Recombinant Human DPYSL2 Protein

Beta LifeScience SKU/CAT #: BL-1515SG

Recombinant Human DPYSL2 Protein

Beta LifeScience SKU/CAT #: BL-1515SG
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Product Overview

Tag GST
Host Species Human
Accession BC056408
Synonym CRMP2, DHPRP2, DRP-2, DRP2
Background Dihydropyrimidinase-related protein 2 (DPYSL2) is express-ed in both the CNS and PNS, playing a key role in neuronal development, axonal and neuronal growth, cell migration, and protein trafficking. Disruptions of DPYSL2 function have been implicated in neurodegenerative disorders such as Alzheimer's disease, neuropathic pain, and Batten disease, and to psychiatric disorders such as schizophrenia.
Description Full-length recombinant human DPYSL2 was produced by baculovirus in Sf9 insect cells, fused with a GST tag at N-terminus. This protein is purified with our unique purification methods.
Source Sf9 insect cells
AA Sequence Full Length
Molecular Weight ~89 kDa
Purity For specific purity information on a given lot, see related COA.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability The recombinant protein is stable for up to 12 months at -70°C
Usage For Research Use Only
Storage Recombinant Human DPYSL2 Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function Plays a role in neuronal development and polarity, as well as in axon growth and guidance, neuronal growth cone collapse and cell migration. Necessary for signaling by class 3 semaphorins and subsequent remodeling of the cytoskeleton. May play a role in endocytosis.
Subcellular Location Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Membrane. Note=Tightly but non-covalently associated with membranes.
Protein Families Metallo-dependent hydrolases superfamily, Hydantoinase/dihydropyrimidinase family
Database References

