CBLN1 Rabbit pAb
CBLN1 Rabbit pAb
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- 实验流程
- 背景知识
Application
| IHC-P, IHC-F, IF |
|---|---|
| Primary Accession | P23435 |
| Reactivity | Rat |
| Predicted | Human, Mouse, Pig, Rabbit |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 21097 Da |
| Physical State | Liquid |
| Immunogen | KLH conjugated synthetic peptide derived from human CBLN1 |
| Epitope Specificity | 51-150/193 |
| Isotype | IgG |
| Purity | affinity purified by Protein A |
| Buffer | 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol. |
| SUBCELLULAR LOCATION | Secreted. Membrane. Cell junction, synapse. |
| SIMILARITY | Contains 1 C1q domain. |
| SUBUNIT | Homohexamer; disulfide-linked homotrimers. The trimers are assembled via the globular C1q domains. The trimers associate via N-terminal cysteine residues to form disulfide-linked hexamers. Probably forms a heteomeric complex with CBLN3. May interact with CBLN2 and CBLN4 |
| Post-translational modifications | The proteolytic processing to yield cerebellin seems to occur either prior to the secretion by presynaptic neurons and subsequent oligomerization or in some other location after release of the mature protein. |
| Important Note | This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications. |
| Background Descriptions | Cerebellin (CER), which was originally isolated from rat cerebellum, is a hexadecapeptide derived from a larger precursor Cerebellin 1, also designated precerebellin 1 or Cbln1. Four propeptides, Cerebellin 1, Cerebellin 2 (Cbln2), Cerebellin 3 (Cbln3), and Cerebellin 4 (Cbln4), comprise the precerebellin subfamily within the C1q protein family. Cerebellin family members act as transneuronal regulators of synapse development and synaptic plasticity in various brain regions. CER and it metabolite des-Ser1-cerebellin are also expressed in several extra-cerebellar tissues, including adrenal gland. Cerebellin 1, 2 and 3 assemble into homomeric and heteromeric complexes, thereby influencing each other’s degradation and secretion. Cerebellin 3 is not able to form homomeric complexes, and can only be secreted upon forming a heteromeric complex with Cerebellin 1. Decreased concentrations of CER has been found in the brain of patients with olivopontocerebellar atrophy (OPCA) and Shy-Drager syndrome, suggesting a role for CER in the pathology of these diseases. |
| Gene ID | 869 |
|---|---|
| Other Names | Cerebellin-1, Precerebellin, Cerebellin, CER, [des-Ser1]-cerebellin, CBLN1 |
| Target/Specificity | In the Purkinje cells postsynaptic structures. In the cerebellum, cerebellin is much less abundant than [des-Ser1]-cerebellin. |
| Dilution | IHC-P=1:100-500,IHC-F=1:100-500,IF=1:100-500 |
| Storage | Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C. |
| Name | CBLN1 |
|---|---|
| Function | Required for synapse integrity and synaptic plasticity. During cerebellar synapse formation, essential for the matching and maintenance of pre- and post-synaptic elements at parallel fiber- Purkinje cell synapses, the establishment of the proper pattern of climbing fiber-Purkinje cell innervation, and induction of long-term depression at parallel fiber-Purkinje cell synapses. Plays a role as a synaptic organizer that acts bidirectionally on both pre- and post- synaptic components. On the one hand induces accumulation of synaptic vesicles in the pre-synaptic part by binding with NRXN1 and in other hand induces clustering of GRID2 and its associated proteins at the post-synaptic site through association of GRID2. NRXN1-CBLN1-GRID2 complex directly induces parallel fiber protrusions that encapsulate spines of Purkinje cells leading to accumulation of GRID2 and synaptic vesicles. Required for CBLN3 export from the endoplasmic reticulum and secretion (By similarity). NRXN1-CBLN1-GRID2 complex mediates the D- Serine-dependent long term depression signals and AMPA receptor endocytosis (PubMed:27418511). Essential for long-term maintenance but not establishment of excitatory synapses (By similarity). Inhibits the formation and function of inhibitory GABAergic synapses in cerebellar Purkinje cells (By similarity). |
| Cellular Location | Secreted {ECO:0000250|UniProtKB:Q9R171}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9R171} |
| Tissue Location | In the Purkinje cells postsynaptic structures. In the cerebellum, cerebellin is much less abundant than [des-Ser1]- cerebellin |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
Cerebellin (CER), which was originally isolated from rat cerebellum, is a hexadecapeptide derived from a larger precursor Cerebellin 1, also designated precerebellin 1 or Cbln1. Four propeptides, Cerebellin 1, Cerebellin 2 (Cbln2), Cerebellin 3 (Cbln3), and Cerebellin 4 (Cbln4), comprise the precerebellin subfamily within the C1q protein family. Cerebellin family members act as transneuronal regulators of synapse development and synaptic plasticity in various brain regions. CER and it metabolite des-Ser1-cerebellin are also expressed in several extra-cerebellar tissues, including adrenal gland. Cerebellin 1, 2 and 3 assemble into homomeric and heteromeric complexes, thereby influencing each other’s degradation and secretion. Cerebellin 3 is not able to form homomeric complexes, and can only be secreted upon forming a heteromeric complex with Cerebellin 1. Decreased concentrations of CER has been found in the brain of patients with olivopontocerebellar atrophy (OPCA) and Shy-Drager syndrome, suggesting a role for CER in the pathology of these diseases.
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