Abcam, ab228868, Anti-SIL1 antibody

Size: 100µL
Rabbit Polyclonal SIL1 antibody. Suitable for WB, IHC-P and reacts with Rat, Human samples. Cited in 3 publications. Immunogen corresponding to Recombinant Fragment Protein within Human SIL1.
Key facts
Host species:Rabbit,
Clonality:Polyclonal,
Isotype:IgG,
Carrier free:No,
Reacts with:Rat, Human,
Applications:IHC-P, WBSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:Recombinant Fragment Protein within Human SIL1. The exact immunogen used to generate this antibody is proprietary information.Q9H173

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Immunogen, Storage buffer-pH: 7Preservative: 0.01% Thimerosal (merthiolate)Constituents: 20% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine, Shipped at conditions-Blue Ice, Appropriate short-term storage duration-1-2 weeks, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
The SIL1 protein known also as nucleotide exchange factor SIL1 or BAP plays a mechanical role as an endoplasmic reticulum (ER)-localized nucleotide exchange factor for BiP a heat shock protein. SIL1 has a molecular mass of approximately 53 kDa. The expression of SIL1 occurs mainly in tissues with high secretory demand such as the pancreas and liver. It exists prominently within the lumen of the ER where it stabilizes protein folding by facilitating nucleotide exchange on BiP.
Biological function summary
SIL1 operates as a critical component for ER homeostasis and proteostasis. It assists the chaperone function of BiP by promoting ADP/ATP exchange which is an essential step in the protein folding cycle. SIL1 forms part of a complex network of proteins within the ER that regulate protein biosynthesis folding and degradation. Its interactive network ensures efficient ER functioning affecting the maturation and stability of secretory and membrane proteins.
Pathways
SIL1 interacts within both the unfolded protein response (UPR) and ER-associated degradation (ERAD) pathways. In the UPR SIL1's role in BiP activity ensures proper folding of nascent polypeptides reducing ER stress. In ERAD SIL1's actions facilitate misfolded protein processing and clearance. SIL1 is closely related to other chaperones and co-chaperones like GRP78 with whom it collaboratively maintains ER function under stress conditions ensuring cellular homeostasis.
SIL1 mutations associate with Marinesco-Sjögren syndrome a rare autosomal recessive disorder. The syndrome results from disrupted protein homeostasis in the ER leading to multisystem clinical symptoms such as muscle weakness and cataracts. SIL1 also connects to neurodegenerative diseases often characterized by ER stress and faulty proteostasis implicating proteins such as BiP whose impairment also results from SIL1 malfunctions. Understanding these connections is essential for identifying potential therapeutic targets for these disorders.