Alternative Name(s):

ssb; ssb-1; BA_5722; GBAA_5722; BAS5326Single-stranded DNA-binding protein; SSB

Species: (Organism)

Bacillus anthracis

Gene Names:

ssb

Tag info:

N-terminal 6xHis-SUMO-tagged

Target Protein AA Sequence:

MNRVILVGRLTKDPDLRYTPNGVAVATFTLAVNRAFANQQGEREADFINCVIWRKQAENVANYLKKGSLAGVDGRLQTRNYEGQDGKRVYVTEVLAESVQFLEPRNGGGEQRGSFNQQPSGAGFGNQSSNPFGQSSNSGNQGNQGNSGFTKNDDPFSNVGQPIDISDDDLPF

Expression Region:

1-172aa

Subcellular Location:

Tissue Specificity:

Protein Length:

Full Length

Pathway:

Mol. Weight:

34.7 kDa

Purity:

Greater than 90% as determined by SDS-PAGE.

Form:

Liquid or Lyophilized powder

Buffer:

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.

Research Areas:

Others

Function:

Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit them to their sites of action during DNA metabolism.

Involvement in disease:

Relevance:

Plays an important role in DNA replication, recombination and repair. Binds to ssDNA and to an array of partner proteins to recruit th to their sites of action during DNA metabolism.

Reconstitution:

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Families:

Reference:

The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria.Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.Nature 423:81-86(2003)