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ADAMTS12 recombinant protein :: A Disintegrin And Metalloproteinase With Thrombospondin 12 (ADAMTS12) Recombinant Protein

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Catalog # MBS2010993 (SPECIAL PROMOTION: Get FREE $5 Starbucks gift card (Maximum 5 gift cards/product). Gift card(s) will be included with shipment)
Unit / Price
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  0.01 mg  /  $145 +1 FREE 8GB USB
  0.05 mg  /  $280 +1 FREE 8GB USB
  0.1 mg  /  $435 +1 FREE 8GB USB
  0.2 mg  /  $535 +1 FREE 8GB USB
  0.5 mg  /  $1,035 +1 FREE 8GB USB
  1 mg  /  $1,540 +1 FREE 8GB USB
Product Name

A Disintegrin And Metalloproteinase With Thrombospondin 12 (ADAMTS12), Recombinant Protein

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Full Product Name

Recombinant A Disintegrin And Metalloproteinase With Thrombospondin 12 (ADAMTS12)

Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
The target protein is fused with N-terminal His-Tag, its sequence is listed below.
Chromosome Location
Chromosome: 2; NC_000002.11 (179390716..179672150, complement). Location: 2q31
3D Structure
ModBase 3D Structure for Q8WZ42
E Coli
> 95%
Supplied as lyophilized form in PBS,pH7.4, containing 5% sucrose, 0.01% sarcosyl.
Mus musculus (Mouse)
Expression System
Prokaryotic expression
Lys827~Pro1001 (Accession # Q8WZ42) with N-terminal His-Tag
Endotoxin Level
<1.0EU per 1ug (determined by the LAL method)
Reconstitute in sterile PBS, pH7.2-pH7.4.
Preparation and Storage
Avoid repeated freeze/thaw cycles. Store at 2-8 degree C for one month. Aliquot and store at -80 degree C for 12 months.
Stability Test: The thermal stability is described by the loss rate of the targetprotein. The loss rate was determined by accelerated thermal degradation test,that is, incubate the protein at 37 degree C for 48h, and no obvious degradation andprecipitation were observed. (Referring from China Biological Products Standard,which was calculated by the Arrhenius equation.) The loss of this protein is lessthan 5% within the expiration date under appropriate storage condition.
ISO Certification
Manufactured in an ISO 9001:2008 and ISO 13485:2003 Certified Laboratory.
Supply Chain Verification
Manufactured in a lab with traceable raw materials. Bulk orders can typically be prepared to the customer’s specifications, please inquire.
Other Notes
Small volumes of ADAMTS12 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
Related Product Information for
ADAMTS12 recombinant protein
About the Marker: Effective Size Range: 10kDa to 70kDa.
Protein bands: 10kDa, 14kDa, 18kDa, 22kDa, 26kDa, 33kDa, 44kDa and70kDa.
Double intensity bands: The 26kDa, 18kDa, 10kDa bands are at doubleintensity to make location and size approximation of proteins of interestquick and easy.
Ready-to-use: No need to heat, dilute or add reducing agents before use.
Applications Tested/Suitable for ADAMTS12 recombinant protein
SDS-PAGE, Western Blot (WB), ELISA (EIA), Immunoprecipitation (IP)

NCBI/Uniprot data below describe general gene information for ADAMTS12. It may not necessarily be applicable to this product.
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
NCBI Official Full Name
titin isoform N2BA
NCBI Official Synonym Full Names
NCBI Official Symbol
NCBI Official Synonym Symbols
  [Similar Products]
NCBI Protein Information
titin; connectin; rhabdomyosarcoma antigen MU-RMS-40.14
UniProt Protein Name
UniProt Synonym Protein Names
Connectin; Rhabdomyosarcoma antigen MU-RMS-40.14
UniProt Gene Name
UniProt Entry Name
NCBI Summary for ADAMTS12
This gene encodes a large abundant protein of striated muscle. The product of this gene is divided into two regions, a N-terminal I-band and a C-terminal A-band. The I-band, which is the elastic part of the molecule, contains two regions of tandem immunoglobulin domains on either side of a PEVK region that is rich in proline, glutamate, valine and lysine. The A-band, which is thought to act as a protein-ruler, contains a mixture of immunoglobulin and fibronectin repeats, and possesses kinase activity. An N-terminal Z-disc region and a C-terminal M-line region bind to the Z-line and M-line of the sarcomere, respectively, so that a single titin molecule spans half the length of a sarcomere. Titin also contains binding sites for muscle associated proteins so it serves as an adhesion template for the assembly of contractile machinery in muscle cells. It has also been identified as a structural protein for chromosomes. Alternative splicing of this gene results in multiple transcript variants. Considerable variability exists in the I-band, the M-line and the Z-disc regions of titin. Variability in the I-band region contributes to the differences in elasticity of different titin isoforms and, therefore, to the differences in elasticity of different muscle types. Mutations in this gene are associated with familial hypertrophic cardiomyopathy 9, and autoantibodies to titin are produced in patients with the autoimmune disease scleroderma. [provided by RefSeq, Feb 2012]
UniProt Comments for ADAMTS12
Function: Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sarcomere extensibility properties of muscle. In non-muscle cells, seems to play a role in chromosome condensation and chromosome segregation during mitosis. Might link the lamina network to chromatin or nuclear actin, or both during interphase. Ref.28

Catalytic activity: ATP + a protein = ADP + a phosphoprotein.

