D-Dimer rapid test
- Known as:
- D-Dimer rapid test
- Catalog number:
- WED03
- Product Quantity:
- test x 10
- Category:
- -
- Supplier:
- Wed bio
- Gene target:
- D-Dimer rapid test
Related genes to: D-Dimer rapid test
- Gene:
- SPOCK1 NIH gene
- Name:
- SPARC (osteonectin), cwcv and kazal like domains proteoglycan 1
- Previous symbol:
- TIC1, SPOCK
- Synonyms:
- testican-1
- Chromosome:
- 5q31.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-10-02
- Date modifiied:
- 2018-02-23
- Gene:
- SPOCK2 NIH gene
- Name:
- SPARC (osteonectin), cwcv and kazal like domains proteoglycan 2
- Previous symbol:
- -
- Synonyms:
- KIAA0275, testican-2
- Chromosome:
- 10q22.1
- Locus Type:
- gene with protein product
- Date approved:
- 2003-01-24
- Date modifiied:
- 2018-02-23
- Gene:
- SPOCK3 NIH gene
- Name:
- SPARC (osteonectin), cwcv and kazal like domains proteoglycan 3
- Previous symbol:
- -
- Synonyms:
- testican-3
- Chromosome:
- 4q32.3
- Locus Type:
- gene with protein product
- Date approved:
- 2003-01-24
- Date modifiied:
- 2018-02-23
Related products to: D-Dimer rapid test
Human ELC ELISA KIT 96 TEST
(R/S)-Pramipexole C-C Dimer Impurity (mixture of diastereomers)
DISCONTINUED CAS: Formula: C20H32N6S2(R_S)-Pramipexole C-C Dimer Impurity (mixture of diastereomers)
C20H32N6S2 CAS:(S)-Lisinopril Dimer C42H60N6O9 CAS:(S)-Lisinopril Dimer CAS: Formula: C42H60N6O9(S)-Lisinopril Dimer-d5 C42H55D5N6O9 CAS:(S)-Lisinopril Dimer-d5 CAS: Formula: C42H55D5N6O9(Trp11,D_Phe15·16)_SDF_1 (7_16) (Dimer) (human, cat, mouse) Salt Trifluoroacetate Binding (Disulfide_bond) Synonym (Trp11,D_Phe15·16)_CXCL12 (7_16) (Dimer) (human, cat, mouse ), (Trp11,D_Phe15·16)_(Trp11,D_Phe15·16)_SDF_1 (7_16) (Dimer) (human, cat, mouse) Salt Trifluoroacetate Binding (Disulfide_bond) Synonym (Trp11,D_Phe15·16)_CXCL12 (7_16) (Dimer) (human, cat, mouse ), (Trp11,D_Phe15·16)_(Trp11,D_Phe15·16)_SDF_1 (7_16) (Dimer) (human, cat, mouse) Salt Trifluoroacetate Binding (Disulfide_bond) Synonym (Trp11,D_Phe15·16)_CXCL12 (7_16) (Dimer) (human, cat, mouse ), (Trp11,D_Phe15·16)_(Trp11,D_Phe15·16)_SDF_1 (7_16) (Dimer) (human, cat, mouse) Salt Trifluoroacetate Binding (Disulfide_bond) Synonym (Trp11,D_Phe15·16)_CXCL12 (7_16) (Dimer) (human, cat, mouse ), (Trp11,D_Phe15·16)_([125I]-Tyr)-b-Atrial Natriuretic Factor (1-28) (Dimer, Antiparallel) (human)([125I]-Tyr)-b-Atrial Natriuretic Factor (1-28) (Dimer, Antiparallel) (human)([125I]-Tyr)-b-Atrial Natriuretic Factor (1-28) (Dimer, Antiparallel) (human), CE-marked, Liquid([125I]-Tyr)-b-Atrial Natriuretic Factor (1-28) (Dimer, Antiparallel) (human), CE-marked, Liquid Related articles to: D-Dimer rapid test
- SPARC/osteonectin, CWCV and Kazal‑like domain proteoglycan (SPOCK) is a family of highly conserved multidomain proteins. In total, three such family members, , and , constitute the majority of extracellular matrix glycoproteins. The gene family has been demonstrated to serve key roles in tumor regulation by affecting MMPs, which accelerates the progression of cancer epithelial‑mesenchymal transition. In addition, they can regulate the cell cycle via overexpression, inhibit tumor cell proliferation by inactivating PI3K/AKT signaling and have been associated with numerous microRNAs that influence the expression of downstream genes. Therefore, the SPOCK gene family are potential cancer‑regulating genes. The present review summarizes the molecular structure, tissue distribution and biological function of the SPOCK family of proteins, in addition to its association with cancer. Furthermore, the present review documents the progress made in investigations into the role of SPOCK, whilst also discussing prospects for the future of SPOCK‑targeted therapy, to provide novel ideas for clinical application and treatment. - Source: PubMed
