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TMEM97 Blocking Peptide (N-term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q5BJF2 |
|---|
| Gene ID | 27346 |
|---|---|
| Other Names | Transmembrane protein 97, Protein MAC30, TMEM97, MAC30 |
| Target/Specificity | The synthetic peptide sequence is selected from aa 42-56 of HUMAN TMEM97 |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | TMEM97 (HGNC:28106) |
|---|---|
| Function | Sigma-2 receptor which contributes to ameliorate dysfunctional cellular processes and slow degenerative progression by regulating cell functions including cholesterol biosynthesis/trafficking, membrane trafficking, autophagy, lipid membrane-bound protein trafficking, and receptor stabilization at the cell surface (PubMed:28559337, PubMed:19583955, PubMed:23922215, PubMed:25620095, PubMed:27378690, PubMed:34799735, PubMed:30443021, PubMed:34233061, PubMed:35970844) (Probable). Forms a ternary complex with PGRMC1 receptor and low density lipoprotein receptor/LDLR at the plasma membrane, which increases LDLR-mediated LDL cholesterol internalization (PubMed:30443021). Decreases lysosomal sterol transporter NPC1 availability to the cell, probably through NPC1- binding, hence controlling lipid transport, including cholesterol and LBPA, outside of late endosome/lysosome (PubMed:19583955, PubMed:27378690). Binds regio- and stereoselective ligand 20(S)- hydroxycholesterol (20(S)-OHC) which enhances TMEM97-NPC1 interaction and decreases TMEM97-PGRMC1 and TMEM97-TSPO interactions, thereby linking OHC binding to cholesterol homeostasis (PubMed:34799735, PubMed:37047353). Also able to bind cholesterol (By similarity). Binds histatin 1 (Hst 1)/HN1 salivary peptide at the ER membrane, which is critical for increasing mitochondria-ER contacts and stimulating Hst1 wound healing properties (PubMed:34233061, PubMed:35970844). May alter the activity of some cytochrome P450 proteins (PubMed:22292588). Although shows homologies with sterol isomerases (EXPERA domain), not able to catalyze sterol isomerization (Probable) (PubMed:34880501). However, may act as sensors of these molecules (Probable) (PubMed:34880501). Acts as a quality control factor in the ER, promoting the proteolytic degradation of nonproductive and extramitochondrial precursor proteins in the ER membrane thus removing them from the ER surface (By similarity). |
| Cellular Location | Rough endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi- pass membrane protein. Note=Localized at cell membrane and in lysosomes in sterol-depleted cells when expression of endogenous TMEM97 is stimulated (PubMed:19583955). Localized at cell membrane, probably in lipid rafts, in serum-starved conditions (PubMed:30443021) |
| Tissue Location | Widely expressed in normal tissues. Expressed in pancreatic, renal, breast, colon, ovarian surface epithelial (OSE) cells. Highly expressed in various proliferating cancer cells (PubMed:23922215). |
Research Areas
Citations (0)
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Application Protocols
Provided below are standard protocols that you may find useful for product applications.
Background
Plays a role as a regulator of cellular cholesterol homeostasis.
References
Murphy M.,et al.Cell Growth Differ. 4:715-722(1993).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Kayed H.,et al.Histol. Histopathol. 19:1021-1031(2004).
Wilcox C.B.,et al.BMC Cancer 7:223-223(2007).
Bartz F.,et al.Cell Metab. 10:63-75(2009).
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$ 277.78
Cat# BP21745a
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