HGNC: 3014

OMIM: 602463

KEGG: hsa:1808

STRING: 9606.ENSP00000309539

UniGene: PMID: 27940916

  • crystal structure of human tetrameric CRMP-2 PMID: 28044206
  • increased pCRMP2 may underlie the axonal pathology of Lewy body dementias. PMID: 27609071
  • These data identify a novel oncogenic mechanism where CDK5 activation induces CRMP2A phosphorylation in the nuclei of tumour cells PMID: 26555036
  • polymorphisms of the DPYSL2 gene in humans may be associated with the development of schizophrenia. PMID: 25847191
  • Functional variants in DPYSL2 sequence increase risk of schizophrenia and suggest a link to mTOR signaling PMID: 25416705
  • Changes for CRMP2, TCP1epsilon, TPM2 and 14-3-3gamma were confirmed in experimental tumors and in a series of 28 human SI-NETs. PMID: 25224486
  • Reduced CRMP2 expression and elevated expression of nuclear phosphorylated CRMP2 may be associated with breast cancer progression. PMID: 23381229
  • Levels of total GSK3 were decreased in the Huntington disease-affected frontal cortex and this correlated with decreased phosphorylated CRMP2. PMID: 24634145
  • High dihydropyrimidinase-related protein 2 expression is associated with lung cancer. PMID: 24518087
  • genetic variants in DPYSL2 may play a role in susceptibility to alcohol dependence. PMID: 23846846
  • A specific and reversible intermolecular Cys-504-Cys-504 dithiol-disulfide switch in homotetrameric CRMP2 determines two conformations of the quaternary CRMP2 complex that controls axonal outgrowth and thus neuronal development. PMID: 24133216
  • CRMP-2-dependent regulation of ROCK II activity is mediated through interaction of the CRMP-2L N terminus with the ROCK II catalytic domain as well as by GSK3-dependent phosphorylation of CRMP-2. PMID: 24036111
  • a novel regulatory mechanism that utilizes CRMP2 SUMOylation to choreograph NaV1.7 trafficking. PMID: 23836888
  • a new insight into CRMP-2 as a controller of myosin II-mediated cellular functions through the inhibition of ROCK II in nonneuronal cells PMID: 22431514
  • No Alzheimer disease-associated differences in CNP and DPYSL2 promoter DNA methylation were observed. PMID: 22954668
  • Deletion analysis of CRMP-2 identified a 51 amino acid sequence in the C-terminus that is required for targeting to the basal body and primary cilium. This domain contains GSK-3beta phosphorylation sites. PMID: 23185275
  • High levels of nuclear phosphorylated CRMP-2 is associated with lung cancer. PMID: 23023514
  • CRMP2 hyperphosphorylation is speci fi c to Alzheimer's disease and is not a common event in all forms of dementia and neurodegeneration, especially other tauopathies. PMID: 21860090
  • findings suggest a major role of phosphorylated CRMP-2 as a mechanism involved in process retraction induced by reactive oxygen species PMID: 22443207
  • HTLV-1 has the capacity to influence the CRMP2/PI3K/Akt axis thus to positively control cytoskeleton organization and lymphocyte migration. PMID: 22227566
  • CRMP2 controls dendritic projection; the phosphorylation of CRMP2 at Ser522 is essential for proper dendritic field organization for axonal guidance and spine development . PMID: 22279220
  • This review discusses the essential biology of CRMP2 in the context of nascent data implicating CRMP2 perturbations as either a correlate of, or plausible contributor to, diverse neuropathologies. PMID: 21271304
  • Data support DPYSL2 and the surrounding genomic region as a susceptibility locus for schizophrenia. PMID: 21302347
  • Data provide the first trafficking regulatory role for Crmp2 in non-neuronal cells and support a model in which Crmp2 is an important endocytic regulatory protein that links MICAL-L1.EHD1-based vesicular transport to dynein motors. PMID: 20801876
  • DPYSL2 does not have a major function in schizophrenia in Japanese subjects. PMID: 20414250
  • CRMP2 as a tubulin direct binder may be a GTPase-activating protein (GAP) of tubulin in neurite formation and its GAP activity may be regulated by an intramolecular interaction with an N-terminal inhibitory region. PMID: 19666111
  • Aberrant expression of dihydropyrimidinase related proteins-2,-3 and -4 in fetal Down syndrome brain. PMID: 11771764
  • No significant associations were found between five polymorphisms of the DRP-2 gene and Bipolar Disorder, nor were associations detected between either of the polymorphisms and bipolar subtypes I and II. PMID: 12951196
  • Here we show that glial cell line-derived neurotrophic factor (GDNF) enhances CRMP-2 expression in TGW human neuroblastoma cells via activation of RET receptor tyrosine kinase. PMID: 15207709
  • significant decrease of crmp-2 protein may represent or underlie impaired neuronal plasticity, neurodegeneration, wiring of the brain in mesial temporal lobe epilepsy PMID: 15672539
  • CRMP-2 transports the Sra-1/WAVE1 complex to axons in a kinesin-1-dependent manner and thereby regulates axon outgrowth and formation PMID: 16260607
  • collapsin response mediator protein-2 transcriptional activity is inhibited by all-trans-retinoic acid during SH-SY5Y neuroblastoma cell differentiation PMID: 17229153
  • These observations implicate hyperphosphorylation of CRMP2 as an early event in the development of AD and suggest that it can be induced by a severe APP over-expression and/or processing defect. PMID: 17683481
  • results indicate that that CRMP-2 may be a novel colorectal cancer biomarker PMID: 18203259
  • association of neurofibromin and CRMP-2 is essential for neuronal cell differentiation PMID: 18218617
  • relative resistance to phosphatases might be a common feature of Cdk5 substrates and could contribute to the hyperphosphorylation of CRMP2 and Tau observed in Alzheimer disease PMID: 18460467
  • Data suggest that collapsin response mediator protein-2 (CRMP-2) is a novel calmodulin-binding protein and that CaM binding may play an important role in regulating CRMP-2 functions. PMID: 19151921
  • Given that CRMP-2 is a key regulator of axon elongation, this interference with cytoplasmic dynein function by CRMP-2 might have an important role in axon formation, and neuronal development PMID: 19659462
  • A significant association was found between a single nucleotide polymorphism of the DRP-2 gene and schizophrenia in a North American sample. PMID: 15858820
  • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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