TMEM97 Antibody (N-term)
Purified Rabbit Polyclonal Antibody (Pab)
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Application ![]()
| WB, E |
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Primary Accession | Q5BJF2 |
Reactivity | Human, Rat, Mouse |
Host | Rabbit |
Clonality | polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 20848 Da |
Gene ID | 27346 |
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Other Names | Transmembrane protein 97, Protein MAC30, TMEM97, MAC30 |
Target/Specificity | This TMEM97 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 22-56 amino acids from the N-terminal region of human TMEM97. |
Dilution | WB~~1:1000 E~~Use at an assay dependent concentration. |
Format | Purified polyclonal antibody supplied in PBS with 0.05% (V/V) Proclin 300. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | TMEM97 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | TMEM97 (HGNC:28106) |
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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 (Probable) (PubMed:19583955, PubMed:23922215, PubMed:25620095, PubMed:27378690, PubMed:28559337, PubMed:30443021, PubMed:34233061, PubMed:34799735, PubMed:35970844). 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
For Research Use Only. Not For Use In Diagnostic Procedures.
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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