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S100A13 Protein, Mouse (His)

Cat. No.: HY-P76583
COA Handling Instructions

S100A13 Protein, acting as a homodimer, facilitates the export of signal peptide-lacking proteins through an alternative pathway, binding two calcium ions and one copper ion per subunit. It is crucial for the copper-dependent stress-induced export of IL1A and FGF1, with the calcium-free form binding to phosphatidylserine-containing lipid vesicles. S100A13 is part of a copper-dependent multiprotein complex, interacting with FGF1, SYT1, and IL1A. S100A13 Protein, Mouse (His) is the recombinant mouse-derived S100A13 protein, expressed by E. coli , with N-His labeled tag. The total length of S100A13 Protein, Mouse (His) is 98 a.a., with molecular weight of ~15 kDa.

For research use only. We do not sell to patients.

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Description

S100A13 Protein, acting as a homodimer, facilitates the export of signal peptide-lacking proteins through an alternative pathway, binding two calcium ions and one copper ion per subunit. It is crucial for the copper-dependent stress-induced export of IL1A and FGF1, with the calcium-free form binding to phosphatidylserine-containing lipid vesicles. S100A13 is part of a copper-dependent multiprotein complex, interacting with FGF1, SYT1, and IL1A. S100A13 Protein, Mouse (His) is the recombinant mouse-derived S100A13 protein, expressed by E. coli , with N-His labeled tag. The total length of S100A13 Protein, Mouse (His) is 98 a.a., with molecular weight of ~15 kDa.

Background

The S100A13 protein plays a crucial role in the export of proteins that lack a signal peptide and are secreted through an alternative pathway. It has the ability to bind two calcium ions per subunit and one copper ion, with the binding of the latter not interfering with calcium binding. S100A13 is essential for the copper-dependent stress-induced export of IL1A and FGF1. Interestingly, the calcium-free form of the protein can bind to lipid vesicles containing phosphatidylserine but not those containing phosphatidylcholine. S100A13 functions as a homodimer and is part of a copper-dependent multiprotein complex alongside FGF1 and SYT1. It also interacts with FGF1, SYT1, and IL1A.

Species

Mouse

Source

E. coli

Tag

N-His

Accession

P97352 (M1-K98)

Gene ID

20196  [NCBI]

Molecular Construction
N-term
His
S100A13 (M1-K98)
Accession # P97352
C-term
Synonyms
Protein S100-A13; S100A13; S100 calcium-binding protein A13
Molecular Weight

Approximately 15 kDa

Purity

Greater than 95% as determined by reducing SDS-PAGE

Appearance

Solution

Formulation

Supplied as a 0.2 μm filtered solution of PBS, 10% Glycerol, pH 7.4.

Endotoxin Level

<1 EU/μg, determined by LAL method.

Reconstitution

N/A.

Storage & Stability

Stored at -80°C for 1 year. It is stable at -20°C for 3 months after opening. It is recommended to freeze aliquots at -80°C for extended storage. Avoid repeated freeze-thaw cycles.

Shipping

Shipping with dry ice.

Documentation

S100A13 Protein, Mouse (His) Related Classifications

Help & FAQs
  • Do most proteins show cross-species activity?

    Species cross-reactivity must be investigated individually for each product. Many human cytokines will produce a nice response in mouse cell lines, and many mouse proteins will show activity on human cells. Other proteins may have a lower specific activity when used in the opposite species.

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The reconstitution calculator equation

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration

Volume (to add to vial) = Mass (in vial) ÷ Desired Reconstitution Concentration
= ÷

The dilution calculator equation

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)

This equation is commonly abbreviated as: C1V1 = C2V2

Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
× = ×
C1   V1   C2   V2

The specific activity calculator equation

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)

Specific Activity (Unit/mg) = 106 ÷ Biological Activity (ED50)
Unit/mg = 106 ÷ ng/mL

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S100A13 Protein, Mouse (His)
Cat. No.:
HY-P76583
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