3742 Results for: "single-use assemblies"
Anti-DDX21 Rabbit Polyclonal Antibody
Supplier: Prosci
DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which is an antigen recognized by autoimmune antibodies from a patient with watermelon stomach disease. This protein unwinds double-stranded RNA, folds single-stranded RNA, and may play important roles in ribosomal RNA biogenesis, RNA editing, RNA transport, and general transcription.
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Anti-DDX21 Rabbit Polyclonal Antibody
Supplier: Genetex
DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which is an antigen recognized by autoimmune antibodies from a patient with watermelon stomach disease. This protein unwinds double-stranded RNA, folds single-stranded RNA, and may play important roles in ribosomal RNA biogenesis, RNA editing, RNA transport, and general transcription. [provided by RefSeq]
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Anti-ATP5J Rabbit Polyclonal Antibody
Supplier: Prosci
Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The Fo seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8). This gene encodes the F6 subunit of the Fo complex, required for F1 and Fo interactions. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. A pseudogene exists on chromosome Yp11.
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Human [Gln22, Asn23]-beta-Amyloid (1-40)
Supplier: Anaspec
This peptide is the mutant form of beta-Amyloid 1 to 40. These mutations within the beta-Amyloid precursor protein (APP) regions result in the substitution of glutamine for glutamic acid and asparagine for aspartic acid. The peptide rapidly assembles in solution to form fibrils compared to the wild-type beta-Amyloid 1 to 40. Double-mutant E22Q/D23N Dutch/Iowa beta-Amyloid 40 is more potent than either of the single mutant form in causing pathologic responses in culture cells. The double mutations further enhances the fibrillogenic and pathogenic properties of beta-Amyloid.
Sequence: DAEFRHDSGYEVHHQKLVFFAQNVGSNKGAIIGLMVGGVV
Molecular Weight: 4327.9 Da
% Peak Area by HPLC: ≥95
Peptide Content: ≥ 60%
Storage condition: -20°C
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Anti-C4 binding protein Rabbit Polyclonal Antibody (Alexa Fluor® 680)
Supplier: Bioss
C4BPB is a member of a superfamily of proteins composed predominantly of tandemly arrayed short consensus repeats of approximately 60 amino acids. A single, unique beta-chain encoded by this gene assembles with seven identical alpha-chains into the predominant isoform of C4b-binding protein, a multimeric protein that controls activation of the complement cascade through the classical pathway. C4b-binding protein has a regulatory role in the coagulation system also, mediated through the beta-chain binding of protein S, a vitamin K-dependent protein that serves as a cofactor of activated protein C. The genes encoding both alpha and beta chains are located adjacent to each other on human chromosome 1 in the regulator of complement activation gene cluster. Alternative splicing gives rise to multiple transcript variants
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Fmoc-Asn(Trt)-Thr(Psi(Me,Me)pro)-OH
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Fmoc-Gln(Trt)-Thr(Psi(Me,Me)pro)-OH
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Fmoc-Trp(Boc)-Ser(Psi(Me,Me)Pro)-Oh
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Fmoc-Lys(Boc)-Thr(Psi(Me,Me)pro)-OH
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Anti-C4 binding protein Rabbit Polyclonal Antibody (Cy3®)
Supplier: Bioss
C4BPB is a member of a superfamily of proteins composed predominantly of tandemly arrayed short consensus repeats of approximately 60 amino acids. A single, unique beta-chain encoded by this gene assembles with seven identical alpha-chains into the predominant isoform of C4b-binding protein, a multimeric protein that controls activation of the complement cascade through the classical pathway. C4b-binding protein has a regulatory role in the coagulation system also, mediated through the beta-chain binding of protein S, a vitamin K-dependent protein that serves as a cofactor of activated protein C. The genes encoding both alpha and beta chains are located adjacent to each other on human chromosome 1 in the regulator of complement activation gene cluster. Alternative splicing gives rise to multiple transcript variants
