ChemicalBook--->CAS DataBase List--->127637-03-0

127637-03-0

127637-03-0 Structure

127637-03-0 Structure
IdentificationBack Directory
[Name]

H-LYS-PHE-HIS-GLU-LYS-HIS-HIS-SER-HIS-ARG-GLY-TYR-OH
[CAS]

127637-03-0
[Synonyms]

HIP
AAG2
SNC6
RPL29
REG3A
HUMRPL29
MGC88589
HISTATIN-8
REG-3-alpha
KFHEKHHSHRGY
Reg III-alpha
inyl-glycyl-tyrosine
L-F-H-E-K-H-H-S-H-R-G-Y
Pancreatitis-associated protein 1
HEMAGGLUTINATION-INHIBITING PEPTIDE
Anti-REG3A antibody produced in rabbit
Anti-RPL29 antibody produced in rabbit
HEMAGGLUTINATION-INHIBITING PEPTIDE HIP
Hedgehog-interacting Protein from mouse
Regenerating islet-derived protein 3-alpha
Regenerating islet-derived protein III-alpha
HIP, HeMagglutination-Inhibiting Peptide (HIP)
ANTI-REG3A (N-TERM) antibody produced in rabbit
LYS-PHE-HIS-GLU-LYS-HIS-HIS-SER-HIS-ARG-GLY-TYR
H-LYS-PHE-HIS-GLU-LYS-HIS-HIS-SER-HIS-ARG-GLY-TYR-OH
HISTATIN-8 [HEMAGGLUTINATION-INHIBITING PEPTIDE (HIP)]
Histatin-8 HIP, HeMagglutination-Inhibiting Peptide (HIP)
lysyl-phenylalanyl-histidyl-glutamyl-lysyl-histidyl-histidyl-seryl-histidyl-arg
lysyl-phenylalanyl-histidyl-glutamyl-lysyl-histidyl-histidyl-seryl-histidyl-arginyl-glycyl-tyrosine
L-Tyrosine, L-lysyl-L-phenylalanyl-L-histidyl-L-α-glutamyl-L-lysyl-L-histidyl-L-histidyl-L-seryl-L-histidyl-L-arginylglycyl-
[Molecular Formula]

C70H99N25O17
[MDL Number]

MFCD00214315
[MOL File]

127637-03-0.mol
[Molecular Weight]

1562.69
Chemical PropertiesBack Directory
[storage temp. ]

−20°C
[form ]

buffered aqueous solution
[biological source]

rabbit
Safety DataBack Directory
[WGK Germany ]

3
Hazard InformationBack Directory
[Uses]

Histatin-8 is a part of the Histatin-3 central sequence and is known as hemagglutination-inhibiting peptide. Histatin-8 is a potent anti-fungal peptide. Histatin-8 shows antimicrobial activity against yeast strains. Histatin-8 can be used for oral thrush research[1][2].
[References]

[1] Neshani A, et al. Antimicrobial peptides as a promising treatment option against Acinetobacter baumannii infections. Microb Pathog. 2020 Sep;146:104238. DOI:10.1016/j.micpath.2020.104238
[2] Matheson S M G, et al. Investigating the Effects of Hydrophobicity and Charge on the Therapeutic Ability of the Antimicrobial Histatin 8 Peptide for Potential Use in Oral Applications. International Journal of Biology, 2013.
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