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AB199580

Recombinant Human Histatin-3 protein (Tagged)

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Recombinant Human Histatin-3 protein (Tagged) is a Human Full Length protein, in the 20 to 51 aa range, expressed in Escherichia coli, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.

View Alternative Names

HIS2, HTN3, Histatin-3, Basic histidine-rich protein, Histatin 3, Histidine-rich protein 3, PB, Hst, Hst 3

Key facts

Purity

>95% SDS-PAGE

Endotoxin level

< 1 EU/µg

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE, HPLC

applications

Biologically active

No

Accession

P15516

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 7.4 Constituents: 1.16% Sodium chloride, 0.32% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "HPLC": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MSPILGYWKIKGLVQPTRLLLEYLEEKYEEHLYERDEGDKWRNKKFELGLEFPNLPYYIDGDVKLTQSMAIIRYIADKHNMLGGCPKERAEISMLEGAVLDIRYGVSRIAYSKDFETLKVDFLSKLPEMLKMFEDRLCHKTYLNGDHVTHPDFMLYDALDVVLYMDPMCLDAFPKLVCFKKRIEAIPQIDKYLKSSKYIAWPLQGWQATFGGGDHPPKSDLVPRGSENLYFQGHMDSHAKRHHGYKRKFHEKHHSHRGYRSNYLYDN","proteinLength":"Full Length","predictedMolecularWeight":"31 kDa","actualMolecularWeight":null,"aminoAcidEnd":51,"aminoAcidStart":20,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P15516","tags":[]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
Avoid freeze / thaw cycle
False

Specifications

Form

Liquid

Additional notes

ab199580 is greater than 95% pure as determined by SEC-HPLC and reducing SDS-PAGE.

General info

Function

Histatins are cationic and histidine-rich peptides mainly found in the saliva of higher primates (PubMed : 3286634). They are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). Hsts can be divided into two major groups according to their biological functions : antimicrobial Hsts (e.g. Hst 5/HTN3) and cell-activating Hsts (e.g. Hst 1/HTN1, Hst 2/HTN1 and Hst 3/HTN3) (PubMed : 32225006).. Histatin-3. Histatin 3 (Hst 3) is mostly involved in cell migration and wound healing in the oral cavity (PubMed : 18650243). Also stimulates cell proliferation after binding to heat shock protein HSC70, which enhances HSC70-CDKN1B complex formation and subsequent ubiquitination during G1/S transition (PubMed : 26775844). Also displays antifungal activity against pathogenic yeast Candida albicans, however with less effectiveness than Hst 5 (PubMed : 11083804, PubMed : 3286634).. His3-(20-43)-peptide. Histatin 5 (Hst 5), a fragment of Hst 3, is the major histatin exhibiting antifungal and antibacterial activities (PubMed : 10066791, PubMed : 11083804, PubMed : 11179305, PubMed : 11717389, PubMed : 12939362, PubMed : 15485849, PubMed : 2372245, PubMed : 8945538). It is effective against pathogenic yeast C. albicans, C. neoformans, C. glabrata and S. cerevisiae as well as ESKAPE bacterial pathogens (PubMed : 18974864, PubMed : 23613860, PubMed : 2372245, PubMed : 28261570, PubMed : 8945538). Secreted Hst 5 mediates a multi-step intracellular mechanism of action against the pathogen. Depending on peptide concentration and pathogen, uptake across the membrane can occur through transporters, direct interaction with plasma membrane and/or receptor-mediated endocytosis (PubMed : 18974864, PubMed : 20487276, PubMed : 28261570). Binds C. albicans cell wall proteins SSA1 and SSA2 and glycans in an energy-independent manner, then is taken up by the cells through fungal polyamine transporters DUR3 and DUR31 in an energy-dependent manner (PubMed : 12761219, PubMed : 20487276, PubMed : 22033918, PubMed : 23613860). Internalized Hst5 is then targeted to the energized mitochondrion to induce reactive oxygen species (ROS) formation and subsequent release of intracellular non-lytic ATP which ultimately leads to fungal cell death (PubMed : 10066791, PubMed : 11083804, PubMed : 11717389). In addition, inhibits C. albicans TRK1 potassium-transporter which causes exudation of intracellular K(+), generating an osmotic imbalance leading to delayed membrane lysis and cell death (PubMed : 15485849). Also acts as a potent inhibitor of bacterial proteases such as Lys-gingipain and Arg-gingipain (rgpB) from P. gingivalis as well as human metalloproteases MMP2 and MMP9 (PubMed : 11179305). The binding of metals such as zinc, copper or nickel with Hst 5 results in the protection of the enamel and antimicrobial activities such as the inhibition of microbial growth by decreasing the metal concentration, the formation of ROS commonly associated with redox-active metals, the induction of membrane disruption mediated by zinc binding (PubMed : 19846304, PubMed : 28261570, PubMed : 28763199, PubMed : 32751915). Also involved in coating oral surfaces in the form of a salivary film which reduces colonization by C. albicans on epithelial cell surfaces (PubMed : 26379655). Secreted Hst 5 can also internalize mammalian epithelial cells and target the mitochondria although it does not exert cytotoxic effects in these cells (PubMed : 32225006). In contrast with Hst 3, not able to promote wound healing in mammalian host cells (PubMed : 18650243).