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Fmoc-Gly-Ser(Psi(Me,Me)pro)-OH
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Fmoc-Glu(Otbu)-Ser(Psi(Me,Me)Pro)-Oh
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Fmoc-Asp(Otbu)-Ser(Psi(Me,Me)Pro)-Oh
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Fmoc-Phe-Thr(Psi(Me,Me)Pro)-Oh
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Fmoc-Trp(Boc)-Thr(Psi(Me,Me)Pro)-Oh
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Fmoc-Val-Ser(Psi(Me,Me)Pro)-Oh
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Fmoc-Ala-Thr(Psi(Me,Me)pro)-OH
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Fmoc-Phe-Ser(Psi(Me,Me)pro)-OH
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Fmoc-Leu-Thr(Psi(Me,Me)pro)-OH
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Fmoc-Ser(Tbu)-Thr(Psi(Me,Me)Pro)-Oh
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Fmoc-Tyr(tBu)-Ser(Psi(Me,Me)pro)-OH
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Fmoc-Gly-Thr(Psi(Me Me)Pro)-Oh
Supplier: Bachem Americas
These dipeptide building blocks containing Ser- or Thr-derived oxazolidines (pseudoprolines) proved to be versatile tools for overcoming some intrinsic problems in the field of peptide chemistry. The presence of pseudoprolines within a peptide sequence results in the disruption of β-sheet structures considered as a source of intermolecular aggregation during chain elongation, thus increasing solvation and coupling kinetics in peptide assembly. Therefore, use of pseudoprolines offer new possibilities for accessing large peptides by convergent strategies and chemoselective ligation techniques. Moreover, incorporation of a pseudoproline unit facilitates cyclization of peptides.
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Anti-G3BP1 Rabbit Polyclonal Antibody
Supplier: Proteintech
GAP SH3 Binding Protein 1 (G3BP1), also named as G3BP, is an effector of stress granule (SG) assembly. SG biology plays an important role in the pathophysiology of TDP-43 in ALS and FTLD-U. G3BP1 can be used as a marker of SG. It has been shown to function downstream of Ras and play a role in RNA metabolism, signal transduction, and proliferation. G3BP1 is a ubiquitously expressed protein that localizes to the cytoplasm in proliferating cells and to the nucleus in non-proliferating cells. G3BP1 has recently been implicated in cancer biology.
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Anti-EPHB1 Rabbit Polyclonal Antibody
Supplier: Bioss
EphB1, previously known as Elk (eph like kinase), is a receptor tyrosine kinase of the highly tissue restricted family of eph proteins. EphB1 and other ephB family members are type 1 membrane spanning proteins, comprised of immunoglobulin, fibronectin type III, and cysteine rich subdomains in the ecto domain, and the single uninterrupted cytoplasmic tyrosine kinase domain upstream of a carboxyterminal sterile alpha motif (SAM) domain. EphB family proteins bind ephrins of the B class. EphB1 is expressed predominately in developing neural structures in embryos, and in vascular epithelium of kidney, and other tissues. Upon binding to alternatively oligomerized ephrin B1, EphB1 signals regulation of cell attachment and cell to cell assembly. Members of this protein family are implicated in neuronal and vascular cell targeting.
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Anti-CATSPER4 Rabbit Polyclonal Antibody (Cy5®)
Supplier: Bioss
CatSpers (cation channel, sperm associated proteins) are ion transport proteins located on the surface of sperm cells in the principal piece of the sperm tail. CatSpers are vital to sperm motility, fertilization and cAMP-mediated calcium influx in sperm. There are four CatSper proteins in mammalian sperm, namely CatSper (or CatSper1), CatSper2, CatSper3 and CatSper4. CatSper proteins contain a single, six-transmembrane-spanning segment and exhibit the voltage-dependent Ca2+ channel four-repeat structure. CatSper proteins are believed to assemble into a heterotetrameric complex, forming an alkalinization-activated Ca2+-selective channel. Mutations in any of the genes encoding CatSper family proteins can result in male infertility. CatSper3 plays an important role in the hyperactivated motility of sperm cells, a process that is required in the preparation of sperm for fertilization.
