Recombinant Human Statherin (STATH) Protein (His-SUMO)

Name: Recombinant Human Statherin (STATH) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09188P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

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.

Product Overview

Description	Recombinant Human Statherin (STATH) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P02808
Target Symbol	STATH
Synonyms	STAT_HUMAN; STATH; Statherin; Statherin precursor ; STR
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-10His-SUMO
Target Protein Sequence	DSSEEKFLRRIGRFGYGYGPYQPVPEQPLYPQPYQPQYQQYTF
Expression Range	20-62aa
Protein Length	Full Length of Mature Protein
Mol. Weight	23.7 kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Salivary protein that stabilizes saliva supersaturated with calcium salts by inhibiting the precipitation of calcium phosphate salts. It also modulates hydroxyapatite crystal formation on the tooth surface.
Subcellular Location	Secreted.
Protein Families	Histatin/statherin family
Database References	HGNC: 11369 OMIM: 184470 KEGG: hsa:6779 STRING: 9606.ENSP00000246895 UniGene: Hs.654495
Tissue Specificity	Secreted by parotid and submandibular glands.

Gene Functions References

The total protein and statherin in the in-vivo AEP were different between eroded and non-eroded tooth surfaces of the same patient PMID: 28837608
effects of statherin on intracellular calcium level and its subsequent related molecular alterations would give us new pathogenic aspect in oral carcinogenesis PMID: 25128293
phenylalanine orientations in statherin bound to hydroxyapatite surfaces PMID: 22563672
Data show that the full characterization of the statherin peptides generated facilitates the elucidation of their novel functional roles in the oral and gastro-intestinal environment. PMID: 20731414
insight into the molecular interactions of statherin with hydroxyapatite surfaces PMID: 19678690
inhibits calcium phosphate precipitation PMID: 12060866
results suggest that a layer rich in statherin forms at the interface of saliva and air, and that the surface rheology developed is dependent upon protein interactions mediated by calcium PMID: 15769251
In conclusion, statherin induces transition to yeast of Candida albicans hyphae and may thus contribute to the oral defense against candidiasis. PMID: 19799638

FAQs

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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.