: Protein Identification by MALDI-TOF-MS, protein shipped in 2 D gel spot
Price: 500 $

Cat. Nr. PIPP01: Protein Identification by MALDI-TOF-MS, purified protein provided
Price: 570 $

Please note: In case the protein amount or purity was not sufficient to perform MALDI-TOF MS, a set up fee of € 175 is charged.
Protein Candidates
Rank
Probability
 Protein Description
MW (kDa)
1
1.0e+00
 gi|6324486|ref|NP_014555.1| Alcohol dehydrogenase; Adh1p [Saccharomyces cerevisiae]
37
2
3.2e-03
 gi|1168350|sp|P00330|ADH1_YEAST ALCOHOL DEHYDROGENASE I
37
3
7.8e-09
 gi|6324174|ref|NP_014244.1| Ynl155wp [Saccharomyces cerevisiae]
32
4
1.1e-09
 gi|7245674|pdb|1YLV|A Chain A, Schiff-Base Complex Of Yeast 5-Aminolaevulinic Acid Dehydratase With Laevulinic Acid
38
5
3.9e-10
 gi|171974|gb|AAA34790.1| (M81696) mitochondrial ribosomal protein [Saccharomyces cerevisiae]
29
6
3.2e-10
 gi|6325350|ref|NP_015418.1| Ypr093cp [Saccharomyces cerevisiae]
36
7
3.0e-10
 gi|223142|prf||0512226A dehydrogenase isozyme I,alcohol [Saccharomyces cerevisiae]
32
8
3.0e-10
 gi|6320613|ref|NP_010693.1| 263-amino acid mitochondrial ribosomal large subunit protein; similar to L23 family of ribosomal proteins; Mrp20p [Saccharomyces cerevisiae]
31
9
1.2e-10
 gi|626218|pir||S45958 probable membrane protein YBR090c - yeast (Saccharomyces cerevisiae)
13
10
1.2e-10
 gi|6319560|ref|NP_009642.1| mitochondrial ADP/ATP translocator; Aac3p [Saccharomyces cerevisiae]
33
       
The contaminating protein was identified as alcohol dehydrogenase and could now be removed easily from the mixture by exploiting its known hydrophobicity (washing the column with isopropanol).
 
Our service:

Sample preparation and MALDI-TOF Mass Spectrometry of the protein. Determination of the absolute mass of the protein subunit(s).
 
Order Information:

Cat. Nr. DMW01
Absolute Molecular Weight Determination of purified protein by MALDI-TOF MS
Price: 225 $
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Molecular weight

MALDI-TOF Determination of the absolute molecular weight of the protein subunit(s)


You provide us with:

At least 10 pmol purified native protein (for subunit molecular weigths up to 30 kDA) or 20 pmol (for subunit molecular weigths up to 100 kDA). For larger proteins more protein is needed. The protein may be ammonium sulfate precipitated or lyophilized. Please enclose a photo of an analytical SDS-PAGE, mention the %age of the gel, clearly mark the band which corresponds to the purified protein, and specify the molecular weight marker and the estimated molecular weight of the protein of interest. Recommend a suitable buffer for dialyzing (ammonium sulfate precipitate) or dissolving (lyophilized material) the protein. If this is not a standard buffer, add your buffer in sufficient amount (esp. for dialysis). Mention special requirements of your protein with respect to solubility and stability (especially important for membrane proteins).

Please ship the protein without cooling (lyophilized protein) or on blue ice (ammonium sulfate precipitate) to:

Gentaur
Avenue de l'Armée 68/B4
B-1040 Brussels

Belgium


Our service: 
Sample preparation and MALDI-TOF Mass Spectrometry of the protein. Determination of the absolute mass of the protein subunit(s).


Order Information:

Cat. Nr. DMW01
Absolute Molecular Weight Determination of purified protein by MALDI-TOF MS
Price: 225 $
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MALDI TOF

 

Cutting out of Bands or Spots of Interest


We offer a MALDI TOF mass analysis and protein identification service together with our partner Mobidab GmbH & Co. KG in Leipzig. All protein gels will be dried by Fraunhofer IGB and will be stored until you have analysed the results. Bands or spots of interest might be cut by Fraunhofer IGB according to your instructions and sent to Mobidab GmbH & Co. KG together with the protein gel data for further analysis.

Order Information:

Cat. No.: CO01
Cut Out of Protein Band or Spot for further analysis by MALDI TOF mass spectometry 15 $ per band or spot.
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Quantitative

Comparative Quantitative Analysis of Electrophoresis Results


The 1 or 2 D gel images will be processed and recorded in TIF format. The TIF files are analysed by the Phoretix analysis software and a detailed analysis report is generated. The report lists the total number of bands or spots, as well as all protein bands or spots which are differentially expressed in the 2 compared samples and gives the quantitative difference of protein amount in the 2 samples for each of these bands or spots.

Cat. No.: CQA01
Quantitative Comparison of 2 comparative 1 D SDS PAGE electrophoresis experiments; 250 $

Cat. No.: CQA02
Quantitative Comparison of 2 comparative 2 D SDS PAGE electrophoresis experiments; 1295 $
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