|Positive IHC detected in||human heart tissue|
Note: suggested antigen retrieval with TE buffer pH 9.0; (*) Alternatively, antigen retrieval may be performed with citrate buffer pH 6.0
|Positive IF detected in||PC-3 cells|
|Immunohistochemistry (IHC)||IHC : 1:50-1:500|
|Immunofluorescence (IF)||IF : 1:20-1:200|
|Sample-dependent, check data in validation data gallery|
18395-1-AP targets SLN in WB, IHC, IF,ELISA applications and shows reactivity with human, mouse, rat samples.
|Tested Reactivity||human, mouse, rat|
|Cited Reactivity||mouse, squirrel|
|Host / Isotype||Rabbit / IgG|
|Immunogen||SLN fusion protein Ag13176|
|Calculated molecular weight||31 aa, 4 kDa|
|Observed molecular weight||4 kDa, 8-10kDa|
|GenBank accession number||BC005261|
|Gene ID (NCBI)||6588|
|Purification Method||Antigen affinity purification|
|Storage Buffer||PBS with 0.02% sodium azide and 50% glycerol pH 7.3.|
|Storage Conditions||Store at -20°C. Stable for one year after shipment. Aliquoting is unnecessary for -20oC storage.|
SLN, also named as Sarcolipin, belongs to the sarcolipin family. It is associated with calcium ATPase SERCA1. It inhibits SERCA pumps. SLN, a key regulator of cardiac sarco(endo)plasmic reticulum (SR) Ca(2+) ATPase, is predominantly expressed in atria and mediates β-adrenergic responses. SLN can self-assembly to dimer and oligomer for playing importantphysiological function. This antibody recognize the 4kd band in Human heart and skeletal muscle. (PMID: 28241400, PMID: 21737843)
J Physiol Biochem
Sarcolipin expression is repressed by endoplasmic reticulum stress in C2C12 myotubes.
A Temporal Examination of Cytoplasmic Ca2 + Levels, Sarcoplasmic Reticulum Ca2 + Levels, and Ca2 + -Handling-Related Proteins in Different Skeletal Muscles of Hibernating Daurian Ground Squirrels.
Exp Cell Res
Effect of sarcolipin-mediated cell transdifferentiation in sarcopenia-associated skeletal muscle fibrosis.
ChREBP-β regulates thermogenesis in brown adipose tissue.
J Biol Chem
Interactions between small ankyrin 1 and sarcolipin coordinately regulate activity of the sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA1).
Ca(2+) permeation and/or binding to CaV1.1 fine-tunes skeletal muscle Ca(2+) signaling to sustain muscle function.