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Anti-EPHB1 Rabbit Polyclonal Antibody (Cy3®)
Supplier: Bioss
EphB1, previously known as Elk (eph like kinase), is a receptor tyrosine kinase of the highly tissue restricted family of eph proteins. EphB1 and other ephB family members are type 1 membrane spanning proteins, comprised of immunoglobulin, fibronectin type III, and cysteine rich subdomains in the ecto domain, and the single uninterrupted cytoplasmic tyrosine kinase domain upstream of a carboxyterminal sterile alpha motif (SAM) domain. EphB family proteins bind ephrins of the B class. EphB1 is expressed predominately in developing neural structures in embryos, and in vascular epithelium of kidney, and other tissues. Upon binding to alternatively oligomerized ephrin B1, EphB1 signals regulation of cell attachment and cell to cell assembly. Members of this protein family are implicated in neuronal and vascular cell targeting.
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Anti-EPHB1 Rabbit Polyclonal Antibody (HRP (Horseradish Peroxidase))
Supplier: Bioss
EphB1, previously known as Elk (eph like kinase), is a receptor tyrosine kinase of the highly tissue restricted family of eph proteins. EphB1 and other ephB family members are type 1 membrane spanning proteins, comprised of immunoglobulin, fibronectin type III, and cysteine rich subdomains in the ecto domain, and the single uninterrupted cytoplasmic tyrosine kinase domain upstream of a carboxyterminal sterile alpha motif (SAM) domain. EphB family proteins bind ephrins of the B class. EphB1 is expressed predominately in developing neural structures in embryos, and in vascular epithelium of kidney, and other tissues. Upon binding to alternatively oligomerized ephrin B1, EphB1 signals regulation of cell attachment and cell to cell assembly. Members of this protein family are implicated in neuronal and vascular cell targeting.
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Anti-CATSPER3 Rabbit Polyclonal Antibody (HRP (Horseradish Peroxidase))
Supplier: Bioss
CatSpers (cation channel, sperm associated proteins) are ion transport proteins located on the surface of sperm cells in the principal piece of the sperm tail. CatSpers are vital to sperm motility, fertilization and cAMP-mediated calcium influx in sperm. There are four CatSper proteins in mammalian sperm, namely CatSper (or CatSper1), CatSper2, CatSper3 and CatSper4. CatSper proteins contain a single, six-transmembrane-spanning segment and exhibit the voltage-dependent Ca2+ channel four-repeat structure. CatSper proteins are believed to assemble into a heterotetrameric complex, forming an alkalinization-activated Ca2+-selective channel. Mutations in any of the genes encoding CatSper family proteins can result in male infertility. CatSper3 plays an important role in the hyperactivated motility of sperm cells, a process that is required in the preparation of sperm for fertilization.
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Anti-C4 binding protein Rabbit Polyclonal Antibody (Cy7®)
Supplier: Bioss
C4BPB is a member of a superfamily of proteins composed predominantly of tandemly arrayed short consensus repeats of approximately 60 amino acids. A single, unique beta-chain encoded by this gene assembles with seven identical alpha-chains into the predominant isoform of C4b-binding protein, a multimeric protein that controls activation of the complement cascade through the classical pathway. C4b-binding protein has a regulatory role in the coagulation system also, mediated through the beta-chain binding of protein S, a vitamin K-dependent protein that serves as a cofactor of activated protein C. The genes encoding both alpha and beta chains are located adjacent to each other on human chromosome 1 in the regulator of complement activation gene cluster. Alternative splicing gives rise to multiple transcript variants
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Anti-SCN2B Rabbit Polyclonal Antibody (Cy7®)
Supplier: Bioss
Voltage-gated sodium channels are selective ion channels that regulate the permeability of sodium ions in excitable cells. During the propagation of an action potential, sodium channels allow an influx of sodium ions, which rapidly depolarizes the cell. Na+ CP type II beta(sodium channel, voltage-gated, type II, beta), also known as SCN2B, is a 215 amino acid single-pass type I membrane protein that plays a critical role in the expression and assembly of the heterotrimeric complex of the sodium channel and interacts with Tenascin-R to influence the clustering and regulation of sodium channels at nodes of Ranvier. Expressed specifically in brain, Na+ CP type II beta contains one Ig-like C2-type (immunoglobulin-like) domain and is encoded by a gene that maps to human chromosome 11q23.3 and mouse chromosome 9 A5.2.