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SRP3157

Sigma-Aldrich

Sox2 human

recombinant, expressed in E. coli, ≥95% (SDS-PAGE), ≥95% (HPLC), suitable for cell culture

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in E. coli

Assay

≥95% (HPLC)
≥95% (SDS-PAGE)

form

lyophilized

mol wt

34.3 kDa

packaging

pkg of 25 μg

technique(s)

cell culture | mammalian: suitable

impurities

<0.1 EU/μg endotoxin, tested

color

white

UniProt accession no.

P48431

shipped in

wet ice

storage temp.

−20°C

Gene Information

human ... SOX2(6657)

General description

Sox2 (sex determining region Y (SRY)-box 2) is one of the 20 human SOX transcription factors, which are characterized by the highly conserved ∼80-residues DNA-binding HMG (high-mobility group) domain. This domain was initially identified in the testis-determining factor Sry.
Recombinant human Sox2 is a 34.3 kDa protein containing 317 amino-acid residues.

Biochem/physiol Actions

Sox2 (sex determining region Y (SRY)-box 2) transcription factor participates in maintaining self-renewal and pluripotency of embryonic stem cells. The expression of this protein is aberrant in various human malignancies, and it acts as an oncogene in esophageal squamous cell carcinoma (SCC). SOX2 promotes proilferation, migration and adhesion abilities of dental pulp stem cells (DPSCs), and this might have applications in tissue engineering. It participates in Ewing′s sarcoma cell proliferation, and its inactivation results in apoptosis and G1/S arrest, in a PI3K (phosphoinositide 3-kinase)/Akt pathway-mediated manner.

Sequence

MYNMMETELK PPGPQQTSGG GGGNSTAAAA GGNQKNSPDR VKRPMNAFMV WSRGQRRKMA QENPKMHNSE ISKRLGAEWK LLSETEKRPF IDEAKRLRAL HMKEHPDYKY RPRRKTKTLM KKDKYTLPGG LLAPGGNSMA SGVGVGAGLG AGVNQRMDSY AHMNGWSNGS YSMMQDQLGY PQHPGLNAHG AAQMQPMHRY DVSALQYNSM TSSQTYMNGS PTYSMSYSQQ GTPGMALGSM GSVVKSEASS SPPVVTSSSH SRAPCQAGDL RDMISMYLPG AEVPEPAAPS RLHMSQHYQS GPVPGTAING TLPLSHM

Physical form

Lyophilized from 10 mM Sodium Acetate, pH 6.0.

Reconstitution

Centrifuge the vial prior to opening. Reconstitute in water to a concentration of 0.1- 1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

SRP3157-25UG:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Inhibition of SOX2 induces cell apoptosis and G1/S arrest in Ewing's sarcoma through the PI3K/Akt pathway.
Ren C et al
Journal of Experimental & Clinical Cancer Research, 35, 44-44 (2016)
Effects of SOX2 on Proliferation, Migration and Adhesion of Human Dental Pulp Stem Cells.
Liu P et al
PLoS ONE, 10(10), e0141346-e0141346 (2015)
High sex determining region Y-box 2 (SOX2) expression correlates with absence of nodal metastasis in esophageal squamous cell carcinoma.
Chuang WY et al
International Journal of Clinical and Experimental Pathology, 8(8), 9248-9255 (2015)
Samudyata et al.
Experimental cell research, 381(1), 129-138 (2019-05-12)
Sox2 is a master transcriptional regulator of embryonic development. In this study, we determined the protein interactome of Sox2 in the chromatin and nucleoplasm of mouse embryonic stem (mES) cells. Apart from canonical interactions with pluripotency-regulating transcription factors, we identified
The crystal structure of the Sox4 HMG domain-DNA complex suggests a mechanism for positional interdependence in DNA recognition.
Jauch R et al
The Biochemical Journal, 443(1), 39-47 (2012)
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