Recombinant Human Complexin-2 (CPLX2) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-08812P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Human Complexin-2 (CPLX2) Protein (GST)

Beta LifeScience SKU/CAT #: BLC-08812P
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

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Product Overview

Description Recombinant Human Complexin-2 (CPLX2) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q6PUV4
Target Symbol CPLX2
Synonyms 921 L; Complexin 2; Complexin II; Complexin-2; Complexin2; ComplexinII; CPLX 2; Cplx2; CPLX2_HUMAN; CPX 2; CPX II; CPXII; Hfb1; Synaphin 1; Synaphin-1; Synaphin1
Species Homo sapiens (Human)
Expression System E.coli
Tag N-GST
Target Protein Sequence MDFVMKQALGGATKDMGKMLGGEEEKDPDAQKKEEERQEALRQQEEERKAKHARMEAEREKVRQQIRDKYGLKKKEEKEAEEKAALEQPCEGSLTRPKKAIPAGCGDEEEEEEESILDTVLKYLPGPLQDMFKK
Expression Range 1-134aa
Protein Length Full Length
Mol. Weight 42.4kDa
Research Area Others
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Negatively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. Positively regulates a late step in exocytosis of various cytoplasmic vesicles, such as synaptic vesicles and other secretory vesicles. Also involved in mast cell exocytosis.
Subcellular Location Cytoplasm, cytosol. Cell junction, synapse, presynapse. Nucleus. Perikaryon.
Protein Families Complexin/synaphin family
Database References

HGNC: 2310

OMIM: 605033

KEGG: hsa:10814

STRING: 9606.ENSP00000352544

UniGene: PMID: 27866231

  • Then results indicated that CPLX2 may be involved in the etiology of schizophrenia and one of its potential biological mechanisms by studying the effects of CPLX2 risk variants on working memory load-dependent neural activity in a frontoparietal network. PMID: 25297695
  • These results suggested that CPLX2 participated in synaptic taste transduction. PMID: 25692331
  • CPLX2 rs1366116*T variant represents a risk factor of schizophrenia, and , at the same time, CPLX2 rs3892909*T variant is protective against schizophrenia (study performed in Armenians). PMID: 25564026
  • role in synaptic vesicle exocytosis PMID: 12058476
  • altered immunoreactivity of this protein in prefrontal cortex in severe mental illness PMID: 12082566
  • in huntingtin mutation, the decline in neurotransmitter release is a direct consequence of complexin II depletion PMID: 12807877
  • In schizophrenia, complexin II was reduced in dorsolateral prefrontal cortex and superior temporal cortex. The impairment of synaptic transmission may contribute to the dysfunction of cortical neural circuits that characterises the disorder. PMID: 15653259
  • CX2 level increased between the fetal and the 6-10 years groups and then plateaued PMID: 18240322
  • 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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