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HMGB3 Protein, Human, Recombinant (His)

TargetMol | SPR
Catalog No. TMPJ-00668 Copy Product Info
High Mobility Group Protein B3 (HMGB3) belongs to the HMGB family. Members of the HMG box subfamily are thought to be have an important role in DNA replication, nucleosome assembly and transcription. HMGB3 binds preferentiallly single-stranded DNA and unwinds double stranded DNA. HMGB3 consists of 200 amino acids and is localized to the cell nucleus. It contains two HMG box DNA-binding domain. HMGB3 binds preferentially single-stranded DNA and unwinds double stranded DNA.

HMGB3 Protein, Human, Recombinant (His)

Catalog No. TMPJ-00668
Copy Product Info
TargetMol | SPR

High Mobility Group Protein B3 (HMGB3) belongs to the HMGB family. Members of the HMG box subfamily are thought to be have an important role in DNA replication, nucleosome assembly and transcription. HMGB3 binds preferentiallly single-stranded DNA and unwinds double stranded DNA. HMGB3 consists of 200 amino acids and is localized to the cell nucleus. It contains two HMG box DNA-binding domain. HMGB3 binds preferentially single-stranded DNA and unwinds double stranded DNA.

HMGB3 Protein, Human, Recombinant (His)
Pack SizePriceUSA StockGlobal StockQuantity
5 μg$807-10 days7-10 days
10 μg$1297-10 days7-10 days
20 μg$1987-10 days7-10 days
50 μg$3907-10 days7-10 days
100 μg$6267-10 days7-10 days
200 μg$9877-10 days7-10 days
500 μg$1,9007-10 days7-10 days
1 mg$2,7307-10 days7-10 days
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For In stock only · Estimated delivery:USA Stock (1-2 days) Global Stock (5-7 days)
For research use only—not for human use. No sales to individuals. Use as intended only.
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Product Information

Biological Activity
Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description
High Mobility Group Protein B3 (HMGB3) belongs to the HMGB family. Members of the HMG box subfamily are thought to be have an important role in DNA replication, nucleosome assembly and transcription. HMGB3 binds preferentiallly single-stranded DNA and unwinds double stranded DNA. HMGB3 consists of 200 amino acids and is localized to the cell nucleus. It contains two HMG box DNA-binding domain. HMGB3 binds preferentially single-stranded DNA and unwinds double stranded DNA.
Species
Human
Expression System
HEK293 Cells
TagC-6xHis
Accession NumberO15347
Synonyms
HMGB3,HMG-4,HMG4,HMG-2a,HMG2A,High Mobility Group Protein B3,High Mobility Group Protein 4,High Mobility Group Protein 2a
Amino Acid
Met1-Glu200
Construction
Met1-Glu200
Protein Purity
Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Molecular Weight26 KDa (reducing condition)
Endotoxin< 0.1 ng/µg (1 EU/µg) as determined by LAL test.
FormulationLyophilized from a solution filtered through a 0.22 μm filter, containing PBS, pH 7.4.
Reconstitution
Reconstitute the lyophilized protein in distilled water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.
Stability & Storage
Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
ShippingIn general, lyophilized powders are shipped with blue ice, while solutions are shipped with dry ice.
Research Background
High Mobility Group Protein B3 (HMGB3) belongs to the HMGB family. Members of the HMG box subfamily are thought to be have an important role in DNA replication, nucleosome assembly and transcription. HMGB3 binds preferentiallly single-stranded DNA and unwinds double stranded DNA. HMGB3 consists of 200 amino acids and is localized to the cell nucleus. It contains two HMG box DNA-binding domain. HMGB3 binds preferentially single-stranded DNA and unwinds double stranded DNA.

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