Human JPH1 protein (Recombinant) (N-His) (STJP006032)

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STJP006032
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Short Description :Recombinant-Human JPH1-N-His protein was developed from e.coli for the region N-His. For use in research applications.
Applications:ELISA/Immunogen/SDS-PAGE/WB
Host:E.coli
Note:STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.
Dilution Range:Reconstitute in sterile water for a stock solution. A copy of datasheet will be provided with the products, please refer to it for details.
Formulation:Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Storage Instruction:Use a manual defrost freezer and avoid repeated freeze thaw cycles. Store at 2 to 8°C for frequent use. Store at-20 to-80°C for twelve months from the date of receipt.
Gene Symbol:JPH1
Gene ID:56704
Uniprot ID:JPH1_HUMAN
Immunogen:Homo sapiens (Human)
Immunogen Region:Met1-Ala201
Function Junctophilins contribute to the formation of junctional membrane complexes (JMCs) which link the plasma membrane with the endoplasmic or sarcoplasmic reticulum in excitable cells. Provides a structural foundation for functional cross-talk between the cell surface and intracellular calcium release channels. JPH1 contributes to the construction of the skeletal muscle triad by linking the t-tubule (transverse-tubule) and SR (sarcoplasmic reticulum) membranes.
Protein Name Junctophilin-1
Jp-1
Junctophilin Type 1
Database Links
Cellular Localisation Cell Membrane
Peripheral Membrane Protein
Endoplasmic Reticulum Membrane
Single-Pass Type Iv Membrane Protein
Sarcoplasmic Reticulum Membrane
Localized Predominantly On The Plasma Membrane
The Transmembrane Domain Is Anchored In Endoplasmic/Sarcoplasmic Reticulum Membrane
While The N-Terminal Part Associates With The Plasma Membrane
In Skeletal Muscle Cells
It Is Predominantly Localized At The Junction Of The A And I Bands
Alternative Protein Names Junctophilin-1 protein
Jp-1 protein
Junctophilin Type 1 protein
JPH1 protein
JP1 protein

Information sourced from Uniprot.org