Publication date: 2024/10/11
Xiao MingyuanXue JianchengJin Enli - Spock3/Testican-3 is a nervous system-expressed heparan sulfate proteoglycan belonging to a subgroup of the BM-40/SPARC/osteonectin family, the role of which in brain development is unclear. Because Spock1, a member of the Spock family, inhibits their attachment to substrates and the neurite outgrowth of cultured neuronal cells, Spock3 is also thought to be similarly involved in the neuronal development. In the present study, we established a Spock3-mutant mouse harboring a deletion extending from the presumptive upstream regulatory region to exon 4 of the Spock3 locus and performed histological and behavioral studies on these mutant mice. In wild-type (WT) mice, all Spock members were clearly expressed during brain development. In adults, intense Spock1 and Spock2 expressions were observed throughout the entire brain; whereas, Spock3 expression was no longer visible except in the thalamic nuclei. Thus, Spock3 expression is mostly confined to the developmental stage of the brain. In adult mutant mice, the cells of all cortical layers were swollen. The corpus callosum was narrowed around the central region along the rostral-caudal axis and many small spaces were observed without myelin sheaths throughout the entire corpus callosum. In addition, the cortical input and output fibers did not form into thick bundled fibers as well as the WT counterparts did. Moreover, a subpopulation of corticospinal axonal fibers penetrated into the dorsal striatum with moderately altered orientations. Consistent with these modifications of brain structures, the mutant mice exhibited decreased anxiety-like behavior and lowered sociability. Together, these results demonstrate that Spock3 plays an important role in the formation or maintenance of major neuronal structures in the brain. - Source: PubMed
Publication date: 2014/08/19
Yamamoto AyakoUchiyama KojiNara TomokaNishimura NaomichiHayasaka MichikoHanaoka KazunoriYamamoto Tatsuro - Using expression cloning to screen a human fetal kidney cDNA library for regulator(s) of pro-matrix metalloproteinase (MMP)-2 processing mediated by membrane-type (MT) 1 MMP, we isolated a cDNA whose product interfered with pro-MMP-2 activation. It encodes the NH(2)-terminal 313-amino acid region of a calcium-binding proteoglycan, testican 3, with a 3-amino acid substitution at the COOH terminus and thus was named N-Tes. N-Tes comprises a signal peptide, a unique domain, a follistatin-like domain, and a Ca(2+)-binding domain but lacks a COOH-terminal thyroglobulin domain and two putative glycosaminoglycan attachment sites of testican 3. Pro-MMP-2 activation by MT3-MMP was also inhibited by the coexpression of N-Tes. Immunoprecipitation analysis demonstrated direct interaction of N-Tes with either MT1-MMP or MT3-MMP. Expression of testican 1 or testican 3 but not testican 2 also inhibited pro-MMP-2 activation by either MT1-MMP or MT3-MMP. Deletion and substitution of amino acids residues in N-Tes revealed that the unique NH(2)-terminal domain of N-Tes is responsible for the inhibition of pro-MMP-2 activation by MT-MMPs. Expression of N-Tes and testican 3 was detected in normal brain but down-regulated in glioma tissues. Transfection of either the N-Tes or testican 3 gene into U251 glioma cells or Madin-Darby canine kidney cells transformed by erbB2 suppressed their invasive growth in collagen gel. These results suggest that both N-Tes and testican 3 would interfere with tumor invasion by inhibiting MT-MMPs. - Source: PubMed
Nakada MYamada ATakino TMiyamori HTakahashi TYamashita JSato H