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AB96630

Mouse Serum Albumin peptide

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(1 Publication)

Mouse Serum Albumin peptide is a Synthetic blocking peptide. >70% and suitable for BL.

View Alternative Names

Alb-1, Alb1, Alb, Albumin

Key facts

Purity

>70% HPLC

Tags

Tag free

Applications

BL

applications

Biologically active

No

Accession

P07724

Animal free

No

Carrier free

No

Species

Mouse

Storage buffer

pH: 6.75 Constituents: 0.87% Sodium chloride, 0.714% HEPES, 0.0584% EDTA, 0.001% Sorbitan monolaurate, ethoxylated

storage-buffer

Reactivity data

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

Product details

- First try to dissolve a small amount of peptide in either water or buffer. The more charged residues on a peptide, the more soluble it is in aqueous solutions.
- If the peptide doesn't dissolve try an organic solvent e.g. DMSO, then dilute using water or buffer.
- Consider that any solvent used must be compatible with your assay. If a peptide does not dissolve and you need to recover it, lyophilise to remove the solvent.
- Gentle warming and sonication can effectively aid peptide solubilisation. If the solution is cloudy or has gelled the peptide may be in suspension rather than solubilised.
- Peptides containing cysteine are easily oxidised, so should be prepared in solution just prior to use.

Sequence info

[{"sequence":null,"proteinLength":null,"predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Synthetic","expressionSystem":null,"accessionNumber":"P07724","tags":[]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Specifications

Form

Liquid

Additional notes

70 - 90% by HPLC

General info

Function

Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity). Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity).

Sequence similarities

Belongs to the ALB/AFP/VDB family.

Post-translational modifications

Phosphorylated by FAM20C in the extracellular medium.

Product protocols

Target data

Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds approximately 45% of circulating calcium and magnesium in plasma (By similarity). Potentially has more than two calcium-binding sites and might additionally bind calcium in a non-specific manner (By similarity). The shared binding site between zinc and calcium at residue Asp-273 suggests a crosstalk between zinc and calcium transport in the blood (By similarity). The rank order of affinity is zinc > calcium > magnesium (By similarity). Binds to the bacterial siderophore enterobactin and inhibits enterobactin-mediated iron uptake of E.coli from ferric transferrin, and may thereby limit the utilization of iron and growth of enteric bacteria such as E.coli (By similarity). Does not prevent iron uptake by the bacterial siderophore aerobactin (By similarity).
See full target information Alb

Publications (1)

Recent publications for all applications. Explore the full list and refine your search

PloS one 12:e0187432 PubMed29091929

2017

The cathelicidin protein CRAMP is a potential atherosclerosis self-antigen in ApoE(-/-) mice.

Applications

Unspecified application

Species

Unspecified reactive species

Peter M Mihailovic,Wai Man Lio,Juliana Yano,Xiaoning Zhao,Jianchang Zhou,Kuang-Yuh Chyu,Prediman K Shah,Bojan Cercek,Paul C Dimayuga
View all publications

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