Sequence similarities

Belongs to the histatin/statherin family.

Post-translational modifications

24 proteolytic products are found in saliva.

Product protocols

Target data

Histatins are cationic and histidine-rich peptides mainly found in the saliva of higher primates (PubMed : 3286634). They are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). Hsts can be divided into two major groups according to their biological functions : antimicrobial Hsts (e.g. Hst 5/HTN3) and cell-activating Hsts (e.g. Hst 1/HTN1, Hst 2/HTN1 and Hst 3/HTN3) (PubMed : 32225006).. Histatin-3. Histatin 3 (Hst 3) is mostly involved in cell migration and wound healing in the oral cavity (PubMed : 18650243). Also stimulates cell proliferation after binding to heat shock protein HSC70, which enhances HSC70-CDKN1B complex formation and subsequent ubiquitination during G1/S transition (PubMed : 26775844). Also displays antifungal activity against pathogenic yeast Candida albicans, however with less effectiveness than Hst 5 (PubMed : 11083804, PubMed : 3286634).. His3-(20-43)-peptide. Histatin 5 (Hst 5), a fragment of Hst 3, is the major histatin exhibiting antifungal and antibacterial activities (PubMed : 10066791, PubMed : 11083804, PubMed : 11179305, PubMed : 11717389, PubMed : 12939362, PubMed : 15485849, PubMed : 2372245, PubMed : 8945538). It is effective against pathogenic yeast C. albicans, C. neoformans, C. glabrata and S. cerevisiae as well as ESKAPE bacterial pathogens (PubMed : 18974864, PubMed : 23613860, PubMed : 2372245, PubMed : 28261570, PubMed : 8945538). Secreted Hst 5 mediates a multi-step intracellular mechanism of action against the pathogen. Depending on peptide concentration and pathogen, uptake across the membrane can occur through transporters, direct interaction with plasma membrane and/or receptor-mediated endocytosis (PubMed : 18974864, PubMed : 20487276, PubMed : 28261570). Binds C. albicans cell wall proteins SSA1 and SSA2 and glycans in an energy-independent manner, then is taken up by the cells through fungal polyamine transporters DUR3 and DUR31 in an energy-dependent manner (PubMed : 12761219, PubMed : 20487276, PubMed : 22033918, PubMed : 23613860). Internalized Hst5 is then targeted to the energized mitochondrion to induce reactive oxygen species (ROS) formation and subsequent release of intracellular non-lytic ATP which ultimately leads to fungal cell death (PubMed : 10066791, PubMed : 11083804, PubMed : 11717389). In addition, inhibits C. albicans TRK1 potassium-transporter which causes exudation of intracellular K(+), generating an osmotic imbalance leading to delayed membrane lysis and cell death (PubMed : 15485849). Also acts as a potent inhibitor of bacterial proteases such as Lys-gingipain and Arg-gingipain (rgpB) from P. gingivalis as well as human metalloproteases MMP2 and MMP9 (PubMed : 11179305). The binding of metals such as zinc, copper or nickel with Hst 5 results in the protection of the enamel and antimicrobial activities such as the inhibition of microbial growth by decreasing the metal concentration, the formation of ROS commonly associated with redox-active metals, the induction of membrane disruption mediated by zinc binding (PubMed : 19846304, PubMed : 28261570, PubMed : 28763199, PubMed : 32751915). Also involved in coating oral surfaces in the form of a salivary film which reduces colonization by C. albicans on epithelial cell surfaces (PubMed : 26379655). Secreted Hst 5 can also internalize mammalian epithelial cells and target the mitochondria although it does not exert cytotoxic effects in these cells (PubMed : 32225006). In contrast with Hst 3, not able to promote wound healing in mammalian host cells (PubMed : 18650243).
See full target information HTN3

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