Human Recombinant ASIC1-VLP protein, His & Strep Tag (V2LY-0526-LY2186)

Name: Human Recombinant ASIC1-VLP protein, His & Strep Tag
SKU: V2LY-0526-LY2186
Rating: 5 (1 reviews)

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Datasheet

SDS

Request for COA

Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Expressed Host

HEK293 Cells

Protein Species

Human

Tag

His & Strep Tag

Protein Construction

This product is Human Recombinant ASIC1-VLP protein, His & Strep Tag consist of Amino Acid: 1-528 and predicts a molecular mass of 55.96 kDa.

Molecule Mass

55.96 kDa

Sequence

Amino Acid: 1-528

Species

Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Endotoxin

Please contact us for more information.

Format

Liquid

Buffer

Tris, NaCl, Glutathione, EDTA, DTT, PMSF, Glycerol

Preservative

None

Storage

Samples are stable for up to twelve months from date of receipt at -70°C. Store it under sterile conditions at -70°C or lower. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

More Infomation

Target

Full Name

Acid Sensing Ion Channel Subunit 1

Function

Isoform 2 and isoform 3 function as proton-gated sodium channels; they are activated by a drop of the extracellular pH and then become rapidly desensitized. The channel generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Isoform 2 can also transport potassium, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. Isoform 3 can also transport calcium ions. Mediates glutamate-independent Ca2+ entry into neurons upon acidosis. This Ca2+ overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties. Functions as a postsynaptic proton receptor that influences intracellular Ca2+ concentration and calmodulin-dependent protein kinase II phosphorylation and thereby the density of dendritic spines. Modulates activity in the circuits underlying innate fear.
Isoform 1 does not display proton-gated cation channel activity.

Biological Process

Associative learning Source: Ensembl
Behavioral fear response Source: Ensembl
Calcium ion transmembrane transport Source: Ensembl
Cellular response to pH Source: UniProtKB
Ion transmembrane transport Source: Reactome
Memory Source: Ensembl
Negative regulation of neurotransmitter secretion Source: Ensembl
Protein homotrimerization Source: UniProtKB
Regulation of membrane potential Source: Ensembl
Response to acidic pH Source: Ensembl
Response to amphetamine Source: Ensembl
Response to pH Source: ProtInc
Sensory perception of sour taste Source: UniProtKB
Signal transduction Source: ProtInc
Sodium ion transmembrane transport Source: UniProtKB
Sodium ion transport Source: UniProtKB

Cellular Location

Cell membrane. Localizes in synaptosomes at dendritic synapses of neurons. Colocalizes with DLG4 (By similarity).

Topology

Cytoplasmic: 1-45 aa
Helical: 46-69 aa
Extracellular: 70-427 aa
Discontinuously helical: 428-454 aa
Cytoplasmic: 455-528 aa

PTM

Phosphorylation by PKA regulates interaction with PRKCABP and subcellular location. Phosphorylation by PKC may regulate the channel.

Yang, Y. L., & Lai, T. W. (2021). Citric acid in drug formulations causes pain by potentiating acid-sensing ion channel 1. Journal of Neuroscience, 41(21), 4596-4606.

Liu, Y., Ma, J., DesJarlais, R. L., Hagan, R., Rech, J., Lin, D., ... & Maher, M. (2021). Molecular mechanism and structural basis of small-molecule modulation of the gating of acid-sensing ion channel 1. Communications biology, 4(1), 1-15.

Cristofori-Armstrong, B., Saez, N. J., Chassagnon, I. R., King, G. F., & Rash, L. D. (2019). The modulation of acid-sensing ion channel 1 by PcTx1 is pH-, subtype-and species-dependent: Importance of interactions at the channel subunit interface and potential for engineering selective analogues. Biochemical pharmacology, 163, 381-390.

Sun, D., Yu, Y., Xue, X., Pan, M., Wen, M., Li, S., ... & Tian, C. (2018). Cryo-EM structure of the ASIC1a–mambalgin-1 complex reveals that the peptide toxin mambalgin-1 inhibits acid-sensing ion channels through an unusual allosteric effect. Cell discovery, 4(1), 1-11.

Gregory, N. S., Gautam, M., Benson, C. J., & Sluka, K. A. (2018). Acid sensing ion channel 1a (ASIC1a) mediates activity-induced pain by modulation of heteromeric ASIC channel kinetics. Neuroscience, 386, 166-174.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
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Isotype control

For research use only. Not intended for any clinical use.

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