Cofactor: Magnesium.

Enzyme regulation: Full activation of the protein kinase domain requires both phosphorylation of Tyr-32341, preventing it from blocking the catalytic aspartate residue, and binding of Ca/CALM to the C-terminal regulatory tail of the molecule which results in ATP binding to the kinase. Ref.28

Subunit structure: Interacts with MYOM1, MYOM2, tropomyosin and myosin. Interacts with actin, primarily via the PEVK domains and with MYPN

By similarity. Interacts with FHL2, NEB, CRYAB, LMNA/lamin-A and LMNB/lamin-B. Interacts with TCAP/telethonin and/or ANK1 isoform Mu17/ank15, via the first two N-terminal immunoglobulin domains. Interacts with TRIM63 and TRIM55, through several domains including immunoglobulin domains 141 and 142. Interacts with ANKRD1, ANKRD2 and ANKRD23, via the region between immunoglobulin domains 77 and 78 and interacts with CAPN3, via immunoglobulin domain 79. Interacts with NBR1 through the protein kinase domain. Interacts with CALM/calmodulin. Isoform 6 interacts with OBSCN isoform 3. Interacts with CMYA5. Ref.3 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.26 Ref.28 Ref.38

Subcellular location: Cytoplasm

Probable. Nucleus Ref.23.

Tissue specificity: Isoforms 3, 7 and 8 are expressed in cardiac muscle. Isoform 4 is expressed in vertebrate skeletal muscle. Isoform 6 is expressed in skeletal muscle (at protein level). Ref.3 Ref.7

Domain: ZIS1 and ZIS5 regions contain multiple SPXR consensus sites for ERK- and CDK-like protein kinases as well as multiple SP motifs. ZIS1 could adopt a closed conformation which would block the TCAP-binding site.The PEVK region may serve as an entropic spring of a chain of structural folds and may also be an interaction site to other myofilament proteins to form interfilament connectivity in the sarcomere.

Post-translational modification: Autophosphorylated

By similarity. Ref.14 Ref.28

Involvement in disease: Hereditary myopathy with early respiratory failure (HMERF) [MIM:603689]: Autosomal dominant, adult-onset myopathy with early respiratory muscle involvement.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.38Cardiomyopathy, familial hypertrophic 9 (CMH9) [MIM:613765]: A hereditary heart disorder characterized by ventricular hypertrophy, which is usually asymmetric and often involves the interventricular septum. The symptoms include dyspnea, syncope, collapse, palpitations, and chest pain. They can be readily provoked by exercise. The disorder has inter- and intrafamilial variability ranging from benign to malignant forms with high risk of cardiac failure and sudden cardiac death.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.32Cardiomyopathy, dilated 1G (CMD1G) [MIM:604145]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.34 Ref.35 Ref.37Tardive tibial muscular dystrophy (TMD) [MIM:600334]: Autosomal dominant, late-onset distal myopathy. Muscle weakness and atrophy are usually confined to the anterior compartment of the lower leg, in particular the tibialis anterior muscle. Clinical symptoms usually occur at age 35-45 years or much later.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.33 Ref.36Limb-girdle muscular dystrophy 2J (LGMD2J) [MIM:608807]: An autosomal recessive degenerative myopathy characterized by progressive weakness of the pelvic and shoulder girdle muscles. Severe disability is observed within 20 years of onset.Note: The disease is caused by mutations affecting the gene represented in this entry.Early-onset myopathy with fatal cardiomyopathy (EOMFC) [MIM:611705]: Early-onset myopathies are inherited muscle disorders that manifest typically from birth or infancy with hypotonia, muscle weakness, and delayed motor development. EOMFC is a titinopathy that, in contrast with the previously described examples, involves both heart and skeletal muscle, has a congenital onset, and is purely recessive. This phenotype is due to homozygous out-of-frame TTN deletions, which lead to a total absence of titin's C-terminal end from striated muscles and to secondary CAPN3 depletion.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.39

Miscellaneous: In some isoforms, after the PEVK repeat region there is a long PEVK duplicated region. On account of this region, it has been very difficult to sequence the whole protein. The length of this region (ranging from 183 to 2174 residues), may be a key elastic element of titin.

Sequence similarities: Belongs to the protein kinase superfamily. CAMK Ser/Thr protein kinase family.Contains 132 fibronectin type-III domains.Contains 152 Ig-like (immunoglobulin-like) domains.Contains 19 Kelch repeats.Contains 1 protein kinase domain.Contains 17 RCC1 repeats.Contains 14 TPR repeats.Contains 15 WD repeats.

Sequence caution: The sequence AAH58824.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 553.The sequence AAH70170.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence starting in position 627.The sequence CAA62188.1 differs from that shown. Reason: Frameshift at positions 17036 and 17043. The sequence CAD12455.1 differs from that shown. Reason: Frameshift at positions 17036 and 17043.
Research Articles on ADAMTS12
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While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

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