Recombinant Human Stomatin Protein (Fc Tag)

Name: Recombinant Human Stomatin Protein (Fc Tag)
Brand: Beta LifeScience
SKU: BLPSN-4367
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag	Fc
Host Species	Human
Accession	AAH10703.1
Synonym	BND7, EPB7, EPB72
Description	A DNA sequence encoding the human STOM (AAH10703.1) (Lys55-Gly288) was expressed with the Fc region of mouse IgG1 at the C-terminus.
Source	HEK293
Predicted N Terminal	Lys 55
AA Sequence	Lys55-Gly288
Molecular Weight	The recombinant human STOM consists 468 a.a. and predicts a molecular mass of 52.1 kDa.
Purity	>95% as determined by SDS-PAGE.
Endotoxin	< 1.0 EU per μg protein as determined by the LAL method.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.4..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Regulates ion channel activity and transmembrane ion transport. Regulates ASIC2 and ASIC3 channel activity.
Subcellular Location	Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Cell membrane; Lipid-anchor; Cytoplasmic side. Membrane raft. Melanosome. Cytoplasmic vesicle.
Protein Families	Band 7/mec-2 family
Database References	HGNC: 3383 OMIM: 133090 KEGG: hsa:2040 STRING: 9606.ENSP00000286713 UniGene: Hs.253903
Tissue Specificity	Detected in erythrocytes (at protein level). Widely expressed.

Gene Functions References

we show that stomatin modulates the transport activity of AE1 through a direct protein-protein interaction. PMID: 28387307
These results may suggest that stomatin is a new prognostic indicator for HER2-positive breast cancer PMID: 27577936
FRAP analyses indicate that the stomatin C-terminus is the dominant entity for lateral mobility and binding site for the cortical actin cytoskeleton PMID: 28575093
This study showed that cells expressing more stomatin or exposed to exogenous stomatin are more prone to undergoing cell fusion; during osteoclastogenesis, depletion of stomatin inhibited cell fusion but had little effect on tartrate-resistant acid phosphatase production. PMID: 27663861
Authors took a proteomic approach to identify stomatin, a member of the integral proteins of lipid rafts, as a cellular protein interacting with hepatitis C virus NS5B. PMID: 25262680
Stomatin protein expression is down-regulated in 80% of non-small cell lung cancer samples. PMID: 24533441
upregulation of stomatin by hypoxia and dex may enhance the barrier function of alveolar epithelia and mediate the adaptive role of glucocorticoid to hypoxia PMID: 23672602
Stomatin interacts with GLUT1/SLC2A1, band 3/SLC4A1, and aquaporin-1 in human erythrocyte membrane domains PMID: 23219802
[review] Stomatin family member STOM is oligomeric; it localizes mostly to membrane domains and has been shown to modulate ion channel activity. PMID: 21501885
The study indicates that stomatin, sorcin, and synexin are echinophilic membrane components that mainly locate outside GM1 rafts in the human erythrocyte membrane. PMID: 20858460
This study demonstrated the existence of alpha-granular lipid rafts and suggests an important role for stomatin in the organization and function of alpha granules. PMID: 12130500
stomatin is localized to detergent-insoluble domains of neutrophil granule membranes PMID: 12429719
in stomatocytosis there is no significant abnormality in stomatin gene sequence instead, deficiency of stomatin from red cells appears to be due to a loss of stomatin from these red cells on maturation in the bone marrow and in the circulation. PMID: 12750157
study of strongly homologous stomatin-like genes in prokaryotes reveals a close connection with a gene coding for a hydrophobic protein with a probable serine protease motif; stomatin could be a partner protein for a membrane-bound proteolytic process PMID: 15121101
stomatin binds to and alters the gating of acid-sensing ion channels PMID: 15471860
A small C-terminal region of stomatin that is largely hydrophobic (residues 264-272) is crucial for oligomerization, whereas the N-terminal domain (residues 1-20) and the last 12 C-terminal amino acids (residues 276-287) are not essential. PMID: 16766530
The stomatin-actin association is important in maintaining the structure and in modulating the function of stomatin-containing membrane rafts in red cells. PMID: 17961506
Data indicate that a stomatin-specific, raft-based process is involved in storage-associated vesiculation. PMID: 18067507
Stomatin-like protein-1 interacts with stomatin and is targeted to late endosomes PMID: 19696025
Stomatin is a member of an ancient protein family that has extremely well conserved homologues in all three domains of life. PMID: 18267007

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.